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

Catalog #: AFL338 Datasheet / COA / SDS

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Catalog #	Availability	Size / Price	Qty
AFL338-050
AFL338-01M
AFL338-250

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

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

Learn more about Animal-Free Recombinant Proteins

Animal Free Proteins
Animal-free proteins are particularly important for researchers concerned with experimental variables caused by trace animal components or mammalian pathogens. Our products generated under animal-free conditions share the same biological activities as those produced using our standard laboratory techniques.

Product Specifications

Purity

>95%, 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.

Activity

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 0.200-1.20 ng/mL.
The specific activity of Recombinant Human/Mouse/Rat Activin A is >1000 units/mg, which is calibrated against the human Activin A WHO reference standard (NIBSC code: 91/626).

Source

E. coli-derived Activin A protein
Gly311-Ser426
Produced using non-animal reagents in an animal-free laboratory.

Accession #

P08476

N-terminal Sequence
Analysis

Gly311

Structure / Form

Disulfide-linked homodimer

Predicted Molecular Mass

13 kDa (monomer)

SDS-PAGE

14 kDa, reducing conditions
24 kDa, non-reducing conditions

Product Datasheets

AFL338

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.

AFL338

Formulation	Lyophilized from a 0.2 μm filtered solution in HCl.
Reconstitution	Reconstitute at 100-500 μg/mL in sterile 4 mM HCl.
Shipping	The product is shipped with polar packs. 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.

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

Manufacturing Specifications

Animal-Free Manufacturing Conditions
Our dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.

Production

All molecular biology procedures use animal-free media and dedicated labware.
Dedicated fermentors are utilized in committed animal-free areas.

Purification

Protein purification columns are animal-free.
Bulk proteins are filtered using animal-free filters.
Purified proteins are stored in animal-free containers in a dedicated cold storage room.

Quality Assurance

Low Endotoxin Level.
No impairment of biological activity.
High quality product obtained under stringent conditions.
For ex vivo research or bioproduction, additional documentation can be provided.

Please read our complete Animal-Free Statement