Activin A is a member of the TGFbeta family of proteins produced by many cell types throughout development. Activins interact with Type I and Type II serine/threonine kinases to signal to SMAD proteins to regulate a variety of functions, including cell proliferation, differentiation, wound healing, apoptosis, metabolism, etc. Activin A is a homodimer of two beta A chains and is not biologically active until the N terminal propeptide is cleaved from each. Human Activin A has 100% amino acid sequence identity to mouse, rat, porcine, bovine and feline proteins. Recombinant human Activin A is a non-glycosylated homodimer, containing two 117aa chains, with a total molecular weight of 26.2kD.
Source:
Recombinant corresponding to human Activin A expressed in E.coli.
Molecular Weight:
~26kD
Biological Activity:
The activity is determined by the ability to induce cytoxicity of MPC-11 cells and is typically less than 2ng/ml.
Endotoxin:
~0.1EU/ug purified protein
Storage and Stability:
Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
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