A practical reference on PTMA gene: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
This page was last updated on 2026-01-29 and is reviewed periodically as new material appears.
The peptide was identified during work in the 1970s on thymosin fraction 5, a partially purified extract of calf thymus. Investigators separated that mixture and characterized individual components, one of which they named thymosin alpha-1. The same compound later received the international nonproprietary name thymalfasin. Commercial material is produced by solid-phase peptide synthesis rather than by extraction, so synthetic and natural forms share an identical sequence. Naming conventions vary across the literature, and readers should distinguish the alpha-1 peptide from other thymosins that have unrelated sequences and functions.
Thymosin beta-4 is a separate 43-residue peptide that binds actin and participates in cell migration; it shares no sequence similarity with thymosin alpha-1 despite the common family name. Other preparative materials, such as thymosin fraction 5 and thymopoietin, contain distinct mixtures or peptides. The shared thymosin label reflects the tissue of origin used in early purification, not a common structural core. Treating these molecules as interchangeable is a frequent source of confusion in laboratory reports and in popular summaries alike.
Thymosin alpha-1 is a synthetic peptide of 28 amino acid residues that corresponds to a naturally occurring fragment first isolated from thymus tissue. Its chain is acetylated at the amino terminus, a modification that shields the peptide from rapid cleavage by aminopeptidases. The molecule carries a net negative charge at physiological pH and dissolves freely in water. Researchers classify it as an immune-modulating agent rather than a classical hormone, because it acts on several cell types of both the innate and the adaptive immune system.
Overall evidence quality varies considerably. A large share of published reports come from single centers, rely on surrogate immunological markers, or lack adequate control groups. Systematic reviews have highlighted this heterogeneity as a barrier to pooling results. Open questions include which patients, if any, might benefit, what treatment duration is appropriate, and whether any effect is independent of standard care. The peptide is often described as an immune modulator rather than a therapy for one disease, which complicates confirmatory trial design.
Thymosin alpha 1 was identified in 1977 as a component of thymosin fraction 5, a heterogeneous preparation used in early studies of thymic function. Investigators purified the active material and determined its amino acid sequence, which enabled chemical synthesis. Work in the following decades concentrated on T-cell maturation and immune reconstitution in animals and small human cohorts. Early preparations varied in composition, so results from that period are difficult to compare with studies using defined synthetic peptide.
| Property | Value | Notes |
|---|---|---|
| Molecular mass | About 3.1 kDa | 28 residues, N-terminally acetylated |
| Appearance | White to off-white powder | Lyophilized solid |
| Solubility | Freely soluble in water | Also soluble in aqueous buffers |
| Storage temperature | 2 to 8 °C | Protect from light and moisture |
| Common synonyms | Thymalfasin; Tα1 | Same peptide sequence |
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.
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.
Thymosin alpha-1 is a synthetic peptide of 28 amino acids, corresponding to the N-terminal fragment of prothymosin alpha. Its sequence begins with acetylation at the N-terminus, a modification that affects stability and receptor interaction. The peptide is acidic, with a calculated isoelectric point near 4.2, and carries no disulfide bonds, so its secondary structure is largely flexible in solution. Molecular mass is approximately 3108 daltons. The native form was first isolated from bovine thymus tissue, while pharmaceutical material is produced by solid-phase peptide synthesis.
The molecule consists of 28 amino acid residues with an acetyl group attached to the N-terminal serine. Its sequence is acidic overall, with several glutamic and aspartic acid residues distributed along the chain and no cysteine, so disulfide bridges do not form. The peptide carries a net negative charge at physiological pH. Because the N-terminus is blocked, the intact molecule resists degradation by many aminopeptidases, which contributes to its stability in biological fluids.
The peptide is generated in cells by cleavage of prothymosin alpha, a larger acidic protein encoded by the PTMA gene. Prothymosin alpha is expressed in many tissues, not only in the thymus, and its functions include nuclear roles in chromatin-related processes. The 28-residue fragment corresponds to the N-terminal portion of that precursor. How the cleavage occurs and how the fragment's concentration is regulated remain open questions; circulating amounts are small and difficult to measure reliably with routine assays.
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.
==== Film works and graphic novel ==== Antonov worked on the 2006 film Renaissance directed by Christian Volkman. He then wrote and illustrated the graphic novel The Colony: A Structure Celebrating the Triumphs of Technology, published in 2010. Antonov was also a co-writer and production designer of the 2011 French sci-fi film The Prodigies.
==== Microbial metabolism ==== Biological deuterium fractionation through metabolism is very organism and pathway dependent, resulting in a wide variability in fractionations. Despite this, some trends still hold. Hydrogen isotopes tend to fractionate very strongly in autotrophs relative to heterotrophs during lipid biosynthesis - chemoautotrophs produce extremely depleted lipids, with the fractionation ranging from roughly −200 to −400‰. This has been observed both in laboratory-grown cultures fed a known quantity of deuterated water and in the environment. Proteins, however, do not follow as significant a trend, with both heterotrophs and autotrophs capable of generating large and variable fractionations. In part, kinetic fractionation of the lighter isotope during formation of reducing equivalents NADH and NADPH result in lipids and proteins that are isotopically lighter. Salinity appears to play a role in the degree of deuterium fractionation as well; more saline waters affect growth rate, the rate of hydrogen exchange, and evaporation rate. All of these factors influence lipid δD upon hydrogen being incorporated into biomass. In coccolithophores Emiliania huxleyi and Gephyrocapsa oceanica, alkenone δD has been found to correlate strongly to organism growth rate divided by salinity. The relationship between deuterium fractionation and salinity could potentially be used in paleoenvironment reconstruction with preserved lipids in the rock record to determine, for example, ocean salinity at the time of organismal growth.
Ethanol (alcohol) is first converted into acetaldehyde, consuming NAD+ twice, before being converted into acetate. The acetate is then converted into acetyl-CoA. When alcohol is consumed in small quantities, the NADH/NAD+ ratio remains in balance enough for the acetyl-CoA to be used by the Krebs cycle for oxidative phosphorylation. However, even moderate amounts of alcohol (1-2 drinks) results in more NADH than NAD+, which inhibits oxidative phosphorylation. When the NADH/NAD+ ratio is disrupted (far more NADH than NAD+), this is called pseudohypoxia. The Krebs cycle needs NAD+ as well as oxygen, for oxidative phosphorylation. Without sufficient NAD+, the impaired aerobic metabolism mimics hypoxia (insufficient oxygen), resulting in excessive use of anaerobic glycolysis and a disrupted pyruvate/lactate ratio (low pyruvate, high lactate). The conversion of pyruvate into lactate produces NAD+, but only enough to maintain anaerobic glycolysis. In chronic excessive alcohol consumption (alcoholism), the microsomal ethanol oxidizing system (MEOS) is used in addition to alcohol dehydrogenase.
In the second phase, British fortunes changed when their commanding officer, General Redvers Buller, was replaced by Lord Roberts and Lord Kitchener, who relieved the besieged cities and invaded the Boer republics at the head of a 180,000-strong expeditionary force. The Boers, aware that they were unable to resist such a force, refrained from fighting pitched battles, thereby allowing the British to occupy both republics and their capitals. Boer politicians fled or went into hiding; the British annexed the two republics in 1900. In Britain, the Conservative ministry attempted to capitalise by calling an early general election, dubbed a "khaki election". In the third phase, Boer fighters launched a guerrilla campaign. They used hit-and-run attacks and ambushes against the British for two years. The guerrilla campaign proved difficult for the British to defeat, due to unfamiliarity with tactics and support among civilians. British high command ordered scorched earth policies as part of a counterinsurgency campaign. Over 100,000 Boer civilians were forcibly relocated into concentration camps, where 26,000 died, by starvation and disease. Native Africans were interned to prevent them from supplying the Boers; 20,000 died. British mounted infantry were deployed to track down guerrillas, and few combatants were killed in action, most dying from disease. Kitchener offered terms to remaining Boer leaders to end the conflict. Eager to ensure Boers were released from the camps, most Boer commanders accepted the terms in the Treaty of Vereeniging, surrendering in May 1902.
Blood Coagulation factor VII with the name of AryoSeven Altebrel with the generic name of Etanercept and original trade name of Enbrel Zytux with the generic name of Rituximab and original trade name of Rituxan َAryoTrust with the generic name of trastuzumab and original name of Herceptin Stivant with the generic name of bevacizumab and original trade name of Avestin AryoSeven is now approved by Iranian food and drug organisation and from August 2012 is in the market.
Sources: en.wikipedia.org
Familial: Family history of hirsutism with normal androgen levels. Drug-induced: medications were used before the onset of hirsutism. The recommendation is to stop the medication and replace it with another. Minoxidil Androgens like testosterone, anabolic steroids, and androgenic progestins Valproic acid and methyldopa Pregnancy: Due to changes in hormone production Idiopathic: When no other cause can be attributed to an individual's hirsutism, the cause is considered idiopathic by exclusion. In these cases, menstrual cycles and levels of conventionally tested androgens (testosterone, androstenedione, and dehydroepiandrosterone sulfate) are normal. Around 10 to 15% of women with hirsutism have idiopathic hirsutism. Idiopathic hirsutism may be due to increased production of dihydrotestosterone (DHT) in hair follicles and hence may actually still be due to hyperandrogenism. It may be detectable by measurement of DHT or DHT metabolites. Rice et al. 2016 propose that idiopathic hirsutism is caused by epigenetic inheritance of discordant epigenetic markers. It is testable with current technology.
=== EC 1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water === EC 1.14.19.1: stearoyl-CoA 9-desaturase EC 1.14.19.2: stearoyl-[acyl-carrier-protein] 9-desaturase EC 1.14.19.3: linoleoyl-CoA desaturase EC 1.14.19.4: acyl-lipid (11-3)-desaturase EC 1.14.19.5: acyl-CoA 11-(Z)-desaturase EC 1.14.19.6: acyl-CoA (9+3)-desaturase EC 1.14.19.7: Now EC 1.11.1.23, (S)-2-hydroxypropylphosphonic acid epoxidase EC 1.14.19.8: pentalenolactone synthase EC 1.14.19.9: tryptophan 7-halogenase EC 1.14.19.10: icosanoyl-CoA 5-desaturase EC 1.14.19.11: acyl-[acyl-carrier-protein] 4-desaturase EC 1.14.19.12: acyl-lipid ω-(9-4) desaturase EC 1.14.19.13: acyl-CoA 15-desaturase EC 1.14.19.14: linoleoyl-lipid Δ9 conjugase EC 1.14.19.15: (11Z)-hexadec-11-enoyl-CoA conjugase EC 1.14.19.16: linoleoyl-lipid Δ12 conjugase (11E,13Z-forming) EC 1.14.19.17: sphingolipid 4-desaturase EC 1.14.19.18: sphingolipid 8-(E)-desaturase EC 1.14.19.19: sphingolipid 10-desaturase EC 1.14.19.20: Δ7-sterol 5(6)-desaturase EC 1.14.19.21: cholesterol 7-desaturase EC 1.14.19.22: acyl-lipid ω-6 desaturase (cytochrome b5) EC 1.14.19.23: acyl-lipid (n+3)-(Z)-desaturase (ferredoxin) EC 1.14.19.24: acyl-CoA 11-(E)-desaturase EC 1.14.19.25: acyl-lipid ω-3 desaturase (cytochrome b5) EC 1.14.19.26: acyl-[acyl-carrier-protein] 6-desaturase EC 1.14.19.27: sn-2 palmitoyl-lipid 9-desaturase EC 1.14.19.28: sn-1 stearoyl-lipid 9-desaturase EC 1.14.19.29: sphingolipid 8-(E/Z)-desaturase EC 1.14.19.30: acyl-lipid (8-3)-desaturase EC 1.14.19.31: acyl-lipid (7-3)-desaturase EC 1.14.19.32: palmitoyl-CoA 14-(E/Z)-desaturase EC 1.14.19.33: Δ12 acyl-lipid conjugase (11E,13E-forming) EC 1.14.19.34: acyl-lipid (9+3)-(E)-desaturase EC 1.14.19.35: sn-2 acyl-lipid ω-3 desaturase (ferredoxin) EC 1.14.19.36: sn-1 acyl-lipid ω-3 desaturase (ferredoxin) EC 1.14.19.37: acyl-CoA 5-desaturase EC 1.14.19.38: acyl-lipid Δ6-acetylenase EC 1.14.19.39: acyl-lipid Δ12-acetylenase EC 1.14.19.40: hex-5-enoyl-[acyl-carrier protein] acetylenase EC 1.14.19.41: sterol 22-desaturase EC 1.14.19.42: palmitoyl-[glycerolipid] 7-desaturase EC 1.14.19.43: palmitoyl-[glycerolipid] 3-(E)-desaturase EC 1.14.19.44: acyl-CoA (8-3)-desaturase EC 1.14.19.45: sn-1 oleoyl-lipid 12-desaturase EC 1.14.19.46: sn-1 linoleoyl-lipid 6-desaturase EC 1.14.19.47: acyl-lipid (9-3)-desaturase EC 1.14.19.48: tert-amyl alcohol desaturase EC 1.14.19.49: tetracycline 7-halogenase EC 1.14.19.50: noroxomaritidine synthase EC 1.14.19.51: (S)-corytuberine synthase EC 1.14.19.52: camalexin synthase EC 1.14.19.53: all-trans-retinol 3,4-desaturase EC 1.14.19.54: 1,2-dehydroreticuline synthase EC 1.14.19.55: 4-hydroxybenzoate brominase (decarboxylating) EC 1.14.19.56: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] chlorinase EC 1.14.19.57: 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] brominase EC 1.14.19.58: tryptophan 5-halogenase EC 1.14.19.59: tryptophan 6-halogenase EC 1.14.19.60: 7-chloro-L-tryptophan 6-halogenase EC 1.14.19.61: dihydrorhizobitoxine desaturase EC 1.14.19.62: secologanin synthase EC 1.14.19.63: pseudobaptigenin synthase EC 1.14.19.64: (S)-stylopine synthase EC 1.14.19.65: (S)-cheilanthifoline synthase EC 1.14.19.66: berbamunine synthase EC 1.14.19.67: salutaridine synthase EC 1.14.19.68: (S)-canadine synthase EC 1.14.19.69: biflaviolin synthase EC 1.14.19.70: mycocyclosin synthase EC 1.14.19.71: fumitremorgin C synthase EC 1.14.19.72: (–)-pluviatolide synthase EC 1.14.19.73: (S)-nandinine synthase EC 1.14.19.74: (+)-piperitol/(+)-sesamin synthase EC 1.14.19.75: very-long-chain acyl-lipid ω-9 desaturase EC 1.14.19.76: flavone synthase II EC 1.14.19.77: plasmanylethanolamine desaturase EC 1.14.19.78: decanoyl-[acyl-carrier protein] acetylenase
The ideal relationship between products and reactants in a chemical reaction can be obtained by using a chemical reaction equation. Stoichiometry is used to run calculations about chemical reactions, for example, the stoichiometric mole ratio between reactants and products. The stoichiometry of a chemical reaction is based on chemical formulas and equations that provide the quantitative relation between the number of moles of various products and reactants, including yields. Stoichiometric equations are used to determine the limiting reagent or reactant—the reactant that is completely consumed in a reaction. The limiting reagent determines the theoretical yield—the relative quantity of moles of reactants and the product formed in a chemical reaction. Other reactants are said to be present in excess. The actual yield—the quantity physically obtained from a chemical reaction conducted in a laboratory—is often less than the theoretical yield. The theoretical yield is what would be obtained if all of the limiting reagent reacted to give the product in question. A more accurate yield is measured based on how much product was actually produced versus how much could be produced. The ratio of the theoretical yield and the actual yield results in a percent yield. When more than one reactant participates in a reaction, the yield is usually calculated based on the amount of the limiting reactant, whose amount is less than stoichiometrically equivalent (or just equivalent) to the amounts of all other reactants present.
== Molecular studies == A monophyletic Pancrustacea has been supported by several molecular studies, in most of which the subphylum Crustacea is paraphyletic with regard to hexapods (that is, that hexapods, including insects, are derived from crustacean ancestors). This means that within Pancrustacea, only some members are actually crustaceans, hexapods being the main exception. The evidence for this clade derives from molecular data and morphological characteristics. The molecular data consists of comparisons of nuclear ribosomal RNA genes, mitochondrial ribosomal RNA genes, and protein coding genes. The morphological data consists of ommatidial structures (see arthropod eye), the presence of neuroblasts, and the form and style of axonogenesis by pioneer neurons.
Sources: en.wikipedia.org
It is a 28-residue synthetic peptide studied as an immune-modulating agent and approved as a drug in some countries. The sequence matches a naturally occurring fragment isolated from thymus tissue. It is not a hormone in the endocrine sense.
The name traces back to thymosin fraction 5, a crude thymus extract examined in the 1970s. Individual peptides in that mixture were labeled with Greek letters, and alpha-1 was one of them. The international nonproprietary name thymalfasin was assigned later.
No. Thymosin beta-4 contains 43 residues and binds actin, while thymosin alpha-1 contains 28 residues and acts on immune cells. The two sit in a historical naming group but share no sequence similarity, and they are not substitutes for one another.
Trials differ in patient population, dose schedule, background treatment, and the endpoints used to judge success. Many are small and single-center, so random variation can dominate the reported effects.