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由来生物
human
リコンビナント
expressed in E. coli
アッセイ
≥95% (HPLC)
≥95% (SDS-PAGE)
形状
lyophilized
有効性
0.5-10 μg/mL
分子量
5.2 kDa
包装
pkg of 100 μg
不純物
endotoxin, tested
UniProtアクセッション番号
輸送温度
wet ice
保管温度
−20°C
遺伝子情報
human ... TMSB4X(7114)
詳細
Thymosin-β4 is a small, actin-sequestering protein belonging to the thymosin-β family that is found at high concentrations within the spleen, thymus, and peritoneal macrophages, where it is most notably responsible for the organization of cytoskeletal structure. Commonly found at significant quantities within the brain, lungs, liver, kidneys, testes, and heart, Thymosin-β4 has also been shown to be synthesized by cells unrelated to the reticuloendothelial system, such as myoblasts and fibroblasts, and expressed at irregular levels by several hemopoietic cell lines, malignant lymphoid cells and myeloma cells. The gene is mapped to human chromosome Xq21-22. Recombinant Human Thymosin-β4 is a 5.2kDa glycoprotein containing 45 amino acid residues.
生物化学的／生理学的作用
In mammalian tissues, thymosin-β4 protein acts as a modulator for the polymerization/depolymerization of actin through the formation of a 1:1 complex with the monomer G (globular)-actin, and inhibits actin′s polymerization to form F (filamentous) actin, which together with other proteins binds microfilaments to construct the cytoskeleton. In addition to regulating actin polymerization, research has also found thymosin-β4 to stimulate the secretion of hypothalamic luteinizing hormone-releasing hormone and luteinizing hormone, inhibit the migration of peritoneal macrophages, induce phenotypic changes in T cell lines during early host defense mechanisms, and inhibit the progression of hematopoietic pluripotent stem cells into the S-phase. It also enhances angiogenesis, endothelial cell migration and adhesion and tubule formation. Thymosin-β4 also participates in wound healing by reducing inflammation and by exhibiting anti-fibrotic effects. It also controls the migration of cancer cells.
物理的形状
Lyophilized with no additives.
再構成
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8 °C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20 °C to -80 °C.
保管分類コード
11 - Combustible Solids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
SRP3324-100UG:
試験成績書（COA）
製品のロット番号・バッチ番号を入力して、試験成績書（COA） を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。
Alexander Belyy et al.
Nature communications, 12(1), 6628-6628 (2021-11-18)
Bacterial human pathogens secrete initially inactive nucleotidyl cyclases that become potent enzymes by binding to actin inside eukaryotic host cells. The underlying molecular mechanism of this activation is, however, unclear. Here, we report structures of ExoY from Pseudomonas aeruginosa and
The actin binding site on thymosin beta4 promotes angiogenesis.
Philp D, et al.
Faseb Journal, 17, 2103-2105 (2003)
Gender, neuroendocrine-immune interactions and neuron-glial plasticity. Role of luteinizing hormone-releasing hormone (LHRH).
Marchetti B, et al.
Annals of the New York Academy of Sciences, 917, 678-709 (2000)
Thymosin beta4: actin-sequestering protein moonlights to repair injured tissues.
Goldstein AL, et al.
Trends in Molecular Medicine, 11, 421-429 (2005)
beta-Thymosins, small acidic peptides with multiple functions.
Huff T, et al.
The International Journal of Biochemistry & Cell Biology, 33, 205-220 (2001)
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