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

R&D Systems, part of Bio-Techne | Catalog # Qk005

Human/Mouse/Rat/Bovine/Porcine
R&D Systems, part of Bio-Techne
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Qk005-0050
Qk005-0500
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Key Product Details

Source

E. coli

Accession #

P08476.2

Conjugate

Unconjugated

Applications

Bioactivity

View all Activin A Proteins and Enzymes »

Product Specifications

Source

E. coli-derived Activin A protein

Purity

Single species with expected mass

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

Predicted Molecular Mass

24 kDa (dimer)

SDS-PAGE

Dimeric Activin A PLUS protein only

Activity

No significant difference between EC50 of reference and test lots

Scientific Data Images for Recombinant Human/Mouse Activin A PLUS, Animal-Free Protein

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

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 and normalized to the control Renilla luciferase activity.EC50 = 0.103 ng/ml (4.24 pM).

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

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 resolved using 15% w/v SDS-PAGE in reduced (+ beta-mercaptothanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250.

Formulation, Preparation and Storage

Qk005
Formulation Lyophilized from acetonitrile/TFA
Reconstitution Resuspend in 10mM HCl at >100 µg/ml, prepare single use aliquots, add carrier protein if desired
Shipping The product is shipped lyophilized at ambient temperture, on ice blocks or dry ice. Shipping at ambient temperture does not affect the bioactivity or stability of the protein. Upon reciept, store immediately at the conditions stated below.
Stability & Storage Store lyophilized protein between -20 and -80 °C until the date of expiry. Avoid freeze-thaw cycles.

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 ( betaA, betaB, betaC, and betaE 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 betaA chains. The betaA subunit can also heterodimerize with a betaB or betaC subunit to form Activin AB and Activin AC, respectively (10). The 14 kDa mature human betaA chain shares 100% amino acid sequence identity with bovine, feline, mouse, porcine, and rat betaA. 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 betaA subunit into Activin AC or Inhibin A (3, 10). And the bioavailability of Activin A is restricted by its incorporation into inactive complexes with alpha2-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).

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. 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.

Alternate Names

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

Entrez Gene IDs

3624 (Human); 16323 (Mouse); 29200 (Rat)

Gene Symbol

INHBA

UniProt

P08476.2

Additional Activin A Products

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

Product Datasheets

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human/Mouse Activin A PLUS, Animal-Free Protein

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.

For research use only

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