Recombinant Human/Mouse/Rat Activin A GMP Protein, CF

Catalog #: 338-GMP Datasheet / COA / SDS

Catalog #	Availability	Size / Price	Qty
338-GMP-010
338-GMP-050
338-GMP-01M

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Recombinant Human/Mouse/Rat Activin A GMP Protein Bioactivity

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

Recombinant Human/Mouse/Rat Activin A GMP Protein, CF Summary

Product Specifications

Purity

>97%, by SDS-PAGE with silver 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 0.2-1.2 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

Chinese Hamster Ovary cell line, CHO-derived Activin A protein
Gly311-Ser426
Manufactured and tested under cGMP guidelines.

Accession #

P08476.2

N-terminal Sequence
Analysis

Gly₃₁₁-Leu-Glu-(Cys)-Asp-Gly-Lys-Val-Asn-Ile

Structure / Form

Disulfide-linked homodimer

Predicted Molecular Mass

13 kDa (monomer)

SDS-PAGE

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

Product Datasheets

338-GMP

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.

338-GMP

Formulation	Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
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. A minimum of 12 months when stored at ≤ -20 °C as supplied. Refer to lot specific COA for the Use by Date. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, ≤ -20 °C under sterile conditions after reconstitution.

Scientific Data

Bioactivity

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GMP-grade Recombinant Human/Mouse/Rat Activin A (Catalog # 338‑GMP) induces hemoglobin expression in K562 human chronic myelogenous leukemia cells in a dose-dependent manner. The ED₅₀ for this effect is 0.2‑1.2 ng/mL.

SDS-PAGE

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1 μg/lane of GMP-grade Recombinant Human/ Mouse/Rat Activin A (Catalog # 338‑GMP) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing single bands at 14 kDa and 24 kDa, respectively.

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

GMP Proteins
R&D Systems, a Bio-Techne Brand's GMP proteins are produced according to relevant sections of the following documents: USP Chapter 1043, Ancillary Materials for Cell, Gene and Tissue-Engineered Products and Eu. Ph. 5.2.12, Raw Materials of Biological Origin for the Production of Cell-based and Gene Therapy Medicinal Products.

R&D Systems' quality focus includes:

Designed, manufactured and tested under an ISO 9001:2015 and ISO 13485:2016 certified quality system
Documented and controlled manufacturing process
Control of documentation and process changes by QA
Personnel training programs
Raw material inspection and vendor qualification/monitoring program
Validated equipment, processes and test methods
Equipment calibration and maintenance schedules using a Regulatory Asset Manager
Facility/Utilities maintenance, contamination controls, safety and pest control programs
Material review process for variances
Robust product stability program following relevant ICH guidelines

R&D Systems strives to provide our customers with the analytical characteristics of each product so that customers may determine whether our products are appropriate for their application. Each product is provided with a lot-specific Certificate of Analysis that contains the product's specifications and test results. Quality control testing may include, but is not limited to:

N-terminal amino acid analysis
SDS-PAGE purity analysis
Molecular weight analysis via mass spectrometry
Endotoxin assessment per USP <85> and Ph. Eur. 2.6.14 guidelines
Bioassay analysis
Microbial testing per USP <71> and Ph. Eur. 2.6.1 guidelines
Host cell protein assessment
Host cell DNA assessment
Mycoplasma assessment

Additional testing and documentation requested by the customer can be arranged at an additional cost.

Production records and facilities are available for examination by appropriate personnel on-site at R&D Systems in Minneapolis and St. Paul, Minnesota USA.

R&D Systems sells GMP grade products for preclinical or clinical ex vivo use. They are not for in vivo use. Please read the following End User Terms prior to using this product.