This is a working overview of thymalfasin, written for readers who want more than a one-paragraph summary but less than a textbook.
Reviewed 2026-06-11. Anything still debated is marked as such rather than presented as settled.
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。
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.
Immunological studies connect the peptide to multiple parts of the immune response. It has been reported to engage Toll-like receptor signaling, to promote dendritic cell maturation, and to influence the balance of T helper cell subsets. Changes in natural killer cell activity and in cytokine release appear in cell culture and animal models. These observations describe broad immunomodulatory behavior rather than a single defined receptor target, and the primary molecular interaction has not been settled.
| Property | Value | Notes |
|---|---|---|
| 化学分类 | 线性肽 | 由28个氨基酸组成 |
| 分子量 | 约3108 Da | 合成版本一致 |
| 外观 | 白色至类白色粉末 | 冻干品 |
| 溶解度 | 易溶于水 | 微溶于有机溶剂 |
| 储存温度 | -20°C（冻干） | 溶解后2-8°C |
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 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.
Lyophilized material is typically treated as a hygroscopic solid that should be brought to room temperature before the container is opened, which limits condensation on the powder. Reconstitution is commonly done with sterile water or a buffered diluent, and gentle mixing is preferred over vigorous agitation to reduce foaming and surface adsorption. Because peptides can bind to plastic and glass, diluents containing a small amount of carrier protein are sometimes used in laboratory work. Working solutions are generally aliquoted and prepared fresh rather than subjected to repeated freezing and thawing.
Stability depends on temperature, pH, and the number of freeze-thaw events the sample has experienced. Freeze-dried material is commonly held at -20 °C or colder, while reconstituted liquid is kept cold and used within a short window. Extreme pH and prolonged light exposure can promote deamidation, oxidation, or aggregation, particularly at asparagine and methionine positions. Adsorption to container walls can lower the measured concentration of a dilute solution even when the peptide molecules themselves remain intact.
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.
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.
=== Clarity === Dexcom Clarity is a diabetes management software and mobile application that allows users to view, analyze, and share their Dexcom CGM data. It displays glucose data through various visual reports and graphs, helping users recognize key trends and patterns, such as nighttime highs or lows, that are important for optimizing diabetes care. In addition to mobile and desktop access, Dexcom Clarity offers a clinic portal for healthcare providers, allowing them to remotely access and review patient data. The software generates several types of reports, including summaries of key statistics, analyses of glucose patterns, and trend graphs that can be customized and filtered for detailed examination.
==== Plants ==== Plant genome studies have revealed the existence of protein isovariants within the actin family of genes. Within Arabidopsis thaliana, a model organism, there are ten types of actin, six profilins, and dozens of myosins. This diversity is explained by the evolutionary necessity of possessing variants that slightly differ in their temporal and spatial expression. The majority of these proteins were jointly expressed in the tissue analysed. Actin networks are distributed throughout the cytoplasm of cells that have been cultivated in vitro. There is a concentration of the network around the nucleus that is connected via spokes to the cellular cortex, this network is highly dynamic, with a continuous polymerization and depolymerization.
=== Permanent hair removal === Electrology has been practiced in the United States since 1875. It is approved by the FDA. This technique permanently destroys germ cells responsible for hair growth by way of the insertion of a fine probe into the hair follicle and the application of a current adjusted to each hair type and treatment area. Electrology is the only permanent hair removal method recognized by the FDA.
== Distribution == Cold seeps were discovered in 1983 by Charles Paull and colleagues on the Florida Escarpment in the Gulf of Mexico at a depth of 3,200 meters (10,500 ft). Since then, seeps have been discovered in many other parts of the world's oceans. Most have been grouped into five biogeographic provinces: Gulf of Mexico, Atlantic, Mediterranean, East Pacific, and West Pacific, but cold seeps are also known from under the ice shelf in Antarctica, the Arctic Ocean, the North Sea, Skagerrak, Kattegat, the Gulf of California, the Red Sea, the Indian Ocean, off southern Australia, and in the inland Caspian Sea. In the Pacific Northwest, a cold seep called Pythia's Oasis was discovered in 2015. With the recent discovery of a methane seep in the Southern Ocean, cold seeps are now known in all major oceans. Cold seeps are common along continental margins in areas of high primary productivity and tectonic activity, where crustal deformation and compaction drive emissions of methane-rich fluid. Cold seeps are patchily distributed, and they occur most frequently near ocean margins from intertidal to hadal depths. In Chile, cold seeps are known from the intertidal zone, in Kattegat, the methane seeps are known as "bubbling reefs" and are typically at depths of 0–30 m (0–100 ft), and off northern California, they can be found as shallow as 35–55 m (115–180 ft). Most cold seeps are located considerably deeper, well beyond the reach of ordinary scuba diving, and the deepest seep community known is found in the Japan Trench at a depth of 7,326 m (24,035 ft).
Sources: en.wikipedia.org
=== EC 2.1.1: Methyltransferases === EC 2.1.1.1: nicotinamide N-methyltransferase EC 2.1.1.2: guanidinoacetate N-methyltransferase EC 2.1.1.3: thetin—homocysteine S-methyltransferase EC 2.1.1.4: acetylserotonin O-methyltransferase EC 2.1.1.5: betaine—homocysteine S-methyltransferase EC 2.1.1.6: catechol O-methyltransferase EC 2.1.1.7: nicotinate N-methyltransferase EC 2.1.1.8: histamine N-methyltransferase EC 2.1.1.9: thiol S-methyltransferase EC 2.1.1.10: homocysteine S-methyltransferase EC 2.1.1.11: magnesium protoporphyrin IX methyltransferase EC 2.1.1.12: methionine S-methyltransferase EC 2.1.1.13: methionine synthase EC 2.1.1.14: 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase EC 2.1.1.15: fatty-acid O-methyltransferase EC 2.1.1.16: methylene-fatty-acyl-phospholipid synthase EC 2.1.1.17: phosphatidylethanolamine N-methyltransferase EC 2.1.1.18: polysaccharide O-methyltransferase EC 2.1.1.19: trimethylsulfonium—tetrahydrofolate N-methyltransferase EC 2.1.1.20: glycine N-methyltransferase EC 2.1.1.21: methylamine—glutamate N-methyltransferase EC 2.1.1.22: carnosine N-methyltransferase EC 2.1.1.23: now covered by EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126 EC 2.1.1.24: now covered by EC 2.1.1.77, EC 2.1.1.80 and EC 2.1.1.100 EC 2.1.1.25: phenol O-methyltransferase EC 2.1.1.26: iodophenol O-methyltransferase EC 2.1.1.27: tyramine N-methyltransferase EC 2.1.1.28: phenylethanolamine N-methyltransferase EC 2.1.1.29: Now covered by EC 2.1.1.202, EC 2.1.1.203 and EC .1.1.204 EC 2.1.1.30: tRNA (purine-2- or -6-)-methyltransferase: Reactions previously described are due to EC 2.1.1.32 EC 2.1.1.31: Now covered by EC 2.1.1.221 and EC 2.1.1.228 EC 2.1.1.32: Now covered by EC 2.1.1.213, EC 2.1.1.214, EC 2.1.1.215 and EC 2.1.1.216 EC 2.1.1.33: tRNA (guanine46-N7)-methyltransferase EC 2.1.1.34: tRNA (guanosine18-2′-O)-methyltransferase EC 2.1.1.35: tRNA (uracil54-C5)-methyltransferase EC 2.1.1.36: Now covered by EC 2.1.1.217, EC 2.1.1.218, EC 2.1.1.219, EC 2.1.1.220 EC 2.1.1.37: DNA (cytosine-5-)-methyltransferase EC 2.1.1.38: O-demethylpuromycin O-methyltransferase EC 2.1.1.39: inositol 3-methyltransferase EC 2.1.1.40: inositol 1-methyltransferase EC 2.1.1.41: sterol 24-C-methyltransferase EC 2.1.1.42: flavone 3′-O-methyltransferase EC 2.1.1.43: Now described by EC 2.1.1.354, EC 2.1.1.355, EC 2.1.1.356, EC 2.1.1.357, EC 2.1.1.358, EC 2.1.1.359, EC 2.1.1.360, EC 2.1.1.361 and EC 2.1.1.362 EC 2.1.1.44: L-histidine Nα-methyltransferase EC 2.1.1.45: thymidylate synthase EC 2.1.1.46: isoflavone 4′-O-methyltransferase EC 2.1.1.47: indolepyruvate C-methyltransferase EC 2.1.1.48: Now covered by EC 2.1.1.181, EC 2.1.1.182, EC 2.1.1.183 and EC 2.1.1.184 EC 2.1.1.49: amine N-methyltransferase EC 2.1.1.50: loganate O-methyltransferase EC 2.1.1.51: Now covered by EC 2.1.1.187 and EC 2.1.1.188 EC 2.1.1.52: Now covered by EC 2.1.1.171, EC 2.1.1.172, EC 2.1.1.173 and EC 2.1.1.174 EC 2.1.1.53: putrescine N-methyltransferase EC 2.1.1.54: deoxycytidylate C-methyltransferase EC 2.1.1.55: tRNA (adenine-N6-)-methyltransferase EC 2.1.1.56: mRNA (guanine-N7)-methyltransferase EC 2.1.1.57: methyltransferase cap1 EC 2.1.1.58: deleted, included in EC 2.1.1.57 EC 2.1.1.59: [cytochrome c]-lysine N-methyltransferase EC 2.1.1.60: calmodulin-lysine N-methyltransferase EC 2.1.1.61: tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase EC 2.1.1.62: mRNA (2′-O-methyladenosine-N6-)-methyltransferase EC 2.1.1.63: methylated-DNA—[protein]-cysteine S-methyltransferase EC 2.1.1.64: 3-demethylubiquinol 3-O-methyltransferase EC 2.1.1.65: licodione 2′-O-methyltransferase EC 2.1.1.66: Now covered by EC 2.1.1.230 EC 2.1.1.67: thiopurine S-methyltransferase EC 2.1.1.68: caffeate O-methyltransferase EC 2.1.1.69: 5-hydroxyfuranocoumarin 5-O-methyltransferase EC 2.1.1.70: 8-hydroxyfuranocoumarin 8-O-methyltransferase EC 2.1.1.71: phosphatidyl-N-methylethanolamine N-methyltransferase EC 2.1.1.72: site-specific DNA-methyltransferase (adenine-specific) EC 2.1.1.73: deleted: reaction is that of EC 2.1.1.37, DNA (cytosine-5-)-methyltransferase EC 2.1.1.74: methylenetetrahydrofolate—tRNA-(uracil54-C5)-methyltransferase [NAD(P)H-oxidizing] EC 2.1.1.75: apigenin 4′-O-methyltransferase EC 2.1.1.76: quercetin 3-O-methyltransferase EC 2.1.1.77: protein-L-isoaspartate(D-aspartate) O-methyltransferase EC 2.1.1.78: isoorientin 3′-O-methyltransferase EC 2.1.1.79: cyclopropane-fatty-acyl-phospholipid synthase EC 2.1.1.80: protein-glutamate O-methyltransferase EC 2.1.1.81: deleted, included in EC 2.1.1.49 EC 2.1.1.82: 3-methylquercetin 7-O-methyltransferase EC 2.1.1.83: 3,7-dimethylquercetin 4′-O-methyltransferase EC 2.1.1.84: methylquercetagetin 6-O-methyltransferase EC 2.1.1.85: protein-histidine N-methyltransferase EC 2.1.1.86: Now covered by EC 7.2.1.4 EC 2.1.1.87: pyridine N-methyltransferase EC 2.1.1.88: 8-hydroxyquercetin 8-O-methyltransferase EC 2.1.1.89: tetrahydrocolumbamine 2-O-methyltransferase EC 2.1.1.90: methanol—5-hydroxybenzimidazolylcobamide Co-methyltransferase EC 2.1.1.91: isobutyraldoxime O-methyltransferase EC 2.1.1.92: Now included with EC 2.1.1.69 EC 2.1.1.93: is identical to EC 2.1.1.70, 8-hydroxyfuranocoumarin 8-O-methyltransferase EC 2.1.1.94: tabersonine 16-O-methyltransferase EC 2.1.1.95: tocopherol C-methyltransferase EC 2.1.1.96: thioether S-methyltransferase EC 2.1.1.97: 3-hydroxyanthranilate 4-C-methyltransferase EC 2.1.1.98: diphthine synthase EC 2.1.1.99: 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase EC 2.1.1.100: protein-S-isoprenylcysteine O-methyltransferase EC 2.1.1.101: macrocin O-methyltransferase EC 2.1.1.102: demethylmacrocin O-methyltransferase EC 2.1.1.103: phosphoethanolamine N-methyltransferase EC 2.1.1.104: caffeoyl-CoA O-methyltransferase EC 2.1.1.105: N-benzoyl-4-hydroxyanthranilate 4-O-methyltransferase EC 2.1.1.106: tryptophan 2-C-methyltransferase EC 2.1.1.107: uroporphyrinogen-III C-methyltransferase EC 2.1.1.108: 6-hydroxymellein O-methyltransferase EC 2.1.1.109: demethylsterigmatocystin 6-O-methyltransferase EC 2.1.1.110: sterigmatocystin 8-O-methyltransferase EC 2.1.1.111: anthranilate N-methyltransferase EC 2.1.1.112: glucuronoxylan 4-O-methyltransferase EC 2.1.1.113: site-specific DNA-methyltransferase (cytosine-N4-specific) EC 2.1.1.114: polyprenyldihydroxybenzoate methyltransferase EC 2.1.1.115: (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase EC 2.1.1.116: 3′-hydroxy-N-methyl-(S)-coclaurine 4′-O-methyltransferase EC 2.1.1.117: (S)-scoulerine 9-O-methyltransferase EC 2.1.1.118: columbamine O-methyltransferase EC 2.1.1.119: 10-hydroxydihydrosanguinarine 10-O-methyltransferase EC 2.1.1.120: 12-hydroxydihydrochelirubine 12-O-methyltransferase EC 2.1.1.121: 6-O-methylnorlaudanosoline 5′-O-methyltransferase EC 2.1.1.122: (S)-tetrahydroprotoberberine N-methyltransferase EC 2.1.1.123: [cytochrome-c]-methionine S-methyltransferase EC 2.1.1.124: Now covered by EC 2.1.1.319, EC 2.1.1.320, EC 2.1.1.321 and EC 2.1.1.322 EC 2.1.1.125: Now covered by EC 2.1.1.319, EC 2.1.1.320 and EC 2.1.1.321 EC 2.1.1.126: Now covered by EC 2.1.1.319, EC 2.1.1.320 and EC 2.1.1.321 EC 2.1.1.127: [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase EC 2.1.1.128: (RS)-norcoclaurine 6-O-methyltransferase EC 2.1.1.129: inositol 4-methyltransferase EC 2.1.1.130: precorrin-2 C20-methyltransferase EC 2.1.1.131: precorrin-2 C17-methyltransferase EC 2.1.1.132: precorrin-6B C5,15-methyltransferase (decarboxylating) EC 2.1.1.133: precorrin-4 C11-methyltransferase EC 2.1.1.134: now with EC 2.1.1.129 EC 2.1.1.135: now EC 1.16.1.8 EC 2.1.1.136: chlorophenol O-methyltransferase EC 2.1.1.137: arsenite methyltransferase EC 2.1.1.138: deleted: Reaction due to EC 2.1.1.137 EC 2.1.1.139: 3′-demethylstaurosporine O-methyltransferase EC 2.1.1.140: (S)-coclaurine-N-methyltransferase EC 2.1.1.141: jasmonate O-methyltransferase EC 2.1.1.142: cycloartenol 24-C-methyltransferase EC 2.1.1.143: 24-methylenesterol C-methyltransferase EC 2.1.1.144: trans-aconitate 2-methyltransferase EC 2.1.1.145: trans-aconitate 3-methyltransferase EC 2.1.1.146: (iso)eugenol O-methyltransferase EC 2.1.1.147: corydaline synthase EC 2.1.1.148: thymidylate synthase (FAD) EC 2.1.1.149: Now covered by EC 2.1.1.267, flavonoid 3′,5′-methyltransferase EC 2.1.1.150: isoflavone 7-O-methyltransferase EC 2.1.1.151: cobalt-factor II C20-methyltransferase EC 2.1.1.152: precorrin-6A synthase (deacetylating) EC 2.1.1.153: vitexin 2′′-O-rhamnoside 7-O-methyltransferase EC 2.1.1.154: isoliquiritigenin 2′-O-methyltransferase EC 2.1.1.155: kaempferol 4′-O-methyltransferase EC 2.1.1.156: glycine/sarcosine N-methyltransferase EC 2.1.1.157: sarcosine/dimethylglycine N-methyltransferase EC 2.1.1.158: 7-methylxanthosine synthase EC 2.1.1.159: theobromine synthase EC 2.1.1.160: caffeine synthase EC 2.1.1.161: dimethylglycine N-methyltransferase EC 2.1.1.162: glycine/sarcosine/dimethylglycine N-methyltransferase EC 2.1.1.163: demethylmenaquinone methyltransferase EC 2.1.1.164: demethylrebeccamycin-D-glucose O-methyltransferase EC 2.1.1.165: methyl halide transferase EC 2.1.1.166: 23S rRNA (uridine2552-2′-O)-methyltransferase EC 2.1.1.167: 27S pre-rRNA (guanosine2922-2′-O)-methyltransferase EC 2.1.1.168: 21S rRNA (uridine2791-2′-O)-methyltransferase EC 2.1.1.169: tricetin 3′,4′,5′-O-trimethyltransferase EC 2.1.1.170: 16S rRNA (guanine527-N7)-methyltransferase EC 2.1.1.171: 16S rRNA (guanine966-N2)-methyltransferase EC 2.1.1.172: 16S rRNA (guanine1207-N2))-methyltransferase EC 2.1.1.173: 23S rRNA (guanine2445-N2)-methyltransferase EC 2.1.1.174: 23S rRNA (guanine1835-N2)-methyltransferase EC 2.1.1.175: tricin synthase EC 2.1.1.176: 16S rRNA (cytosine967-C5)-methyltransferase EC 2.1.1.177: 23S rRNA (pseudouridine1915-N3)-methyltransferase EC 2.1.1.178: 16S rRNA (cytosine1407-C5)-methyltransferase EC 2.1.1.179: 16S rRNA (guanine1405-N7)-methyltransferase EC 2.1.1.180: 16S rRNA (adenine1408-N1)-methyltransferase EC 2.1.1.181: 23S rRNA (adenine1618-N6)-methyltransferase EC 2.1.1.182: 16S rRNA (adenine1518-N6/adenineadenine1519-N6)-dimethyltransferase EC 2.1.1.183: 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase EC 2.1.1.184: 23S rRNA (adenine2085-N6)-dimethyltransferase EC 2.1.1.185: 23S rRNA (guanosine2251-2′-O)-methyltransferase EC 2.1.1.186: 23S rRNA (cytidine2498-2′-O)-methyltransferase EC 2.1.1.187: 23S rRNA (guanine745-N1)-methyltransferase EC 2.1.1.188: 23S rRNA (guanine748-N1)-methyltransferase EC 2.1.1.189: 23S rRNA (uracil747-C5)-methyltransferase EC 2.1.1.190: 23S rRNA (uracil1939-C5)-methyltransferase EC 2.1.1.191: 23S rRNA (cytosine1962-C5)-methyltransferase EC 2.1.1.192: 23S rRNA (adenine2503-C2)-methyltransferase EC 2.1.1.193: 16S rRNA (uracil1498-N3)-methyltransferase EC 2.1.1.194: A mixture of EC 2.1.1.192 and EC 2.1.1.224 EC 2.1.1.195: cobalt-precorrin-5B (C1)-methyltransferase EC 2.1.1.196: cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) EC 2.1.1.197: malonyl-[acyl-carrier protein] O-methyltransferase EC 2.1.1.198: 16S rRNA (cytidine1402-2′-O)-methyltransferase EC 2.1.1.199: 16S rRNA (cytosine1402-N4)-methyltransferase EC 2.1.1.200: tRNA (cytidine32/uridine32-2′-O)-methyltransferase EC 2.1.1.201: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase EC 2.1.1.202: multisite-specific tRNA:(cytosine-C5)-methyltransferase EC 2.1.1.203: tRNA (cytosine34-C5)-methyltransferase EC 2.1.1.204: tRNA (cytosine38-C5)-methyltransferase EC 2.1.1.205: tRNA (cytidine32/guanosine34-2′-O)-methyltransferase EC 2.1.1.206: tRNA (cytidine56-2′-O)-methyltransferase EC 2.1.1.207: tRNA (cytidine34-2′-O)-methyltransferase EC 2.1.1.208: 23S rRNA (uridine2479-2′-O)-methyltransferase EC 2.1.1.209: 23S rRNA (guanine2535-N1)-methyltransferase EC 2.1.1.210: demethylspheroidene O-methyltransferase EC 2.1.1.211: tRNASer(uridine44-2′-O)-methyltransferase EC 2.1.1.212: 2,7,4′-trihydroxyisoflavanone 4′-O-methyltransferase EC 2.1.1.213: tRNA (guanine110-N2)-dimethyltransferase EC 2.1.1.214: tRNA (guanine10-N2)-methyltransferase EC 2.1.1.215: tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase EC 2.1.1.216: tRNA (guanine26-N2)-dimethyltransferase EC 2.1.1.217: tRNA (adenine22-N1)-methyltransferase EC 2.1.1.218: tRNA (adenine9-N1)-methyltransferase EC 2.1.1.219: tRNA (adenine57-N1/adenine58-N1)-methyltransferase EC 2.1.1.220: tRNA (adenine58-N1)-methyltransferase EC 2.1.1.221: tRNA (guanine9-N1)-methyltransferase EC 2.1.1.222: 2-polyprenyl-6-hydroxyphenyl methylase EC 2.1.1.223: tRNA1Val (adenine937-N6)-methyltransferase EC 2.1.1.224: 23S rRNA (adenine2503-C8)-methyltransferase EC 2.1.1.225: tRNA:m4X modification enzyme EC 2.1.1.226: 23S rRNA (cytidine1920-2′-O)-methyltransferase EC 2.1.1.227: 16S rRNA (cytidine1409-2′-O)-methyltransferase EC 2.1.1.228: tRNA (guanine37-N1)-methyltransferase EC 2.1.1.229: tRNA (carboxymethyluridine34-5-O)-methyltransferase EC 2.1.1.230: 23S rRNA (adenosine1067-2′-O)-methyltransferase EC 2.1.1.231: flavonoid 4′-O-methyltransferase EC 2.1.1.232: naringenin 7-O-methyltransferase EC 2.1.1.233: [phosphatase 2A protein]-leucine-carboxy methyltransferase EC 2.1.1.234: dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose N,N-dimethyltransferase EC 2.1.1.235: dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose N,N-dimethyltransferase EC 2.1.1.236: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose N,N-dimethyltransferase EC 2.1.1.237: mycinamicin III 3′′-O-methyltransferase EC 2.1.1.238: mycinamicin VI 2′′-O-methyltransferaseD EC 2.1.1.239: L-olivosyl-oleandolide 3-O-methyltransferase EC 2.1.1.240: trans-resveratrol di-O-methyltransferase EC 2.1.1.241: 2,4,7-trihydroxy-1,4-benzoxazin-3-one-glucoside 7-O-methyltransferase EC 2.1.1.242: 16S rRNA (guanine1516-N2)-methyltransferase EC 2.1.1.243: 2-ketoarginine methyltransferase EC 2.1.1.244: protein N-terminal methyltransferase EC 2.1.1.245: 5-methyltetrahydrosarcinapterin—corrinoid/iron-sulfur protein Co-methyltransferase EC 2.1.1.246: [methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase EC 2.1.1.247: (methyl-Co(III) methylamine-specific corrinoid protein)—coenzyme M methyltransferase EC 2.1.1.248: methylamine—corrinoid protein Co-methyltransferase EC 2.1.1.249: dimethylamine—corrinoid protein Co-methyltransferase EC 2.1.1.250: trimethylamine—corrinoid protein Co-methyltransferase EC 2.1.1.251: methylated-thiol—coenzyme M methyltransferase EC 2.1.1.252: tetramethylammonium—corrinoid protein Co-methyltransferase EC 2.1.1.253: [methyl-Co(III) tetramethylammonium-specific corrinoid protein]—coenzyme M methyltransferase EC 2.1.1.254: erythromycin 3′′-O-methyltransferase EC 2.1.1.255: geranyl diphosphate 2-C-methyltransferase EC 2.1.1.256: tRNA (guanine6-N6-methyltransferase) EC 2.1.1.257: tRNA (pseudouridine54-N1)-methyltransferase EC 2.1.1.258: 5-methyltetrahydrofolate—corrinoid/iron-sulfur protein Co-methyltransferase EC 2.1.1.259: [fructose-bisphosphate aldolase]-lysine N-methyltransferase EC 2.1.1.260: rRNA small subunit pseudouridine methyltransferase Nep1 EC 2.1.1.261: 4-dimethylallyltryptophan N-methyltransferase EC 2.1.1.262: squalene methyltransferase EC 2.1.1.263: botryococcene C-methyltransferase EC 2.1.1.264: 23S rRNA (guanine2069-N7)-methyltransferase EC 2.1.1.265: tellurite methyltransferase EC 2.1.1.266: 23S rRNA (adenine2030-N6)-methyltransferase EC 2.1.1.267: flavonoid 3′,5′-methyltransferase EC 2.1.1.268: tRNAThr (cytosine32-N3)-methyltransferase EC 2.1.1.269: dimethylsulfoniopropionate demethylase EC 2.1.1.270: (+)-6a-hydroxymaackiain 3-O-methyltransferase EC 2.1.1.271: cobalt-precorrin-4 methyltransferase EC 2.1.1.272: cobalt-factor III methyltransferase EC 2.1.1.273: benzoate O-methyltransferase EC 2.1.1.274: salicylate 1-O-methyltransferase EC 2.1.1.275: gibberellin A9 O-methyltransferase EC 2.1.1.276: gibberellin A4 carboxyl methyltransferase EC 2.1.1.277: anthranilate O-methyltransferase EC 2.1.1.278: indole-3-acetate O-methyltransferase EC 2.1.1.279: trans-anol O-methyltransferase EC 2.1.1.280: selenocysteine Se-methyltransferase EC 2.1.1.281: phenylpyruvate C3-methyltransferase EC 2.1.1.282: tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase EC 2.1.1.283: emodin O-methyltransferase EC 2.1.1.284: 8-demethylnovobiocic acid C8-methyltransferase EC 2.1.1.285: demethyldecarbamoylnovobiocin O-methyltransferase EC 2.1.1.286: 25S rRNA (adenine2142-N1)-methyltransferase EC 2.1.1.287: 25S rRNA (adenine645-N1)-methyltransferase EC 2.1.1.288: aklanonic acid methyltransferase EC 2.1.1.289: cobalt-precorrin-7 (C5)-methyltransferase EC 2.1.1.290: tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase EC 2.1.1.291: (R,S)-reticuline 7-O-methyltransferase EC 2.1.1.292: carminomycin 4-O-methyltransferase EC 2.1.1.293: 6-hydroxytryprostatin B O-methyltransferase EC 2.1.1.294: 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase EC 2.1.1.295: 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase EC 2.1.1.296: methyltransferase cap2 EC 2.1.1.297: peptide chain release factor N5-glutamine methyltransferase EC 2.1.1.298: ribosomal protein L3 N5-glutamine methyltransferase EC 2.1.1.299: protein N-terminal monomethyltransferase EC 2.1.1.300: pavine N-methyltransferase EC 2.1.1.301: cypemycin N-terminal methyltransferase EC 2.1.1.302: 3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase EC 2.1.1.303: 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase EC 2.1.1.304: L-tyrosine C3-methyltransferase EC 2.1.1.305: 8-demethyl-8-α-L-rhamnosyltetracenomycin-C 2′-O-methyltransferase EC 2.1.1.306: 8-demethyl-8-(2-methoxy-α-L-rhamnosyl)tetracenomycin-C 3′-O-methyltransferase EC 2.1.1.307: 8-demethyl-8-(2,3-dimethoxy-α-L-rhamnosyl)tetracenomycin-C 4′-O-methyltransferase EC 2.1.1.308: cytidylyl-2-hydroxyethylphosphonate methyltransferase EC 2.1.1.309: 18S rRNA (guanine1575-N7)-methyltransferase EC 2.1.1.310: 25S rRNA (cytosine2870-C5)-methyltransferase EC 2.1.1.311: 25S rRNA (cytosine2278-C5)-methyltransferase EC 2.1.1.312: 25S rRNA (uracil2843-N3)-methyltransferase EC 2.1.1.313: 25S rRNA (uracil2634-N3)-methyltransferase EC 2.1.1.314: diphthine methyl ester synthase EC 2.1.1.315: 27-O-demethylrifamycin SV methyltransferase EC 2.1.1.316: mitomycin 6-O-methyltransferase EC 2.1.1.317: sphingolipid C9-methyltransferase EC 2.1.1.318: [trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase EC 2.1.1.319: type I protein arginine methyltransferase EC 2.1.1.320: type II protein arginine methyltransferase EC 2.1.1.321: type III protein arginine methyltransferase EC 2.1.1.322: type IV protein arginine methyltransferase EC 2.1.1.323: (–)-pluviatolide 4-O-methyltransferase EC 2.1.1.324: dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase EC 2.1.1.325: juvenile hormone-III synthase EC 2.1.1.326: N-acetyldemethylphosphinothricin P-methyltransferase EC 2.1.1.327: phenazine-1-carboxylate N-methyltransferase EC 2.1.1.328: N-demethylindolmycin N-methyltransferase EC 2.1.1.329: demethylphylloquinol methyltransferase EC 2.1.1.330: 5′-demethylyatein 5′-O-methyltransferase EC 2.1.1.331: bacteriochlorophyllide d C-121-methyltransferase EC 2.1.1.332: bacteriochlorophyllide d C-82-methyltransferase EC 2.1.1.333: bacteriochlorophyllide d C-20 methyltransferase EC 2.1.1.334: methanethiol S-methyltransferase EC 2.1.1.335: 4-amino-anhydrotetracycline N4-methyltransferase EC 2.1.1.336: norbelladine O-methyltransferase EC 2.1.1.337: reticuline N-methyltransferase EC 2.1.1.338: desmethylxanthohumol 6′-O-methyltransferase EC 2.1.1.339: xanthohumol 4-O-methyltransferase EC 2.1.1.340: 3-aminomethylindole N'-methyltransferase EC 2.1.1.341: vanillate/3-O-methylgallate O-demethylase EC 2.1.1.342: anaerobilin synthase EC 2.1.1.343: 8-amino-8-demethylriboflavin N,N-dimethyltransferase EC 2.1.1.344: ornithine lipid N-methyltransferase EC 2.1.1.345: psilocybin synthase EC 2.1.1.346: U6 snRNA m6A methyltransferase EC 2.1.1.347: (+)-O-methylkolavelool synthase EC 2.1.1.348: mRNA m6A methyltransferase EC 2.1.1.349: toxoflavin synthase EC 2.1.1.350: menaquinone C8-methyltransferase EC 2.1.1.351: nocamycin O-methyltransferase EC 2.1.1.352: 3-O-acetyl-4′-O-demethylpapaveroxine 4′-O-methyltransferase EC 2.1.1.353: demethylluteothin O-methyltransferase EC 2.1.1.354: [histone H3]-lysine4 N-trimethyltransferase EC 2.1.1.355: [histone H3]-lysine9 N-trimethyltransferase EC 2.1.1.356: [histone H3]-lysine27 N-trimethyltransferase EC 2.1.1.357: [histone H3]-lysine36 N-dimethyltransferase EC 2.1.1.358: [histone H3]-dimethyl-L-lysine36 N-methyltransferase. Now known to have the activity of EC 2.1.1.359, [histone H3]-lysine36 N-trimethyltransferase. EC 2.1.1.359: [histone H3]-lysine36 N-trimethyltransferase EC 2.1.1.360: [histone H3]-lysine79 N-trimethyltransferase EC 2.1.1.361: [histone H4]-lysine20 N-methyltransferase EC 2.1.1.362: [histone H4]-N-methyl-L-lysine20 N-methyltransferase EC 2.1.1.363: pre-sodorifen synthase EC 2.1.1.364: [histone H3]-lysine4 N-methyltransferase EC 2.1.1.365: MMP 1-O-methyltransferase EC 2.1.1.366: [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase EC 2.1.1.367: [histone H3]-lysine9 N-methyltransferase EC 2.1.1.368: [histone H3]-lysine9 N-dimethyltransferase EC 2.1.1.369: [histone H3]-lysine27 N-methyltransferase EC 2.1.1.370: [histone H3]-lysine4 N-dimethyltransferase EC 2.1.1.371: [histone H3]-lysine27 N-dimethyltransferase EC 2.1.1.372: [histone H4]-lysine20 N-trimethyltransferase EC 2.1.1.373: 2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase EC 2.1.1.374: 2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase EC 2.1.1.375: NNS virus cap methyltransferase EC 2.1.1.376: glycine betaine—corrinoid protein Co-methyltransferase EC 2.1.1.377: [methyl-Co(III) glycine betaine-specific corrinoid protein]—coenzyme M methyltransferase EC 2.1.1.378: [methyl-Co(III) glycine betaine-specific corrinoid protein]—tetrahydrofolate methyltransferase EC 2.1.1.379: [methyl coenzyme M reductase]-L-arginine C-5-methyltransferase
cell biology genetics cancer biology metabolism and obesity neuroscience and neurodegeneration infectious disease structural biology chemical biology chemistry In addition to faculty labs, the institute is home to research cores that provide services to the institute, the university, and external partners:
Machine vision systems often require bright and homogeneous illumination, so features of interest are easier to process. LEDs are often used. Barcode scanners are the most common example of machine vision applications, and many of those scanners use red LEDs instead of lasers. Optical computer mice use LEDs as a light source for the miniature camera within the mouse. LEDs are useful for machine vision because they provide a compact, reliable source of light. LED lamps can be turned on and off to suit the needs of the vision system, and the shape of the beam produced can be tailored to match the system's requirements.
Lately Chief Executive, Convention of Scottish Local Authorities. For services to Local Government. Joshua MacAlister. Chair, Independent Review of Children's Social Care and Founder, Frontline. For services to Vulnerable Children. Norman Alexander MacDonald. Lately Local Councillor, Comhairle nan Eilean Siar. For services to the communities of Uig, Isle of Lewis and the Western Isles. Charles Piers Mackesy. Artist, Illustrator and Author. For services to Art and Literature. Catherine Elizabeth Magee. Chief Executive Officer, Dyslexia Scotland. For services to People with Dyslexia. Moni Mannings. Founder, EPOC (Empowering People of Colour). For services to Cultural Philanthropy, to Business and to Charity. Dr. Kathryn Jean Marks. Deputy Director, Environment Agency. For services to Flood Risk Management and to Equality, Diversity and Inclusion. Steven David Marshall. Chief Executive Officer, The Royal Naval, Army and Air Force Institute. For services to the Armed Forces. Sophia Mary Mason. Trustee, Garfield Weston Foundation. For services to Arts Philanthropy. Ian Stuart Matthews. Portfolio Leader, Ministry of Defence. For services to Defence. Samantha Kate Mayhew. Assistant Principal, Special Educational Needs and Disabilities, Weston College. For services to Further Education. Catherine McBride. Member, Trade and Agriculture Commission. For services to Economic Commentary and Trade Policy. Jonathan Robert McGoh. Chair and Co-Founder, The Reach Foundation and Co-Founder and Trustee, Reach Academy Feltham, London Borough of Hounslow. For services to Education.
=== Maximum depositional age === Some of the most important information we can get from detrital zircon ages is the maximum depositional age of the referring sedimentary unit. The sedimentary unit cannot be older than the youngest age of the analyzed detrital zircons because the zircon should have existed before the rock formation. This provides useful age information to rock strata where fossils are unavailable, such as the terrestrial successions during Precambrian or pre-Devonian times. Practically, maximum depositional age is averaged from a cluster of youngest age data or the peak in age probability because the youngest U-Pb age within a sample is almost always younger with uncertainty.
Sources: en.wikipedia.org
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。
天然胸腺素α1主要从胸腺组织提取，也可在脾脏和淋巴结中检出。目前研究和临床使用的多为化学合成版本，不再依赖动物组织。
胸腺素组分5是牛胸腺提取物的粗组分，包含多种肽。胸腺素α1是其中一种被纯化和表征的单一肽，具有明确的28个氨基酸序列。
It is usually described as an immunomodulatory peptide rather than a classic circulating hormone. No endocrine gland is known to release it as a primary secretory product, and its measured presence in blood is not firmly established.