Recombinant Mouse Activin B Protein, CF

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Recombinant Mouse Activin B (Catalog # 8260-AB/CF) induces hemoglobin expression in K562 human chronic myelogenous leukemia cells. The ED50 for this effect is 0.2-1.2 ng/mL.
1 μg/lane ofRecombinant Mouse Activin Bwas resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditionsand visualized by silver staining, showing bands at 12 and 21 kDa, respectively.

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Mouse Activin B Protein, CF 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 0.2‑1.2 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived mouse Activin B protein
Gly297-Ala411
Accession #
N-terminal Sequence
Gly297
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Inhbb
Purity
>95%, by SDS-PAGE with silver staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
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.
SDS-PAGE
12 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
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 HCl.
Purity
>95%, by SDS-PAGE with silver staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCl.

Notes

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 B
  • INHBB
  • inhibin, beta B

Background

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).
  1. Woodruff, T.K. (1998) Biochemical Pharmacology 55:953.
  2. Paulusma, C.C. et al. (1994) J. Immunol. Methods 169:143.
  3. Vassalli, A. et al. (1994) Genes Dev. 8:414.
  4. Shat-Tal, Y. and D. Zipori (2002) Stem Cells 20:493.
  5. Ying, S.Y. et al. (1997) Proc. Soc. Exp. Biol. Med. 214:114.
  6. Gray, A.M. and A.J. Mason (1990) Science 247:1328.
  7. Mason, A.J. et al. (1996) Mol. Endocrinol. 10:1055.
  8. de Caestecker, M. (2004) Cytokine Growth Factor Rev. 15:1.
  9. Hedger, M.P. and D.M. de Kretser (2013) Cytokine Growth Factor Rev. 24: 285.
  10. Gray, P.C. and W. Vale (2012) FEBS Letters 586:1836.
  11. Kelber, J.A. et al. (2008) J. Biol. Chem. 283: 4490.
  12. Xia, Y. and A.L. Schneyer (2009) Journal of Endocrinology 202:1.

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Bioinformatics

Gene Symbol Inhbb
Uniprot