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 |
|
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
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).
- Kumanov, P. et al. (2005) Reprod. Biomed. Online 10:786.
- Maeshima, A. et al. (2008) Endocr. J. 55:1.
- Rodgarkia-Dara, C. et al. (2006) Mutat. Res. 613:123.
- Werner, S. and C. Alzheimer (2006) Cytokine Growth Factor Rev. 17:157.
- Xu, P. and A.K. Hall (2006) Dev. Biol. 299:303.
- Shav-Tal, Y. and D. Zipori (2002) Stem Cells 20:493.
- Chen, Y.G. et al. (2006) Exp. Biol. Med. 231:534.
- Gray, A.M. and A.J. Mason (1990) Science 247:1328.
- Mason, A.J. et al. (1996) Mol. Endocrinol. 10:1055.
- Thompson, T.B. et al. (2004) Mol. Cell. Endocrinol. 225:9.
- Harrison, C.A. et al. (2005) Trends Endocrinol. Metab. 16:73.
- Onichtchouk, D. et al. (1999) Nature 401:480.
- Gray, P.C. et al. (2002) Mol. Cell. Endocrinol. 188:254.
- Kelber, J.A. et al. (2008) J. Biol. Chem. 283:4490.
- Phillips, D.J. et al. (1997) J. Endocrinol. 155:65.
- Schneyer, A. et al. (2003) Endocrinology 144:1671.
- Ghorbani-Dalini, S. et al. (2020) 3 Biotech. 10:215.
- Mennen, R.H. et al. (2022) Reprod Toxicol. 107:44.
- Mishra, S. et al. (2021) Stem Cells. 39:551.
- Tanigawa, S. et al. (2019) Stem Cell Reports 13:322.
- Cangkrama, M. et al. (2020) Trends Mol. Med. 26:1107.
- Ries, A. et al. (2020) Expert Opin. Ther. Targets. 24:985.
- Pinjusic, K. et al. (2022) J. Immunother. Cancer. 10:e004533.
- Dadheech, N. et al. (2020) Stem Cell Res. Ther. 11:327.
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