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Recombinant Human Activin B Protein Summary
Details of Functionality
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 0.3‑1.5 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human Activin B protein Gly293-Ala407
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
12.8 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.
SDS-PAGE
12.4 kDa, reducing conditions
Publications
Read Publications using 659-AB 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.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 50 μg/mL in 4 mM HCl containing at least 0.1% human or bovine serum albumin.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Activin B Protein
activin AB beta polypeptide
Activin Beta B
Activin beta-B chain
INHBB
inhibin beta B chain
Inhibin Beta B
Inhibin Subunit Beta B
inhibin, beta B (activin AB beta polypeptide)
inhibin, beta B
Inhibin, beta-2
Background
Activins and inhibins, members of the TGF-beta superfamily, are disulfide-linked dimeric proteins that were originally purified from gonadal fluids as proteins that stimulated or inhibited, respectively, pituitary follicle stimulating hormone (FSH) release. These proteins have since been shown to have a wide range of biological activities including: mesoderm induction, neural cell differentiation, bone remodeling, hematopoiesis and reproductive physiology. Activins/inhibins are produced as precursor proteins with an amino-terminal propeptide that is cleaved to release the carboxy-terminal bioactive ligands. Activins are homodimers or heterodimers of the various beta subunit isoforms, while inhibins are heterodimers of a unique alpha subunit and one of the various beta subunits. Five beta subunits (mammalian beta A, beta B, beta C, beta E and Xenopus beta D) have been cloned. The activin/inhibin nomenclature reflects the subunit composition of the proteins: activin A ( beta A - beta A), activin B ( beta B - beta B), activin AB ( beta A ‑ beta B), inhibin A ( alpha - beta A) and inhibin B ( alpha - beta B). At present, little is known about the contribution of the other beta subunits to activin or inhibin formation and biology. At the amino acid sequence level, the mature human beta B subunit is greater than 98% identical to mouse beta B, while the human and mouse alpha subunits share approximately 80% identity. Similarly to other TGF-beta family members, activins exert their biological activities through binding to the heterodimeric complex composed of two membrane spanning serine-threonine kinases designated as type I and type II. Two forms of activin receptor type I (Act RI-A and Act RI-B) and two forms of activin receptor type II (Act RII-A and Act RII-B) have been identified. Activin binds directly to Act RII, the complex then associates with Act RI and initiates signaling. Besides activins, Act RII has been shown to bind certain other TGF-beta superfamily members. Inhibin A has been shown to bind with low‑affinity to Act RII. The existence of a distinct inhibin-specific receptor and/or signal transduction pathway has been hypothesized.
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