A practical reference on prothymosin alpha: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
Reviewed 2026-07-03. Anything still debated is marked as such rather than presented as settled.
Clinical research has examined the peptide in chronic hepatitis B and C, as a vaccine adjuvant, and in sepsis and oncology settings. Results across trials have been mixed, and several studies were small or conducted under differing protocols. Regulatory status varies by country, and the compound is not approved in every jurisdiction where it is studied. Evidence for any single indication should be read with attention to sample size and endpoint choice.
Thymosin alpha-1 is a 28-residue peptide first isolated from thymus tissue in the 1970s. It corresponds to the N-terminal portion of thymosin beta-4, from which it is cleaved in vivo. The peptide carries an acetyl group at its N-terminus, a modification that affects its charge and stability. Synthetic material produced by solid-phase peptide synthesis is chemically identical to the natural fragment and is the form used in research and clinical studies.
Laboratory work indicates that the peptide acts on cells of both the innate and adaptive immune systems. Reported effects include signalling through Toll-like receptors on dendritic cells, enhanced T-cell maturation, and increased natural killer cell activity. These actions are described largely from cell-culture and animal experiments, and the precise receptor-level events remain incompletely defined. Studies in humans have generally measured immune markers rather than a single defined molecular target. The resulting picture remains partly descriptive.
市售的胸腺素α1通常以冻干粉形式提供，溶解后用于注射。其氨基酸组成包括多个酸性残基，因此在中性pH下带负电荷。该肽可溶于水和生理盐水，但在有机溶剂中溶解度有限。储存条件通常为冻干状态下负20摄氏度，溶解后需冷藏并避免反复冻融。常见的同义词包括胸腺肽α1、thymalfasin和Tα1。
胸腺素α1（thymosin alpha 1，Tα1）是一种由28个氨基酸组成的酸性肽，N端被乙酰化，分子量约为3108道尔顿。该肽最早从牛胸腺组织提取物中分离，属于胸腺素组分5的一个成分。其序列在不同哺乳动物中高度保守，提示其具有基本的生物学功能。名称中的“α1”指其在电泳中的迁移位置，并非表示亚型编号。它既存在于胸腺，也存在于脾脏和淋巴结等免疫组织。
20世纪70年代，研究者从胸腺提取物中纯化出多种小肽，Tα1是其中被较早表征的一种。最初的制备依赖组织匀浆和层析步骤，产量低且成分复杂。随着固相肽合成技术成熟，实验室和工业界能够生产与天然序列一致的合成版本。合成肽的纯度可达95%以上，并可通过反相高效液相色谱和质谱进行鉴定。这一转变使研究不再依赖动物胸腺来源。
| Property | Value | Notes |
|---|---|---|
| Chemical class | Peptide | 28 amino acid residues |
| Molecular weight | Approximately 3108 Da | Depends on acetylation state |
| N-terminal modification | Acetylated | Affects charge and stability |
| Natural source | Fragment of thymosin beta-4 | Cleaved in vivo |
| Sequence length | 28 residues | Synthetic form matches natural |
Biologically, the peptide is studied mainly in the context of immune cell development and regulation. It is produced in the thymus and in several other tissues, and it appears to influence the maturation and activity of T cells and other immune populations. Laboratory work describes effects on cytokine production, on the balance between T cell subsets, and on the function of dendritic cells. Much of this evidence comes from cell culture and animal models, so the extent to which the same pathways operate in humans remains an open question.
Clinical interest has centered on chronic viral hepatitis, on immune restoration in various conditions, and on use as an adjuvant intended to improve responses to vaccines. Trials have reported mixed results, and regulatory status differs sharply between countries; in some places it is a prescription product, while elsewhere it is sold without an approved therapeutic indication. Because published studies vary widely in design, population, and endpoints, comparisons across them are difficult and no single conclusion covers the whole literature.
Thymosin alpha 1 is a short peptide of 28 amino acid residues that derives from the amino terminal region of a larger precursor protein known as prothymosin alpha. The peptide carries an acetyl group on its first residue and contains no disulfide bonds or carbohydrate chains. Its sequence is highly conserved across mammalian species, which is one reason laboratories treat it as a molecule with a defined and reproducible structure rather than a variable tissue extract. The name follows an early naming convention for thymus-derived fractions and does not imply that the peptide acts as a hormone in the classical endocrine sense.
Thymosin alpha-1 is a synthetic 28-amino-acid peptide whose sequence was first identified in extracts of bovine thymus tissue during the 1970s. The chain carries an acetyl group on its N-terminal serine. Its acidic residue content is high, which produces strong water solubility and an isoelectric point well below neutrality. Material supplied for laboratory and clinical use is manufactured by solid-phase peptide synthesis rather than purified from animal tissue. Different salt forms, such as the acetate, alter the counter-ion content without changing the peptide backbone.
Whether the free 28-residue peptide circulates in human tissue remains debated. The best-documented human source is prothymosin alpha, a larger acidic protein that carries the sequence at its N-terminus. Reports of measurable peptide levels in serum and lymphoid tissue exist, yet some of that signal may come from cross-reacting fragments or from the parent protein. Most reviews therefore treat prothymosin alpha as the established human molecule and describe independent circulation of the small peptide as an unresolved question.
Thymosin alpha 1 is a synthetic 28-amino-acid peptide first isolated in 1966 from thymosin fraction 5, a bovine thymus extract. Its chain begins with an acetylated serine residue and ends with asparagine. The native peptide carries a molecular mass near 3,108 daltons. Researchers classify it as an immunomodulatory agent rather than a hormone with a single endocrine target. Early work framed it as a thymus-derived factor that supports T-cell maturation. The synthetic form used in research and clinical products matches the natural sequence.
Immune signaling studies link thymosin alpha 1 to Toll-like receptor pathways, particularly TLR2 and TLR9, on dendritic cells and other antigen-presenting cells. Activation of these receptors promotes maturation of T cells and increases natural killer cell activity. The peptide shifts cytokine output toward a T helper 1 profile, raising interferon gamma and interleukin 2 while modulating interleukin 10. Whether these effects translate into clinical benefit for any specific disease remains a subject of debate. Reported outcomes vary across trials and populations.
Thymosin alpha 1 is approved as a medicine in several countries, including Italy and China, for indications such as chronic hepatitis B and as an immune adjuvant. It is not approved by the United States Food and Drug Administration as a therapeutic product. In research settings the peptide appears in studies of sepsis, vaccine response, and oncology support, often with mixed or inconclusive results. The evidence base is uneven, and reviews note that many trials were small. Regulatory status therefore differs widely between jurisdictions.
Within the immune system, the peptide acts on several cell types rather than a single target. Reported activities include promotion of T-cell maturation, enhancement of natural killer cell activity, and modulation of cytokine production by dendritic cells and macrophages. Some of these effects appear to operate through toll-like receptor signaling, though the precise receptor-level mechanism remains debated. Whether the observed immune changes translate into clinical benefit is a separate question and depends on the indication studied.
The peptide was described in the 1970s as a component of thymic extracts, and early research focused on restoring immune function in immunodeficiency states. A synthetic version entered clinical development in the 1980s and is approved as a drug in several countries for conditions such as chronic hepatitis B and certain immunodeficiencies. Approval status varies widely by jurisdiction, and in the United States it is not an approved therapeutic. Regulatory and clinical positions differ, so statements about efficacy should be tied to specific indications and studies.
Paraneoplastic pemphigus (PNP) is an autoimmune disorder stemming from an underlying tumor. It is hypothesized that antigens associated with the tumor trigger an immune response resulting in blistering of the skin and mucous membranes. While patients with malignant and benign tumors are both at risk, malignancy is associated with high mortality rates (near 90%). Current treatment focuses on general wound healing and administering corticosteroids, which has not demonstrated a high success rate. Recent research developments aim to treat the underlying tumor in order to alleviate the symptoms of PNP.
In animals, fatty acids are formed from carbohydrates predominantly in the liver, adipose tissue, and the mammary glands during lactation. Carbohydrates are converted into pyruvate by glycolysis as the first important step in the conversion of carbohydrates into fatty acids. Pyruvate is then decarboxylated to form acetyl-CoA in the mitochondrion. However, this acetyl CoA needs to be transported into cytosol where the synthesis of fatty acids occurs. This cannot occur directly. To obtain cytosolic acetyl-CoA, citrate (produced by the condensation of acetyl-CoA with oxaloacetate) is removed from the citric acid cycle and carried across the inner mitochondrial membrane into the cytosol. There it is cleaved by ATP citrate lyase into acetyl-CoA and oxaloacetate. The oxaloacetate is returned to the mitochondrion as malate. The cytosolic acetyl-CoA is carboxylated by acetyl-CoA carboxylase into malonyl-CoA, the first committed step in the synthesis of fatty acids. Malonyl-CoA is then involved in a repeating series of reactions that lengthens the growing fatty acid chain by two carbons at a time. Almost all natural fatty acids, therefore, have even numbers of carbon atoms. When synthesis is complete the free fatty acids are nearly always combined with glycerol (three fatty acids to one glycerol molecule) to form triglycerides, the main storage form of fatty acids, and thus of energy in animals.
In its deuterated form (DMSO-d6), it is a useful solvent for NMR spectroscopy, again due to its ability to dissolve a wide range of analytes, the simplicity of its own spectrum, and its suitability for high-temperature NMR spectroscopic studies. Disadvantages to the use of DMSO-d6 are its high viscosity, which broadens signals, and its hygroscopicity, which leads to an overwhelming H2O resonance in the 1H-NMR spectrum. It can be mixed with CDCl3 or CD2Cl2 for lower viscosity and melting points.
=== EC 2.4.1: Hexosyltransferases === EC 2.4.1.1: Glycogen phosphorylase EC 2.4.1.2: dextrin dextranase EC 2.4.1.3: deleted, included in EC 2.4.1.25 EC 2.4.1.4: amylosucrase EC 2.4.1.5: dextransucrase EC 2.4.1.6: deleted EC 2.4.1.7: sucrose phosphorylase EC 2.4.1.8: maltose phosphorylase EC 2.4.1.9: inulosucrase EC 2.4.1.10: levansucrase EC 2.4.1.11: glycogen(starch) synthase EC 2.4.1.12: cellulose synthase (UDP-forming) EC 2.4.1.13: sucrose synthase EC 2.4.1.14: sucrose-phosphate synthase EC 2.4.1.15: α,α-trehalose-phosphate synthase (UDP-forming) EC 2.4.1.16: chitin synthase EC 2.4.1.17: glucuronosyltransferase EC 2.4.1.18: ,4-α-glucan branching enzyme EC 2.4.1.19: cyclomaltodextrin glucanotransferase EC 2.4.1.20: cellobiose phosphorylase EC 2.4.1.21: starch synthase EC 2.4.1.22: lactose synthase EC 2.4.1.23: sphingosine β-galactosyltransferase EC 2.4.1.24: 1,4-α-glucan 6-α-glucosyltransferase EC 2.4.1.25: 4-α-glucanotransferase EC 2.4.1.26: DNA α-glucosyltransferase EC 2.4.1.27: DNA β-glucosyltransferase EC 2.4.1.28: glucosyl-DNA β-glucosyltransferase EC 2.4.1.29: cellulose synthase (GDP-forming) EC 2.4.1.30: 1,3-β-oligoglucan phosphorylase EC 2.4.1.31: laminaribiose phosphorylase EC 2.4.1.32: glucomannan 4-β-mannosyltransferase EC 2.4.1.33: mannuronan synthase EC 2.4.1.34: 1,3-β-glucan synthase EC 2.4.1.35: phenol β-glucosyltransferase EC 2.4.1.36: α,α-trehalose-phosphate synthase (GDP-forming) EC 2.4.1.37: fucosylgalactoside 3-α-galactosyltransferase EC 2.4.1.38: β-N-acetylglucosaminylglycopeptide β-1,4-galactosyltransferase EC 2.4.1.39: steroid N-acetylglucosaminyltransferase EC 2.4.1.40: glycoprotein-fucosylgalactoside α-N-acetylgalactosaminyltransferase EC 2.4.1.41: polypeptide N-acetylgalactosaminyltransferase EC 2.4.1.42: deleted, included in EC 2.4.1.17 EC 2.4.1.43: polygalacturonate 4-α-galacturonosyltransferase EC 2.4.1.44: lipopolysaccharide 3-α-galactosyltransferase EC 2.4.1.45: now included with EC 2.4.1.47, N-acylsphingosine galactosyltransferase EC 2.4.1.46: monogalactosyldiacylglycerol synthase EC 2.4.1.47: N-acylsphingosine galactosyltransferase EC 2.4.1.48: heteroglycan α-mannosyltransferase EC 2.4.1.49: cellodextrin phosphorylase EC 2.4.1.50: procollagen galactosyltransferase EC 2.4.1.51: now covered by EC 2.4.1.101, EC 2.4.1.143, EC 2.4.1.144 and EC 2.4.1.145 EC 2.4.1.52: poly(glycerol-phosphate) α-glucosyltransferase EC 2.4.1.53: poly(ribitol-phosphate) β-glucosyltransferase EC 2.4.1.54: undecaprenyl-phosphate mannosyltransferase EC 2.4.1.55: Now EC 2.7.8.14, CDP-ribitol ribitolphosphotransferase EC 2.4.1.56: lipopolysaccharide N-acetylglucosaminyltransferase EC 2.4.1.57: Newer studies have shown that this is catalysed by two independent activities now covered by EC 2.4.1.345, phosphatidyl-myo-inositol α-mannosyl transferase and EC 2.4.1.346, phosphatidyl-myo-inositol dimannoside synthase EC 2.4.1.58: lipopolysaccharide glucosyltransferase I EC 2.4.1.59: deleted, included in EC 2.4.1.17 EC 2.4.1.60: CDP-abequose:α-D-Man-(1→4)-α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase EC 2.4.1.61: deleted, included in EC 2.4.1.17 EC 2.4.1.62: ganglioside galactosyltransferase EC 2.4.1.63: linamarin synthase EC 2.4.1.64: α,α-trehalose phosphorylase EC 2.4.1.65: 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase EC 2.4.1.66: procollagen glucosyltransferase EC 2.4.1.67: galactinol—raffinose galactosyltransferase EC 2.4.1.68: glycoprotein 6-α-L-fucosyltransferase EC 2.4.1.69: type 1 galactoside α-(1,2)-fucosyltransferase EC 2.4.1.70: poly(ribitol-phosphate) α-N-acetylglucosaminyltransferase EC 2.4.1.71: arylamine glucosyltransferase EC 2.4.1.72: now EC 2.4.2.24, 1,4-β-D-xylan synthase EC 2.4.1.73: lipopolysaccharide glucosyltransferase II EC 2.4.1.74: glycosaminoglycan galactosyltransferase EC 2.4.1.75: deleted entry, insufficient evidence to conclude that this is a different enzyme from EC 2.4.1.43 EC 2.4.1.76: deleted, included in EC 2.4.1.17 EC 2.4.1.77: deleted, included in EC 2.4.1.17 EC 2.4.1.78: phosphopolyprenol glucosyltransferase EC 2.4.1.79: globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase EC 2.4.1.80: ceramide glucosyltransferase EC 2.4.1.81: flavone 7-O-β-glucosyltransferase EC 2.4.1.82: galactinol—sucrose galactosyltransferase EC 2.4.1.83: dolichyl-phosphate β-D -mannosyltransferase EC 2.4.1.84: deleted, included in EC 2.4.1.17 EC 2.4.1.85: cyanohydrin β-glucosyltransferase EC 2.4.1.86: N-acetyl-β-D-glucosaminide β-(1,3)-galactosyltransferase EC 2.4.1.87: N-acetyllactosaminide 3-α-galactosyltransferase EC 2.4.1.88: globoside α-N-acetylgalactosaminyltransferase EC 2.4.1.89: deleted, included in EC 2.4.1.69, type 1 galactoside α-(1,2)-fucosyltransferase EC 2.4.1.90: N-acetyllactosamine synthase EC 2.4.1.91: flavonol 3-O-glucosyltransferase EC 2.4.1.92: (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase EC 2.4.1.93: Now EC 4.2.2.18, inulin fructotransferase (DFA-III-forming) EC 2.4.1.94: protein N-acetylglucosaminyltransferase EC 2.4.1.95: deleted EC 2.4.1.96: sn-glycerol-3-phosphate 1-galactosyltransferase EC 2.4.1.97: 1,3-β-D-glucan phosphorylase EC 2.4.1.98: deleted, Now included with EC 2.4.1.90, N-acetyllactosamine synthase EC 2.4.1.99: sucrose:sucrose fructosyltransferase EC 2.4.1.100: 2,1-fructan:2,1-fructan 1-fructosyltransferase EC 2.4.1.101: α-1,3-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase EC 2.4.1.102: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase EC 2.4.1.103: alizarin 2-β-glucosyltransferase EC 2.4.1.104: o-dihydroxycoumarin 7-O-glucosyltransferase EC 2.4.1.105: vitexin β-glucosyltransferase EC 2.4.1.106: isovitexin β-glucosyltransferase EC 2.4.1.107: deleted, now included with EC 2.4.1.17, glucuronosyltransferase EC 2.4.1.108: deleted, now included with EC 2.4.1.17, glucuronosyltransferase EC 2.4.1.109: dolichyl-phosphate-mannose—protein mannosyltransferase EC 2.4.1.110: tRNA-queuosine β-mannosyltransferase EC 2.4.1.111: coniferyl-alcohol glucosyltransferase EC 2.4.1.112: The protein referred to in this entry is now known to be glycogenin so the entry has been incorporated into EC 2.4.1.186, glycogenin glucosyltransferase EC 2.4.1.113: α-1,4-glucan-protein synthase (ADP-forming) EC 2.4.1.114: 2-coumarate O-β-glucosyltransferase EC 2.4.1.115: anthocyanidin 3-O-glucosyltransferase EC 2.4.1.116: cyanidin 3-O-rutinoside 5-O-glucosyltransferase EC 2.4.1.117: dolichyl-phosphate β-glucosyltransferase EC 2.4.1.118: cytokinin 7-β-glucosyltransferase EC 2.4.1.119: transferred to EC 2.4.99.18, dolichyl-diphosphooligosaccharideprotein glycotransferase EC 2.4.1.120: sinapate 1-glucosyltransferase EC 2.4.1.121: indole-3-acetate β-glucosyltransferase EC 2.4.1.122: N-acetylgalactosaminide β-1,3-galactosyltransferase EC 2.4.1.123: inositol 3-α-galactosyltransferase EC 2.4.1.124: Now EC 2.4.1.87, N-acetyllactosaminide 3-α-galactosyltransferase EC 2.4.1.125: sucrose—1,6-α-glucan 3(6)-α-glucosyltransferase EC 2.4.1.126: hydroxycinnamate 4-β-glucosyltransferase EC 2.4.1.127: monoterpenol β-glucosyltransferase EC 2.4.1.128: scopoletin glucosyltransferase EC 2.4.1.129: peptidoglycan glycosyltransferase EC 2.4.1.130: Now covered by EC 2.4.1.258, EC 2.4.1.259, EC 2.4.1.260 and EC 2.4.1.261 EC 2.4.1.131: GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase EC 2.4.1.132: GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase EC 2.4.1.133: xylosylprotein 4-β-galactosyltransferase EC 2.4.1.134: galactosylxylosylprotein 3-β-galactosyltransferase EC 2.4.1.135: galactosylgalactosylxylosylprotein 3-β-glucuronosyltransferase EC 2.4.1.136: gallate 1-β-glucosyltransferase EC 2.4.1.137: sn-glycerol-3-phosphate 2-α-galactosyltransferase EC 2.4.1.138: mannotetraose 2-α-N-acetylglucosaminyltransferase EC 2.4.1.139: maltose synthase EC 2.4.1.140: alternansucrase EC 2.4.1.141: N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase EC 2.4.1.142: chitobiosyldiphosphodolichol β-mannosyltransferase EC 2.4.1.143: α-1,6-mannosyl-glycoprotein 2-β-N-acetylglucosaminyltransferase EC 2.4.1.144: β-1,4-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase EC 2.4.1.145: α-1,3-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase EC 2.4.1.146: β-1,3-galactosyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase EC 2.4.1.147: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,3-N-acetylglucosaminyltransferase EC 2.4.1.148: acetylgalactosaminyl-O-glycosyl-glycoprotein β-1,6-N-acetylglucosaminyltransferase EC 2.4.1.149: N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase EC 2.4.1.150: N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase EC 2.4.1.151: now included with EC 2.4.1.87 N-acetyllactosaminide 3-α-galactosyltransferase EC 2.4.1.152: 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase EC 2.4.1.153: UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminyltransferase EC 2.4.1.154: identical to EC 2.4.1.79, globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase EC 2.4.1.155: α-1,6-mannosyl-glycoprotein 6-β-N-acetylglucosaminyltransferase EC 2.4.1.156: indolylacetyl-myo-inositol galactosyltransferase EC 2.4.1.157: 1,2-diacylglycerol 3-glucosyltransferase, now classified as EC 2.4.1.336, monoglucosyldiacylglycerol synthase, and EC 2.4.1.337, 1,2-diacylglycerol 3-α-glucosyltransferase EC 2.4.1.158: 13-hydroxydocosanoate 13-β-glucosyltransferase EC 2.4.1.159: flavonol-3-O-glucoside L-rhamnosyltransferase EC 2.4.1.160: pyridoxine 5′-O-β-D-glucosyltransferase EC 2.4.1.161: oligosaccharide 4-α-D-glucosyltransferase EC 2.4.1.162: aldose β-D-fructosyltransferase EC 2.4.1.163: now included in EC 2.4.1.149, N-acetyllactosaminide β-1,3-N-acetylglucosaminyltransferase EC 2.4.1.164: now included with EC 2.4.1.150, N-acetyllactosaminide β-1,6-N-acetylglucosaminyltransferase EC 2.4.1.165: N-acetylneuraminylgalactosylglucosylceramide β-1,4-N-acetylgalactosaminyltransferase EC 2.4.1.166: raffinose—raffinose α-galactosyltransferase EC 2.4.1.167: sucrose 6F-α-galactosyltransferase EC 2.4.1.168: xyloglucan 4-glucosyltransferase EC 2.4.1.169: now EC 2.4.2.39, xyloglucan 6-xylosyltransferase EC 2.4.1.170: isoflavone 7-O-glucosyltransferase EC 2.4.1.171: methyl-ONN-azoxymethanol β-D-glucosyltransferase EC 2.4.1.172: salicyl-alcohol β-D-glucosyltransferase EC 2.4.1.173: sterol 3β-glucosyltransferase EC 2.4.1.174: glucuronylgalactosylproteoglycan 4-β-N-acetylgalactosaminyltransferase EC 2.4.1.175: glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-β-N-acetylgalactosaminyltransferase EC 2.4.1.176: gibberellin β-D-glucosyltransferase EC 2.4.1.177: cinnamate β-D-glucosyltransferase EC 2.4.1.178: hydroxymandelonitrile glucosyltransferase EC 2.4.1.179: lactosylceramide β-1,3-galactosyltransferase EC 2.4.1.180: lipopolysaccharide N-acetylmannosaminouronosyltransferase EC 2.4.1.181: hydroxyanthraquinone glucosyltransferase EC 2.4.1.182: lipid-A-disaccharide synthase EC 2.4.1.183: α-1,3-glucan synthase EC 2.4.1.184: galactolipid galactosyltransferase EC 2.4.1.185: flavanone 7-O-β-glucosyltransferase EC 2.4.1.186: glycogenin glucosyltransferase EC 2.4.1.187: N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-β-D-mannosaminyltransferase EC 2.4.1.188: N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase EC 2.4.1.189: uteolin 7-O-glucuronosyltransferase EC 2.4.1.190: luteolin-7-O-glucuronide 2′′-O-glucuronosyltransferase EC 2.4.1.191: luteolin-7-O-diglucuronide 4′-O-glucuronosyltransferase EC 2.4.1.192: nuatigenin 3β-glucosyltransferase EC 2.4.1.193: sarsapogenin 3β-glucosyltransferase EC 2.4.1.194: 4-hydroxybenzoate 4-O-β-D-glucosyltransferase EC 2.4.1.195: N-hydroxythioamide S-β-glucosyltransferase EC 2.4.1.196: nicotinate glucosyltransferase EC 2.4.1.197: high-mannose-oligosaccharide β-1,4-N-acetylglucosaminyltransferase EC 2.4.1.198: phosphatidylinositol N-acetylglucosaminyltransferase EC 2.4.1.199: β-mannosylphosphodecaprenol—mannooligosaccharide 6-mannosyltransferase EC 2.4.1.200: now EC 4.2.2.17, inulin fructotransferase (DFA-I-forming) EC 2.4.1.201: α-1,6-mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase EC 2.4.1.202: 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase EC 2.4.1.203: trans-zeatin O-β-D-glucosyltransferase EC 2.4.1.204: now EC 2.4.2.40, zeatin O-β-D-xylosyltransferase EC 2.4.1.205: galactogen 6β-galactosyltransferase EC 2.4.1.206: lactosylceramide 1,3-N-acetyl-β-D-glucosaminyltransferase EC 2.4.1.207: xyloglucan:xyloglucosyl transferase EC 2.4.1.208: diglucosyl diacylglycerol synthase (1,2-linking) EC 2.4.1.209: cis-p-coumarate glucosyltransferase EC 2.4.1.210: limonoid glucosyltransferase EC 2.4.1.211: 1,3-β-galactosyl-N-acetylhexosamine phosphorylase EC 2.4.1.212: hyaluronan synthase EC 2.4.1.213: glucosylglycerol-phosphate synthase EC 2.4.1.214: glycoprotein 3-α-L-fucosyltransferase EC 2.4.1.215: cis-zeatin O-β-D-glucosyltransferase EC 2.4.1.216: trehalose 6-phosphate phosphorylase EC 2.4.1.217: mannosyl-3-phosphoglycerate synthase EC 2.4.1.218: hydroquinone glucosyltransferase EC 2.4.1.219: vomilenine glucosyltransferase EC 2.4.1.220: indoxyl-UDPG glucosyltransferase EC 2.4.1.221: peptide-O-fucosyltransferase EC 2.4.1.222: O-fucosylpeptide 3-β-N-acetylglucosaminyltransferase EC 2.4.1.223: glucuronosyl-galactosyl-proteoglycan 4-α-N-acetylglucosaminyltransferase EC 2.4.1.224: glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-α-N-acetylglucosaminyltransferase EC 2.4.1.225: N-acetylglucosaminyl-proteoglycan 4-β-glucuronosyltransferase EC 2.4.1.226: N-acetylgalactosaminyl-proteoglycan 3-β-glucuronosyltransferase EC 2.4.1.227: undecaprenyldiphospho-muramoylpentapeptide β-N-acetylglucosaminyltransferase EC 2.4.1.228: lactosylceramide 4-α-galactosyltransferase EC 2.4.1.229: [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase EC 2.4.1.230: kojibiose phosphorylase EC 2.4.1.231: α,α-trehalose phosphorylase (configuration-retaining) EC 2.4.1.232: initiation-specific α-1,6-mannosyltransferase EC 2.4.1.233: deleted: identical to EC 2.4.1.115, anthocyanidin 3-O-glucosyltransferase EC 2.4.1.234: kaempferol 3-O-galactosyltransferase EC 2.4.1.235: deleted: identical to EC 2.4.1.116, cyanidin 3-O-rutinoside 5-O-glucosyltransferase EC 2.4.1.236: flavanone 7-O-glucoside 2′′-O-β-L-rhamnosyltransferase EC 2.4.1.237: flavonol 7-O-β-glucosyltransferase EC 2.4.1.238: delphinidin 3,5-di-O-glucoside 3′-O-glucosyltransferase EC 2.4.1.239: flavonol-3-O-glucoside glucosyltransferase EC 2.4.1.240: flavonol-3-O-glycoside glucosyltransferase EC 2.4.1.241: flavonol-3-O-glycoside glucosyltransferase EC 2.4.1.242: NDP-glucose—starch glucosyltransferase EC 2.4.1.243: 6G-fructosyltransferase EC 2.4.1.244: N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase EC 2.4.1.245: α,α-trehalose synthase EC 2.4.1.246: mannosylfructose-phosphate synthase EC 2.4.1.247: β-D-galactosyl-(1→4)-L-rhamnose phosphorylase EC 2.4.1.248: cycloisomaltooligosaccharide glucanotransferase EC 2.4.1.249: delphinidin 3′,5′-O-glucosyltransferase EC 2.4.1.250: D-inositol-3-phosphate glycosyltransferase EC 2.4.1.251: GlcA-β-(1→2)-D-Man-α-(1→3)-D-Glc-β-(1→4)-D-Glc-α-1-diphospho-ditrans,octacis-undecaprenol 4-β-mannosyltransferase EC 2.4.1.252: GDP-mannose:cellobiosyl-diphosphopolyprenol α-mannosyltransferase EC 2.4.1.253: baicalein 7-O-glucuronosyltransferase EC 2.4.1.254: cyanidin-3-O-glucoside 2′′-O-glucuronosyltransferase EC 2.4.1.255: protein O-GlcNAc transferase EC 2.4.1.256: dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol α-1,2-glucosyltransferase EC 2.4.1.257: GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase EC 2.4.1.258: dolichyl-P-Man:Man5GlcNAc2-PP-dolichol α-1,3-mannosyltransferase EC 2.4.1.259: dolichyl-P-Man:Man6GlcNAc2-PP-dolichol α-1,2-mannosyltransferase EC 2.4.1.260: dolichyl-P-Man:Man7GlcNAc2-PP-dolichol α-1,6-mannosyltransferase EC 2.4.1.261: dolichyl-P-Man:Man8GlcNAc2-PP-dolichol α-1,2-mannosyltransferase EC 2.4.1.262: soyasapogenol glucuronosyltransferase EC 2.4.1.263: abscisate β-glucosyltransferase EC 2.4.1.264: D-Man-α-(1→3)-D-Glc-β-(1→4)-DD-Glc-α-1-diphosphoundecaprenol 2-β-glucuronosyltransferase EC 2.4.1.265: olichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase EC 2.4.1.266: glucosyl-3-phosphoglycerate synthase EC 2.4.1.267: dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol α-1,3-glucosyltransferase EC 2.4.1.268: glucosylglycerate synthase EC 2.4.1.269: mannosylglycerate synthase EC 2.4.1.270: mannosylglucosyl-3-phosphoglycerate synthase EC 2.4.1.271: crocetin glucosyltransferase EC 2.4.1.272: soyasapogenol B glucuronide galactosyltransferase EC 2.4.1.273: soyasaponin III rhamnosyltransferase EC 2.4.1.274: glucosylceramide β-1,4-galactosyltransferase EC 2.4.1.275: neolactotriaosylceramide β-1,4-galactosyltransferase EC 2.4.1.276: zeaxanthin glucosyltransferase EC 2.4.1.277: glycosyltransferase DesVII EC 2.4.1.278: desosaminyl transferase EryCIII EC 2.4.1.279: nigerose phosphorylase EC 2.4.1.280: N,N′-diacetylchitobiose phosphorylase EC 2.4.1.281: 4-O-β-D-mannosyl-D-glucose phosphorylase EC 2.4.1.282: 3-O-α-D-glucosyl-L-rhamnose phosphorylase EC 2.4.1.283: 2-deoxystreptamine N-acetyl-D-glucosaminyltransferase EC 2.4.1.284: 2-deoxystreptamine glucosyltransferase EC 2.4.1.285: UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase EC 2.4.1.286: chalcone 4′-O-glucosyltransferase EC 2.4.1.287: rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,4/1,5-galactofuranosyltransferase EC 2.4.1.288: galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol β-1,5/1,6-galactofuranosyltransferase EC 2.4.1.289: N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase EC 2.4.1.290: N,N′-diacetylbacillosaminyl-diphospho-undecaprenol α-1,3-N-acetylgalactosaminyltransferase EC 2.4.1.291: N-acetylgalactosamine-N,N′-diacetylbacillosaminyl-diphospho-undecaprenol 4-α-N-acetylgalactosaminyltransferase EC 2.4.1.292: GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase EC 2.4.1.293: GalNAc5-diNAcBac-PP-undecaprenol β-1,3-glucosyltransferase EC 2.4.1.294: cyanidin 3-O-galactosyltransferase EC 2.4.1.295: anthocyanin 3-O-sambubioside 5-O-glucosyltransferase EC 2.4.1.296: anthocyanidin 3-O-coumaroylrutinoside 5-O-glucosyltransferase EC 2.4.1.297: anthocyanidin 3-O-glucoside 2′′-O-glucosyltransferase EC 2.4.1.298: anthocyanidin 3-O-glucoside 5-O-glucosyltransferase EC 2.4.1.299: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose) EC 2.4.1.300: cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose) EC 2.4.1.301: 2′-deamino-2′-hydroxyneamine 1-α-D-kanosaminyltransferase EC 2.4.1.302: L-demethylnoviosyl transferase EC 2.4.1.303: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,3-galactosyltransferase EC 2.4.1.304: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol β-1,4-galactosyltransferase EC 2.4.1.305: UDP-Glc:α-D-GlcNAc-glucosaminyl-diphosphoundecaprenol β-1,3-glucosyltransferase EC 2.4.1.306: UDP-GalNAc:α-D-GalNAc-diphosphoundecaprenol α-1,3-N-acetylgalactosaminyltransferase EC 2.4.1.307: UDP-Gal:α-D-GalNAc-1,3-α-D-GalNAc-diphosphoundecaprenol β-1,3-galactosyltransferase. Now included in EC 2.4.1.122, N-acetylgalactosaminide β-1,3-galactosyltransferase EC 2.4.1.308: GDP-Fuc:β-D-Gal-1,3-α-D-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,2-fucosyltransferase EC 2.4.1.309: UDP-Gal:α-L-Fuc-1,2-β-Gal-1,3-α-GalNAc-1,3-α-GalNAc-diphosphoundecaprenol α-1,3-galactosyltransferase EC 2.4.1.310: vancomycin aglycone glucosyltransferase EC 2.4.1.311: chloroorienticin B synthase EC 2.4.1.312: protein O-mannose β-1,4-N-acetylglucosaminyltransferase EC 2.4.1.313: protein O-mannose β-1,3-N-acetylgalactosaminyltransferase EC 2.4.1.314: ginsenoside Rd glucosyltransferase EC 2.4.1.315: diglucosyl diacylglycerol synthase (1,6-linking) EC 2.4.1.316: tylactone mycaminosyltransferase EC 2.4.1.317: O-mycaminosyltylonolide 6-deoxyallosyltransferase EC 2.4.1.318: demethyllactenocin mycarosyltransferase EC 2.4.1.319: β-1,4-mannooligosaccharide phosphorylase EC 2.4.1.320: 1,4-β-mannosyl-N-acetylglucosamine phosphorylase EC 2.4.1.321: cellobionic acid phosphorylase EC 2.4.1.322: devancosaminyl-vancomycin vancosaminetransferase EC 2.4.1.323: 7-deoxyloganetic acid glucosyltransferase EC 2.4.1.324: 7-deoxyloganetin glucosyltransferase EC 2.4.1.325: TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase EC 2.4.1.326: aklavinone 7-L-rhodosaminyltransferase EC 2.4.1.327: aclacinomycin-T 2-deoxy-L-fucose transferase EC 2.4.1.328: erythronolide mycarosyltransferase EC 2.4.1.329: sucrose 6F-phosphate phosphorylase EC 2.4.1.330: β-D-glucosyl crocetin β-1,6-glucosyltransferase EC 2.4.1.331: 8-demethyltetracenomycin C L-rhamnosyltransferase EC 2.4.1.332: 1,2-α-glucosylglycerol phosphorylase EC 2.4.1.333: 1,2-β-oligoglucan phosphorylase EC 2.4.1.334: 1,3-α-oligoglucan phosphorylase EC 2.4.1.335: dolichyl N-acetyl-α-D-glucosaminyl phosphate 3-β-D-2,3-diacetamido-2,3-dideoxy-β-D-glucuronosyltransferase EC 2.4.1.336: monoglucosyldiacylglycerol synthase EC 2.4.1.337: 1,2-diacylglycerol 3-α-glucosyltransferase EC 2.4.1.338: validoxylamine A glucosyltransferase EC 2.4.1.339: β-1,2-mannobiose phosphorylase EC 2.4.1.340: 1,2-β-oligomannan phosphorylase EC 2.4.1.341: α-1,2-colitosyltransferase EC 2.4.1.342: α-maltose-1-phosphate synthase EC 2.4.1.343: UDP-Gal:α-D-GlcNAc-diphosphoundecaprenol α-1,3-galactosyltransferase EC 2.4.1.344: type 2 galactoside α-(1,2)-fucosyltransferase EC 2.4.1.345: phosphatidyl-myo-inositol α-mannosyltransferase EC 2.4.1.346: phosphatidyl-myo-inositol dimannoside synthase EC 2.4.1.347: α,α-trehalose-phosphate synthase (ADP-forming) EC 2.4.1.348: N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase EC 2.4.1.349: mannosyl-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol 3-α-mannosyltransferase EC 2.4.1.350: mogroside IE synthase EC 2.4.1.351: rhamnogalacturonan I rhamnosyltransferase EC 2.4.1.352: glucosylglycerate phosphorylase EC 2.4.1.353: sordaricin 6-deoxyaltrosyltransferase EC 2.4.1.354: (R)-mandelonitrile β-glucosyltransferase EC 2.4.1.355: poly(ribitol-phosphate) β-N-acetylglucosaminyltransferase EC 2.4.1.356: glucosyl-dolichyl phosphate glucuronosyltransferase EC 2.4.1.357: phlorizin synthase EC 2.4.1.358: acylphloroglucinol glucosyltransferase EC 2.4.1.359: glucosylglycerol phosphorylase (configuration-retaining) EC 2.4.1.360: 2-hydroxyflavanone C-glucosyltransferase EC 2.4.1.361: GDP-mannose:di-myo-inositol-1,3′-phosphate β-1,2-mannosyltransferase EC 2.4.1.362: α-(1→3) branching sucrase EC 2.4.1.363: ginsenoside 20-O-glucosyltransferase EC 2.4.1.364: protopanaxadiol-type ginsenoside 3-O-glucosyltransferase EC 2.4.1.365: protopanaxadiol-type ginsenoside-3-O-glucoside 2′′-O-glucosyltransferase EC 2.4.1.366: ginsenoside F1 6-O-glucosyltransferase EC 2.4.1.367: ginsenoside 6-O-glucosyltransferase EC 2.4.1.368: oleanolate 3-O-glucosyltransferase EC 2.4.1.369: enterobactin C-glucosyltransferase EC 2.4.1.370: inositol phosphorylceramide mannosyltransferase EC 2.4.1.371: polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 2,3-α-mannosylpolymerase EC 2.4.1.372: mutansucrase EC 2.4.1.373: α-(1→2) branching sucrase EC 2.4.1.374: β-1,2-mannooligosaccharide synthase EC 2.4.1.375: rhamnogalacturonan I galactosyltransferase EC 2.4.1.376: EGF-domain serine glucosyltransferase EC 2.4.1.377: dTDP-Rha:α-D-Gal-diphosphoundecaprenol α-1,3-rhamnosyltransferase EC 2.4.1.378: GDP-mannose:α-L-Rha-(1→3)-α-D-Gal-PP-Und α-1,4-mannosyltransferase EC 2.4.1.379: GDP-Man:α-D-Gal-diphosphoundecaprenol α-1,3-mannosyltransferase EC 2.4.1.380: GDP-Man:α-D-Man-(1→3)-α-D-Gal diphosphoundecaprenol α-1,2-mannosyltransferase EC 2.4.1.381: dTDP-Rha:α-D-Man-(1→3)-α-D-Gal diphosphoundecaprenol α-1,2-rhamnosyltransferase EC 2.4.1.382: CDP-abequose:α-L-Rha2OAc-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und α-1,3-abequosyltransferase EC 2.4.1.383: GDP-Man:α-L-Rha-(1→3)-α-D-Gal-PP-Und β-1,4-mannosyltransferase EC 2.4.1.384: NDP-glycosyltransferase
The LSI is a 235,000 square feet building with six floors, located between U-M's central campus and the university's medical campus in Ann Arbor. Completed in 2003, the building includes housing for wet lab and laboratory support spaces, administration offices, PI offices, interaction spaces, core laboratory areas, a combined gallery/lobby space and a small library. The exterior design of the building is intended to harmonize with other campus loft-style structures, while also meeting the needs of a modern research institute.
Sources: en.wikipedia.org
In an organic light-emitting diode (OLED), the electroluminescent material composing the emissive layer of the diode is an organic compound. The organic material is electrically conductive due to the delocalization of pi electrons caused by conjugation over all or part of the molecule, and the material therefore functions as an organic semiconductor. The organic materials can be small organic molecules in a crystalline phase, or polymers. The potential advantages of OLEDs include thin, low-cost displays with a low driving voltage, wide viewing angle, and high contrast and color gamut. Polymer LEDs have the added benefit of printable and flexible displays. OLEDs have been used to make visual displays for portable electronic devices such as cellphones, digital cameras, lighting and televisions.
=== Mammalian aminopeptidases === In mammals, aminopeptidases are produced in various tissues and organs, such as the liver, kidney, and intestine. Due to their ability to break down proteins and peptides, they are used in to help digest proteins, regulate peptide-mediated effects, and break down bioactive peptides. Aminopeptidase N (AP-N) is particularly abundant in the brush border membranes of the kidney, small intestine, and placenta, and is also rich in the liver. It has a broad substrate specificity (ability to bind to its targets) and is involved in the final stages of the digestion of peptides generated from breaking-up and hydrolysis of proteins by gastric and pancreatic proteases.
A trachea may be narrowed or compressed, usually a result of enlarged nearby lymph nodes; cancers of the trachea or nearby structures; large thyroid goitres; or rarely as a result of other processes such as unusually swollen blood vessels. Scarring from tracheobronchial injury or intubation; or inflammation associated with granulomatosis with polyangiitis may also cause a narrowing of the trachea (tracheal stenosis). Obstruction invariably causes a harsh breathing sound known as stridor. A camera inserted via the mouth down into the trachea, called bronchoscopy, may be performed to investigate the cause of an obstruction. Management of obstructions depends on the cause. Obstructions as a result of malignancy may be managed with surgery, chemotherapy or radiotherapy. A stent may be inserted over the obstruction. Benign lesions, such as narrowing resulting from scarring, are likely to be surgically excised. One cause of narrowing is tracheomalacia, which is the tendency for the trachea to collapse when there is increased external pressure, such as when airflow is increased during breathing in or out, due to decreased compliance. It can be due to congenital causes, or due to things that develop after birth, such as compression from nearby masses or swelling, or trauma. Congenital tracheomalacia can occur by itself or in association with other abnormalities such as bronchomalacia or laryngomalacia, and abnormal connections between the trachea and the oesophagus, amongst others.
== External links == MedlinePlus drug information - Aminoglycosides (Systemic) Science Daily Bacterial 'Battle for Survival' - Rhodostreptomycin Wikiversity page for the International Ototoxicity Management Group
Sources: en.wikipedia.org
The availability of small and relatively inexpensive nitrogen lasers operating at 337 nm wavelength and the first commercial instruments introduced in the early 1990s brought MALDI to an increasing number of researchers. Today, mostly organic matrices are used for MALDI mass spectrometry.
The lower case letter 'x' can be used as a pattern element to denote any amino acid. A string of characters drawn from the alphabet and enclosed in braces (curly brackets) denotes any amino acid except for those in the string. For example, {ST} denotes any amino acid other than S or T. If a pattern is restricted to the N-terminal of a sequence, the pattern is prefixed with '<'. If a pattern is restricted to the C-terminal of a sequence, the pattern is suffixed with '>'. The character '>' can also occur inside a terminating square bracket pattern, so that S[T>] matches both "ST" and "S>". If e is a pattern element, and m and n are two decimal integers with m <= n, then: e(m) is equivalent to the repetition of e exactly m times; e(m,n) is equivalent to the repetition of e exactly k times for any integer k satisfying: m <= k <= n. Some examples:
Each of these walkways is bordered by London plane (Platanus × hispanica) trees, which contribute to the park's European feel. In addition, numerous statues are scattered throughout the park. A raised terrace on the eastern side of the lawn, which dates to the construction of the library's main branch, is paved with gray flagstones and red brick. Its centerpiece is the William Cullen Bryant Memorial, which is raised on a pedestal of its own. A restroom structure is located at the northern border of the park along 42nd Street. A carousel, installed in 2002, is located at the park's southern border. The park is served by the New York City Subway's 7, <7>, B, D, F, <F>, and M trains at 42nd Street–Bryant Park/Fifth Avenue station, entrances to which are located on the northern and western borders of the park, as well as MTA Regional Bus Operations' M1, M2, M3, M4, M5, M7, M42, M55 and Q32 routes.
Sources: en.wikipedia.org
It corresponds to the first 28 amino acids of thymosin beta-4, a larger protein found in many tissues. The fragment is acetylated at its N-terminus and is produced synthetically for research and pharmaceutical use. Synthetic and natural forms share the same sequence.
It is usually described as an immunomodulatory peptide rather than a classical hormone. It does not travel to a single distant organ in the manner of an endocrine hormone. Classification varies across sources, and some texts group it with thymic peptides generally.
The broad outline involves immune cell activation, but the specific molecular steps remain under investigation. Different studies report effects on dendritic cells, T cells, and natural killer cells. No single receptor has been confirmed as the sole mediator.
它不是经典的内分泌激素，而是一种免疫调节肽。其作用主要通过局部免疫细胞间的信号传递实现，而非经血液循环作用于远隔器官。