Specifications
- SPECIES: Human
- SOURCE SPECIES: CHO cells
- RECOMBINANT PROTEIN SEQUENCE: GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS
- BIOLOGICAL ACTIVITY: Determined by its ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 is ≤ 2.0 ng/ml, corresponding to a specific activity of ≥ 5 x 105 units/mg.
Properties
- PURITY: ≥ 95% by SDS-PAGE gel and HPLC analyses.
- PHYSICAL STATE: Lyophilized
- STORAGE CONDITIONS: The recombinant protein is stable for at least 2 years from date of receipt at -20°C. Reconstituted protein is stable for at least 3 months when stored in working aliquots with a carrier protein at -20°C. As with any protein, exposing the recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.
Additional Info
- NCBI OFFICIAL SYMBOL: ACVR2A
- ADDITIONAL NAMES: Inhibin beta-1, FRP, FSH (Follicle-stimulating hormone)-releasing protein
- NCBI GENE ID NUMBER: 92
Background
- Activin A is a TGF-β family member that exhibits a wide range of biological activities, including regulation of cellular proliferation and differentiation, and promotion of neuronal survival. Elevated levels of Activin A in human colorectal tumors and in postmenopausal women have been implicated in colorectal and breast cancers, respectively. The biological activities of Activin A can be neutralized by inhibins and by the diffusible TGF-β antagonist, follistatin. Activin A binds to the two forms of activin receptor type I (Act RI-A and Act RI-B) and two forms of activin receptor type II (Act RII-A and Act RII-B). Activins are homodimers or heterodimers of different β subunits. They are produced as precursor proteins with an amino terminal propeptide that is cleaved to release the C-terminal bioactive ligand. Recombinant Human/Murine/Rat Activin A is a 26.0 kDa disulfide-linked homodimer of two βA chains, each containing 116 amino acid residues.
Disclaimer
- FOR RESEARCH USE ONLY
For additional information, visit ProSci's Terms & Conditions Page. - Disclaimer: This product is for research use only.
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