Activin A, rat recombinant protein
Inhibin beta-1, FRP, FSH-releasing protein
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P08476 |
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Calculated MW | 26.2 kDa |
Gene ID | 3624 |
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Gene Symbol | INHBA |
Other Names | Inhibin beta-1, FRP, FSH-releasing protein |
Gene Source | Rat |
Source | E. coli |
Assay&Purity | SDS-PAGE; ≥95% |
Assay2&Purity2 | HPLC; ≥95% |
Recombinant | Yes |
Results | < 2 ng/mL |
Sequence | MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS |
Application Notes | Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. It is recommended to reconstitute the lyophilized product with sterile water, which can then be further diluted to other aqueous solutions. |
Format | Lyophilized protein |
Storage | -20°C; Recombinant rat Activin A is lyophilized with 0.02% TFA. |
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Provided below are standard protocols that you may find useful for product applications.
Background
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. Rat Activin A has 100% amino acid sequence identity to human, mouse, porcine, bovine and feline proteins. Recombinant rat Activin A is a non-glycosylated homodimer, containing two 117 amino acid chains, with a total molecular weight of 26.2 kDa.
References
Mason A.J.,et al.Biochem. Biophys. Res. Commun. 135:957-964(1986).
Murata M.,et al.Proc. Natl. Acad. Sci. U.S.A. 85:2434-2438(1988).
Tanimoto K.,et al.DNA Seq. 2:103-110(1991).
Hillier L.W.,et al.Nature 424:157-164(2003).
Stewart A.G.,et al.FEBS Lett. 206:329-334(1986).
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