Product Pathways - Protein Stability
PSMA2 Antibody #2455
|2455S||100 µl (10 western blots)||---||In Stock||---|
|2455||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||28||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IF-IC=Immunofluorescence (Immunocytochemistry)
Specificity / Sensitivity
PSMA2 Antibody detects endogenous levels of total PSMA2 protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Thr223 of human PSMA2 protein. Antibodies are purified by protein A and peptide affinity chromatography.
The 20S proteasome is the major proteolytic enzyme complex involved in intracellular protein degradation. It consists of four stacked rings, each with seven distinct subunits. The two outer layers are identical rings composed of α subunits (called PSMAs), and the two inner layers are identical rings composed of β subunits. While the catalytic sites are located on the β rings (1-3), the α subunits are important for assembly and as binding sites for regulatory proteins (4). Seven different α and ten different β proteasome genes have been identified in mammals (5). PA700, PA28, and PA200 are three major protein complexes that function as activators of the 20S proteasome. PA700 binds polyubiquitin with high affinity and associates with the 20S proteasome to form the 26S proteasome, which preferentially degrades poly-ubiquitinated proteins (1-3). The proteasome has a broad substrate spectrum that includes cell cycle regulators, signaling molecules, tumor suppressors, and transcription factors. By controlling the degradation of these intracellular proteins, the proteasome functions in cell cycle regulation, cancer development, immune responses, protein folding, and disease progression (6-9).
- Dahlmann, B. (2005) Essays Biochem. 41, 31-48.
- Pickart, C.M. and Cohen, R.E. (2004) Nat. Rev. Mol. Cell Biol. 5, 177-187.
- Nandi, D. et al. (2006) J. Biosci. 31, 137-155.
- Lupas, A. et al. (1993) Enzyme Protein 47, 252-273.
- Monaco, J.J. and Nandi, D. (1995) Annu. Rev. Genet. 29, 729-754.
- Murray, A.W. (2004) Cell 116, 221-234.
- Ciechanover, A. (2006) Proc. Am. Thorac. Soc. 3, 21-31.
- Wang, J. and Maldonado, M.A. (2006) Cell. Mol. Immunol. 3, 255-261.
- Rubinsztein, D.C. (2006) Nature 443, 780-786.
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