Product Pathways - Protein Stability
PSMA2 (D3A4) Rabbit mAb #11864
|W||H M R Mk (C) (X) (Z) (B) (Hr)||Endogenous||25||Rabbit IgG|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey C=Chicken X=Xenopus Z=Zebrafish B=Bovine Hr=Horse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
PSMA2 (D3A4) Rabbit mAb recognizes endogenous levels of total PSMA2 protein. This antibody does not cross-react with other α subunits of the 20S proteasome.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Phe173 of human PSMA2 protein.
Western blot analysis of extracts from various cell lines using PSMA2 (D3A4) Rabbit mAb.
Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with constructs expressing Myc/DDK-tagged full-length human PSMA1 (hPSMA1-Myc/DDK; +), full-length human PSMA2 (hPSMA2-Myc/DDK; +), full-length human PSMA3 (hPSMA3-Myc/DDK; +), full-length human PSMA4 (hPSMA4-Myc/DDK; +), full-length human PSMA6 (hPSMA6-Myc/DDK; +), or full-length human PSMA7 (hPSMA7-Myc/DDK; +), using PSMA2 (D3A4) Rabbit mAb (upper) or DYKDDDDK Tag Antibody #2368 (lower).
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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For Research Use Only. Not For Use In Diagnostic Procedures.