Recombinant Human Activin C Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Catalog# & Formulation Size Price

Recombinant Human Activin C Protein Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Activin RIIA Fc Chimera (CHO) (Catalog # 340-RC2) is immobilized at 2.5 µg/mL (100 µL/well), the concentration of Recombinant Human Activin C that produces 50% of the optimal binding response is approximately 6‑30 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human Activin C protein
Gly237-Ser352
Accession #
N-terminal Sequence
Gly237
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
INHBC
Purity
>95%, by SDS-PAGE with silver staining
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
12.5 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
13 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 with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE with silver staining
Reconstitution Instructions
Reconstitute at 100 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 Activin C Protein

  • inhibin beta C chain
  • Activin C
  • IHBC
  • INHBC
  • inhibin, beta C

Background

Activins and Inhibins are TGF‑ beta superfamily proteins that regulate a wide range of processes including mesoderm induction, reproductive system development and function, liver growth and regeneration, wound healing, and inflammation. Activins signal through heterodimeric receptor complexes composed of type I (Activin RIA or RIB) and type II (Activin RIIA or RIIB) transmembrane Ser/Thr kinases. There are four human Inhibin beta subunits ( beta A, beta B, beta C, and beta E) and a single Inhibin alpha subunit, each of which adopts a cysteine‑knot structure (1‑3). Activins are disulfide‑linked homodimers or heterodimers of beta subunits, while Inhibins contain the alpha subunit and beta A or  beta B. Human beta C consists of an 18 aa signal sequence, a 218 aa propeptide, and a 116 aa mature segment (4). Mature human beta C shares 51%, 53%, and 64% aa sequence identity with human beta A, beta B, and beta E, respectively. It shares 93% and 91% aa sequence identity with mouse and rat  beta C, respectively. The expression of beta C is restricted compared to the widespread distribution of beta A and beta B. Activin C is expressed as an approximately 20 kDa dimer predominantly by hepatocytes but also by multiple cell types in the male and female reproductive tracts, posterior pituitary and adrenal glands, and nociceptive afferent dorsal root ganglia neurons (5‑7). The beta C subunit regulates Activin induced effects in a variety of systems by forming intracellular dimers with the beta A subunit and impeding the release of Activins A and AB (8, 9). It also functions extracellularly by interfering with Activin A‑receptor interactions (6, 7, 10). beta C can additionally form heterodimers with the beta B or beta E subunits (9, 11, 12).
  1. Butler, C.M. et al. (2005) Cytokine Growth Factor Rev. 16:377.
  2. Werner, S. and C. Alzheimer (2006) Cytokine Growth Factor Rev. 17:157.
  3. Walton, K.L. et al. (2012) Mol. Cell. Endocrinol. 359:2.
  4. Hötten, G. et al. (1995) Biochem. Biophys. Res. Commun. 206:608.
  5. Gold, E.J. et al. (2004) Mol. Cell. Endocrinol. 222:61.
  6. Wada, W. et al. (2004) Am. J. Physiol. Endocrinol. Metab. 287:E247.
  7. Liu, X.-J. et al. (2012) Brain 135:391.
  8. Mellor, S.L. et al. (2003) Endocrinology 144:4410.
  9. Mellor S.L. et al. (2000) J. Clin. Endocrinol. Metab. 85:4851.
  10. Gold, E. et al. (2009) Am. J. Pathol. 174:184.
  11. Vejda, S. et al. (2002) J. Mol. Endocrinol. 28:137.
  12. Wada, W. et al. (2005) Endocr. J. 52:169.

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Bioinformatics

Gene Symbol INHBC
Entrez
Uniprot