Measured by its ability to induce hemoglobin expression in K562 human chronic myelogenous leukemia cells. Schwall, R.H. et al. (1991) Method Enzymol. 198:340. The ED50 for this effect is 0.2-1.2 ng/mL.
Human embryonic kidney cell, HEK293-derived mouse Activin B protein Gly297-Ala411
<0.10 EU per 1 μg of the protein by the LAL method.
13 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein.
>95%, by SDS-PAGE with silver staining.
Reconstitute at 100 μg/mL in sterile 4 mM HCl.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Activin B Protein
activin AB beta polypeptide
Activin beta-B chain
inhibin beta B chain
inhibin, beta B (activin AB beta polypeptide)
inhibin, beta B
Activin and Inhibin, members of the TGF-beta superfamily of cytokines, are involved in a range of biological processes including neural development, stem cell differentiation, reproductive physiology, inflammation, tissue morphogenesis and bone remodeling (1-5). Activins function as either a homodimer or heterodimer of non-glycosylated beta subunit proteins ( beta A, beta B, beta C, and beta E in mammals). Inhibins are heterodimers consisting of a unique alpha subunit and any one beta subunit. The alpha - and beta -subunits are produced as precursor proteins with an amino-terminal propeptide that is cleaved to release a carboxy-terminal monomeric subunit that becomes bioactive upon disulfide linkage with another Activin monomer (6, 7). The bioactive Activin B dimeric protein consists of two beta B subunits. The 13 kDa mature mouse Activin beta B subunit shares 99% and 98% amino acid sequence identity with rat and human Activin beta B, respectively. Activin B exerts its biological function upon binding to the type 2 serine/threonine kinase Activin receptor (Act RIIA). This receptor-ligand complex noncovalently associates and transphosphorylates the type 1 Activin receptor (ActRI) to initiate intracellular SMAD activation and the subsequent regulation of Activin-responsive gene transcription (8). BAMBI, Betaglycan, and Cripto, regulate the bioactivity of Activin B by restricting its ability to induce receptor complex assembly. Alternatively, bioavailability of Activin B is modulated through sequestration into inactive complexes with alpha 2-Macroglobulin, Follstatin, and FLRG (9-12).
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