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Recombinant Human Inhibin A Protein, CF

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Recombinant Human Inhibin A (Cat# 8506-AB/CF) neutralizes Activin-mediated erythroid differentiation of K562 human chronic myelogenous leukemia cells. The ED50 for this effect is 3‑18 ng/mL.
Recombinant Human Inhibin A (Cat# 8506-AB/CF) neutralizes Activin-mediated erythroid differentiation of K562 human chronic myelogenous leukemia cells. The ED50 for this effect is 3‑18 ng/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Inhibin A Protein, CF Summary

Details of Functionality
Measured by its ability to neutralize Activin-mediated erythroid differentiation of K562 human chronic myelogenous leukemia cells. The ED50 for this effect is 3-18 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human Inhibin A protein
Ser233-Ile366 (alpha chain) & Gly311-Ser426 (beta chain)
Accession #
N-terminal Sequence
Ser233 (alpha chain) & Gly311 (beta chain)
Structure / Form
Disulfide-linked heterodimer
Protein/Peptide Type
Recombinant Proteins
Gene
INHA
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

Dilutions
  • Bioactivity
Theoretical MW
15 kDa (alpha chain) & 13 kDa (beta chain).
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
12-25 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 250 μg/mL in 4 mM HCl.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Inhibin A Protein, CF

  • A-inhibin subunit
  • INHA
  • Inhibin A
  • inhibin alpha chain
  • inhibin, alpha

Background

Inhibin A is a member of the TGF-beta superfamily of proteins (1). Mature Inhibin A is a disulfide-linked dimer composed of alpha and beta  subunits (1). Inhibin A shares a common alpha  subunit with the closely related protein Inhibin B but has a unique beta  subunit ( beta A) (2, 3). The mature alpha  subunit of human Inhibin A has a predicted molecular weight of 18 kDa and shares 80% amino acid (aa) sequence identity with the mouse and rat orthologs (2, 4). The mature beta  subunit of this human protein has a predicted molecular weight of 13 kDa and shares 100% aa sequence identity with the mouse and rat orthologs. Inhibin binds and antagonizes ActRIIA and ActRIIB in complex with the TGF-beta RIII and/or IGSF1 co-receptors and subsequently acts to suppress Activin-induced Follicle Stimulating Hormone (FSH) secretion (1, 5-7). Inhibins are produced by gonadal cells in both males and females (8). They are thought to be involved in the regulation of gametogenesis, and embryonic and fetal development (8, 9). Elevated concentrations of Inhibins are associated with pregnancy, preeclampsia, and ovarian cancer, and Inhibin A levels are typically measured during prenatal screening for Down’s syndrome (10-14).
  1. Phillips, D.J. and T.K. Woodruff (2004) Growth Factors 22:13.
  2. Mason, A.J. et al. (1986) Biochem. Biophys. Res. Commun. 135:957.
  3. Ying, S.Y. (1987) Proc. Soc. Exp. Biol. Med. 186:253.
  4. Mayo, K.E. et al. (1986) Proc. Natl. Acad. Sci. USA 83:5849.
  5. Lewis, K.A. et al. (2000) Nature 404:411.
  6. Martens, J.W. et al. (1997) Endocrinology 138:2928.
  7. Chapman, S.C. et al. (2002) Mol. Cell. Endocrinol. 196:79.
  8. de Kretser, D.M. and D.M. Robertson (1989) Biol. Reprod. 40:33.
  9. Knight, P.G. et al. (2012) Mol. Cell. Endocrinol. 359:53.
  10. Walentowicz, P. et al. (2014) PLoS One 9:e90575.
  11. Kondi-Pafiti, A. et al. (2013) Clin. Exp. Obstet. Gynecol. 40:109.
  12. Kuijper, E.A. et al. (2013) Reprod. Biomed. Online 27:33.
  13. Carty, D.M. et al. (2008) Trends Cardiovasc. Med. 18:186.
  14. Wald, N.J. et al. (1996) Prenat. Diagn. 16:143.

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