Recombinant Human Activin AC Heterodimer Protein, CF


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Recombinant Human Activin AC Heterodimer Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. In a 100 µL reaction mixture containing rhActivin AC at 2 nM and rhActivin RIIB/Fc Chimera dilutions at 0.02-41 nM, the concentration of rhActivin RIIB/Fc Chimera (Catalog # 339-RBB) that produces 50% of the optimal binding response is found to be approximately 0.8-4 nM.
Chinese Hamster Ovary cell line, CHO-derived human Activin AC protein
Human Activin beta A
(Gly311 - Ser426)
Accession # NP_002183
Human Activin beta C
(Gly237 - Ser352)
Accession # NP_005529
N-terminus C-terminus
Accession #
N-terminal Sequence
Gly311 ( beta A subunit) & Gly237 ( beta C subunit)
Structure / Form
Disulfide-linked heterodimer
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


Theoretical MW
12.9 kDa ( beta A subunit), 12.5 kDa ( beta C subunit).
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.
23 kDa, reducing conditions
Read Publications using
4879-AC/CF in the following applications:

Packaging, Storage & Formulations

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 under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCI.


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

Alternate Names for Recombinant Human Activin AC Heterodimer Protein, CF

  • Activin AC


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 and inhibins share a variety of beta  subunits, while inhibins also possess a unique alpha subunit. 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 - 5). Activin AC is a 23 kDa heterodimer of beta A and beta C subunits (6). Human  beta A consists of a 20 amino acid (aa) signal sequence, a 290 aa propeptide, and a 116 aa mature segment, while beta C consists of an 18 aa signal sequence, a 218 aa propeptide, and a 116 aa mature segment (8, 9). The subunit  beta propeptides are required for subunit folding, dimerization, and secretion (10). Mature human beta A shares 64%, 51%, and 44% aa sequence identity with human beta B, beta C, and beta E, respectively. Sequence identity between human, mouse, and rat is 100% for mature beta A, and 91% - 93% for mature  beta C. The beta A and beta C subunits are both expressed in the liver, pituitary, ovary, testis, and adrenal gland (1, 6, 11). The beta C subunit may dimerize with beta A, beta B or the inhibin alpha  subunit (6, 7). Overexpression of  beta C results in increased production of Activin AC as well as a reduction in beta A expression and activin induced signaling (12, 13). The beta C subunit modulates activin induced effects in a variety of systems by forming intracellular dimers with the beta A subunit and impeding the release of Activins A, AB, and B (2, 12). 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.

  1. Thompson, T.B. et al. (2004) Mol. Cell. Endocrinol. 225:9. 
  2. Butler, C.M. et al. (2005) Cytokine Growth Factor Rev. 16:377. 
  3. Abe, Y. et al. (2004) Growth Factors 22:105. 
  4. Vitt, U.A. et al. (2001) Mol. Endocrinol. 15:681. 
  5. Werner, S. and C. Alzheimer (2006) Cytokine Growth Factor Rev. 17:157. 
  6. Mellor S.L. et al. (2000) J. Clin. Endocrinol. Metab. 85:4851.  
  7. Ushiro, Y. et. al. (2006) J. Reprod. Devel. 52:487.
  8. Mason, A.J. et al. (1986) Biochem. Biophys. Res. Commun. 135:957.
  9. Hötten, G. et al. (1995) Biochem. Biophys. Res. Commun. 206:608.
  10. Gray, A.M. and A.J. Mason (1990) Science 247:1328.
  11. Gold, E.J. et al. (2004) Mol. Cell. Endocrinol. 222:61.
  12. Mellor, S.L. et al. (2003) Endocrinology 144:4410.
  13. Wada, W. et al. (2004) Am. J. Physiol. Endocrinol. Metab. 287:E247.

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