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Key Documents

SRP3324

Sigma-Aldrich

Thymosin β4 human

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

Sinónimos:

Hematopoietic system regulatory peptide, Seraspenide, T-4

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About This Item

Código UNSPSC:
12352202
NACRES:
NA.32

origen biológico

human

recombinante

expressed in E. coli

Análisis

≥95% (HPLC)
≥95% (SDS-PAGE)

formulario

lyophilized

potencia

0.5-10 μg/mL

mol peso

5.2 kDa

envase

pkg of 100 μg

impurezas

endotoxin, tested

Nº de acceso UniProt

Condiciones de envío

wet ice

temp. de almacenamiento

−20°C

Información sobre el gen

human ... TMSB4X(7114)

Descripción general

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.

Acciones bioquímicas o fisiológicas

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.

Forma física

Lyophilized with no additives.

Reconstitución

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.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» 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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