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

Catalog #: Qk005 Datasheet / COA / SDS

Human/Mouse/Rat/Bovine/Porcine

Catalog #	Availability	Size / Price	Qty
Qk005-0050
Qk005-0500

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

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Product Details

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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

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

Product Specifications

Endotoxin Level

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

Activity

No significant difference between EC₅₀ of reference and test lots

Source

E. coli-derived Activin A protein

Accession #

P08476.2

Predicted Molecular Mass

24 kDa (dimer)

SDS-PAGE

Dimeric Activin A PLUS protein only

Product Datasheets

QK005

Product Datasheet

COA

SDS

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.

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.

Scientific Data

Bioactivity

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

SDS-PAGE

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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.

Reconstitution Calculator

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).

References

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.

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

Product Specific Notices

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.