1 μg/lane of Recombinant Human/Mouse/Rat Activin A 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, ...read more
Recombinant Human/Mouse/Rat Activin A (Catalog # 338-AC/CF) induces hemoglobin expression in K562 human chronic myelogenous leukemia cells. The ED50 is 0.2‑1.2 ng/mL.
BG01V human embryonic stem cells were differentiated into endoderm using media supplemented with Recombinant Human/Mouse/Rat Activin A (Catalog # 338-AC). Control cells were cultured in medium without recombinant ...read more
Recombinant Human/Mouse/Rat Activin A Protein, CF Summary
Details of Functionality
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 2.5 x 103 units/mg, which is calibrated against human Activin A
WHO International Standard (NIBSC code: 91/626). Specific activity is for reference purposes only and is not routinely tested.
Chinese Hamster Ovary cell line, CHO-derived Activin A protein Gly311-Ser426
<0.01 EU per 1 μg of the protein by the LAL method.
13 kDa (monomer). 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.
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.
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
>95%, by SDS-PAGE with silver staining.
Reconstitute at 100-500 µg/mL in sterile 4 mM HCl.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human/Mouse/Rat Activin A Protein, CF
activin AB alpha polypeptide
Activin beta-A chain
erythroid differentiation factor
Erythroid differentiation protein
follicle-stimulating hormone-releasing protein
inhibin beta A chain
inhibin beta A subunit
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).
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