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.
12 kDa, reducing conditions
Read Publications using 8260-AB/CF in the following applications:
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.
>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, CF
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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