Recombinant Human Latent Activin A Protein, CF

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Recombinant Human Latent Activin A Protein Bioactivity
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Recombinant Human Latent Activin A Protein, CF Summary

Product Specifications

>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.
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 0.600‑3.60 ng/mL.
Chinese Hamster Ovary cell line, CHO-derived human Activin A protein
Accession #
N-terminal Sequence
Ser21 (pro) & Gly311 (mature)
Structure / Form
Noncovalently-linked complex between disulfide-linked homodimer of the mature domain and noncovalently-linked homodimer of the prodomain
Predicted Molecular Mass
32 kDa (pro) & 13 kDa (mature)
13-16 kDa (mature) and 39 - 46 kDa (pro), reducing conditions

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Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.


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.

Scientific Data

Bioactivity Recombinant Human Latent Activin A Protein Bioactivity View Larger

Recombinant Human Latent Activin A (Catalog # 9129-LA) induces hemoglobin expression in K562 human chronic myelogenous leukemia cells. The ED50 is 0.600-3.60 ng/mL.

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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). Activin and Inhibin are produced as precursor proteins. Their amino terminal propeptides are proteolytically cleaved and facilitate formation of disulfide-linked dimers of the bioactive proteins (8, 9). 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 (10). 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, 11). Signaling through this receptor complex leads to Smad activation and regulation of activin-responsive gene transcription (7, 11). The bioactivity of Activin A is regulated by a variety of mechanisms (11). 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 (12‑14). The intracellular formation of Activin A can be prevented by the incorporation of the beta A subunit into Activin AC or Inhibin A (3, 10). And the bioavailability of Activin A is restricted by its incorporation into inactive complexes with alpha 2-Macroglobulin, Follistatin, and FLRG (15, 16). 

Activin A is involved in the differentiation of various cell and tissue types. The induction of definitive endoderm by Activin A is required in differentiation protocols of induced pluripotent stem cells (iPSCs) (17, 18). In vitro models of human gametogenesis use prolonged Activin A supplementation to human embryonic stem cells for differentiation into human primordial germ cell-like cells (19). Activin A can also be used to maintain cells in vitro, as is the case for iPSC-derived nephron cells that can then be used in disease modeling, drug screening and in regenerative medicine (20). 

Activin A is an important factor for tumor cells to evade the immune system as Activin A can act on surrounding immune cells to decrease their antitumor activity (21). Activin A also promotes migration and growth of tumors, making it a target for cancer therapies (22). Specifically, research has shown that interfering with Activin A activity can assist in overcoming CD8 T-cell exclusion and immunotherapy resistance (23). In bone marrow-derived stem cell transplants for treatment of diabetes, Activin A enhances migration and homing of stem cells towards pancreatic lineage (24).

  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. Thompson, T.B. et al. (2004) Mol. Cell. Endocrinol. 225:9.
  11. Harrison, C.A. et al. (2005) Trends Endocrinol. Metab. 16:73.
  12. Onichtchouk, D. et al. (1999) Nature 401:480.
  13. Gray, P.C. et al. (2002) Mol. Cell. Endocrinol. 188:254.
  14. Kelber, J.A. et al. (2008) J. Biol. Chem. 283:4490.
  15. Phillips, D.J. et al. (1997) J. Endocrinol. 155:65.
  16. Schneyer, A. et al. (2003) Endocrinology 144:1671.
  17. Ghorbani-Dalini, S. et al. (2020) 3 Biotech. 10:215.
  18. Mennen, R. H. et al. (2022) Reprod Toxicol. 107:44.
  19. Mishra, S. et al. (2021) Stem Cells. 39:551.
  20. Tanigawa, S. et al. (2019) Stem Cell Reports 13:322.
  21. Cangkrama, M. et al. (2020) Trends Mol. Med. 26:1107.
  22. Ries, A. et al. (2020) Expert Opin. Ther. Targets. 24:985.
  23. Pinjusic, K. et al. (2022) J. Immunother. Cancer. 10:e004533.
  24. Dadheech, N. et al. (2020) Stem Cell Res. Ther. 11:327. 
Entrez Gene IDs
3624 (Human); 16323 (Mouse); 29200 (Rat)
Alternate Names
Activin A; activin AB alpha polypeptide; Activin beta-A chain; erythroid differentiation factor; Erythroid differentiation protein; follicle-stimulating hormone-releasing protein; FSH-releasing protein; inhibin beta A chain; inhibin beta A subunit; Inhibin, beta-1


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