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Key Documents

SRP3324

Sigma-Aldrich

Thymosin β4 human

recombinant, expressed in E. coli, ≥95% (SDS-PAGE), ≥95% (HPLC)

Sinonimo/i:

Hematopoietic system regulatory peptide, Seraspenide, T-4

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About This Item

Codice UNSPSC:
12352202
NACRES:
NA.32

Origine biologica

human

Ricombinante

expressed in E. coli

Saggio

≥95% (HPLC)
≥95% (SDS-PAGE)

Forma fisica

lyophilized

Potenza

0.5-10 μg/mL

PM

5.2 kDa

Confezionamento

pkg of 100 μg

Impurezze

endotoxin, tested

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

Informazioni sul gene

human ... TMSB4X(7114)

Descrizione generale

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.

Azioni biochim/fisiol

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.

Stato fisico

Lyophilized with no additives.

Ricostituzione

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.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

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The actin-sequestering protein thymosin beta-4 is a novel target of hypoxia-inducible nitric oxide and HIF-1a regulation.
Ryu YK, et al.
PLoS ONE, 9, e106532-e106532 (2014)
Thymosin ?4-sulfoxide attenuates inflammatory cell infiltration and promotes cardiac wound healing.
Evans MA, et al.
Nature Communications, 4, 2081-2081 (2013)
The actin binding site on thymosin beta4 promotes angiogenesis.
Philp D, et al.
Faseb Journal, 17, 2103-2105 (2003)
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
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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