Recombinant Human Latent Activin A Protein, CF

  • Purity
    >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
  • Endotoxin Level
    <0.10 EU per 1 μg of the protein by the LAL method.
  • Activity
    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 typically 0.6‑3.6 ng/mL.
  • Source
    Chinese Hamster Ovary cell line, CHO-derived Ser21-Ser426
  • Accession #
  • N-terminal Sequence
    Ser21 (pro) & Gly311 (mature)
  • Predicted Molecular Mass
    32 (pro) & 13 (mature) kDa
    13-16 kDa (mature) and 39 - 46 kDa (pro), reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
Data Images
Recombinant Human Latent Activin A (Catalog #
9129-LA) induces hemoglobin expression in K562 human chronic myelogenous leukemia cells. The ED50 is typically
0.6-3.6 ng/mL.
Background: Activin A
Activin and Inhibin are members of the TGF-beta superfamily of cytokines and are involved in a wide range of biological processes including tissue morphogenesis and repair, fibrosis, inflammation, neural development, hematopoiesis, reproductive system function, and carcinogenesis (1-7). The amino terminal propeptides of Activin and Inhibin are proteolytically cleaved and facilitate formation of disulfide-linked dimers of the bioactive proteins (8, 9). The propeptide of Activin remains associated with the bioactive protein in a latent complex that retains the ability to bind its receptors (10). Activins are nonglycosylated homodimers or heterodimers of various beta  subunits ( beta A, beta B, beta C, and beta E in mammals), while Inhibins are heterodimers of a unique alpha subunit and one of the beta subunits. Activin A is a widely expressed homodimer of two beta A chains. The beta A subunit can also heterodimerize with a beta B or beta C subunit to form Activin AB and Activin AC, respectively (11). The 14 kDa mature human beta A chain shares 100% amino acid sequence identity with bovine, feline, mouse, porcine, and rat beta A. Activin A exerts its biological activities by binding to the type 2 serine/threonine kinase Activin RIIA which then noncovalently associates with the type 1 serine/threonine kinase Activin RIB/ALK-4 (7, 12). Signaling through this receptor complex leads to Smad activation and regulation of activin-responsive gene transcription (7, 12). The bioactivity of Activin A is regulated by a variety of mechanisms (12). BAMBI, Betaglycan, and Cripto are cell-associated molecules that function as decoy receptors or limit the ability of Activin A to induce receptor complex assembly (13-15). The intracellular formation of Activin A can be prevented by the incorporation of the beta A subunit into Activin AC or Inhibin A (3, 11). And the bioavailability of Activin A is restricted by its incorporation into inactive complexes with alpha 2-Macroglobulin, Follistatin, and FLRG (16, 17).
  • References:
    1. Kumanov, P. et al. (2005) Reprod. Biomed. Online 10:786.
    2. Maeshima, A. et al. (2008) Endocr. J. 55:1.
    3. Rodgarkia-Dara, C. et al. (2006) Mutat. Res. 613:123.
    4. Werner, S. and C. Alzheimer (2006) Cytokine Growth Factor Rev. 17:157.
    5. Xu, P. and A.K. Hall (2006) Dev. Biol. 299:303.
    6. Shav-Tal, Y. and D. Zipori (2002) Stem Cells 20:493.
    7. Chen, Y.G. et al. (2006) Exp. Biol. Med. 231:534.
    8. Gray, A.M. and A.J. Mason (1990) Science 247:1328.
    9. Mason, A.J. et al. (1996) Mol. Endocrinol. 10:1055.
    10. Walton, K.L. et al. (2009) J. Biol. Chem. 284:9311.
    11. Thompson, T.B. et al. (2004) Mol. Cell. Endocrinol. 225:9.
    12. Harrison, C.A. et al. (2005) Trends Endocrinol. Metab. 16:73.
    13. Onichtchouk, D. et al. (1999) Nature 401:480.
    14. Gray, P.C. et al. (2002) Mol. Cell. Endocrinol. 188:254.
    15. Kelber, J.A. et al. (2008) J. Biol. Chem. 283:4490.
    16. Phillips, D.J. et al. (1997) J. Endocrinol. 155:65.
    17. Schneyer, A. et al. (2003) Endocrinology 144:1671.
  • Entrez Gene IDs:
    3624 (Human); 16323 (Mouse)
  • Alternate Names:
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