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

  
  • 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 approximately 1 IU/μg, which is calibrated against human Activin A WHO International Standard (NIBSC code: 91/626).
  • Source
    Chinese Hamster Ovary cell line, CHO-derived Gly311-Ser426 Manufactured and tested under cGMP guidelines.
  • Accession #
  • 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
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 at ambient temperature. 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.
Data Images
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.
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.
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).
  • 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.
  • Entrez Gene IDs:
    3624 (Human); 16323 (Mouse)
  • Alternate Names:
    Activin A; INHBA

GMP Proteins
R&D Systems''' GMP proteins are produced according to relevant sections of the following documents: WHO TRS, No. 822, 1992 Annex 1, Good Manufacturing Practices for Biological Products; USP Chapter 1043, Ancillary Materials for Cell, Gene and Tissue-Engineered Products and USP Chapter 92, Growth Factors and Cytokines Used in Cell Therapy Manufacturing.

R&D Systems''' quality focus includes:
  • Manufactured and tested under an ISO 9001:2008 and ISO 13485:2003 certified quality system
  • Documented processes and QA control of documentation and process changes
  • Personnel training programs
  • Raw material testing and vendor qualification/monitoring
  • Fully validated equipment, processes and test methods
  • Equipment calibration schedules using a computerized calibration program
  • Facility maintenance, safety programs and pest control
  • Material review process for variances
  • Monitoring of stability over product shelf-life

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 research. The Certificate of Analysis provided contains the following lot specific information:

  • N-terminal amino acid analysis, SDS-PAGE analysis, and endotoxin level (as determined by LAL assay) performed on each bulk QC lot, not on individual bottlings of each QC lot
  • Post-bottling lot-specific bioassay results (compliance with an established range) and results of microbial bioburden testing (using broth culture, Sabourand'''s dextrose and blood agar plates with results reported at 3 days and at 7 days)

Additional testing and documentation requested by the customer can be arranged at an additional cost. Testing may include, but is not limited to, USP sterility testing, positive identity testing, testing for adventitious agents and testing for residual host cell content.

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

R&D Systems sells its GMP grade recombinant protein products for research use or further manufacturing use in ex vivo cell therapy applications. They are not for in vivo use or for use as therapeutic or other drugs, biologic products or devices. Please read the following End User Terms prior to using this product.

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