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Recombinant Human/Mouse Activin A PLUS, Animal-Free Protein

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Activin A PLUS activity is determined using an activin-responsive firefly luciferase reporter in HEK293T cells. in triplicate) with a serial dilution of activin A for 6 hours. Firefly luciferase activity is measured ...read more
Activin A PLUS migrates as a single band at 24 kDa in non-reducing (NR) and 13 kDa as a single monomeric species upon reduction (R). No contaminating protein bands are visible.Purified recombinant protein (7 µg) was ...read more

Product Details

Summary
Reactivity Hu, Mu, Rt, Po, BvSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human/Mouse Activin A PLUS, Animal-Free Protein Summary

Additional Information
Human/Mouse/Rat/Bovine/Porcine
Details of Functionality
No significant difference between EC50 of reference and test lots
Source
E. coli-derived Activin A protein
Accession #
Protein/Peptide Type
Animal-Free Recombinant Proteins
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
24 kDa (dimer).
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
Dimeric Activin A PLUS protein only

Packaging, Storage & Formulations

Storage
Store lyophilized protein between -20 and -80 °C until the date of expiry. Avoid freeze-thaw cycles.
Buffer
Lyophilized from acetonitrile/TFA
Reconstitution Instructions
Resuspend in 10mM HCl at >100 µg/ml, prepare single use aliquots, add carrier protein if desired

Notes

The above product was manufactured, tested and released by R&D System's contract manufacturer, Qkine Ltd, at 1 Murdoch House, Cambridge, UK, CB5 8HW. The product is for research use only and not for the diagnostic or theraputic use.

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

Alternate Names for Recombinant Human/Mouse Activin A PLUS, Animal-Free Protein

  • 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

Background

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.

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