Product Pathways - Protein Stability
PSMC5/TRIP1 Antibody #13392
|13392S||100 µl (10 western blots)||---||In Stock||---|
|13392||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||45||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: D. melanogaster, Zebrafish, Pig.
Specificity / Sensitivity
PSMC5/TRIP1 Antibody recognizes endogenous levels of total PSMC5 (TRIP1) protein. This antibody does not cross-react with other AAA-ATPase subunits of the 19S proteasome regulatory particle.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human PSMC5 (TRIP1) protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from various cell lines using PSMC5/TRIP1 Antibody.
Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with constructs expressing Myc/DDK-tagged full-length human PSMC1 (hPSMC1-Myc/DDK; +), full-length human PSMC2 (hPSMC2-Myc/DDK; +), full-length human PSMC3 (hPSMC3-Myc/DDK; +), full-length human PSMC4 (hPSMC4-Myc/DDK; +); full-length human PSMC5 (hPSMC5-Myc/DDK; +), or full-length human PSMC6 (hPSMC6-Myc/DDK; +), using PSMC5/TRIP1 Antibody (upper) and DYKDDDDK Tag Antibody #2368 (lower).
The 26S proteasome is a highly abundant, ~2 MDa complex that serves as the proteolytic arm of the ubiquitin-proteasome system. It consists largely of two sub-complexes, the 19S regulatory particle (RP) and the 20S catalytic core particle (CP); in many cases two RPs cap either end of a CP. The CP is made of two stacked β-rings that contain the catalytic sites, each of which is made of seven subunits (β1-7), flanked on either side by two α-rings, which are also made of seven subunits each (α1-7). Thus, the structure of the 20S CP is α1-7β1-7β1-7α1-7. The RP includes a base and a lid. The base, in part, is composed of a hexametric ring of ATPases that function to unfold the substrate and open the gate of the interlacing amino-terminal segments of the α-subunits, thus allowing entry of the unfolded substrate into the catalytic chamber. The lid is predominantly involved in specific recognition of the ubiquitin signal (1). In addition to the 19S cap, other proteins and complexes, such as proteasome activator 28 (PA28/11S), bind to the end of the 20S cylinder and activate it by facilitating opening of the gate. Furthermore, proteasome-associated DUBs and E3s can remodel substrate-anchored polyubiquitin chains, which may modulate their susceptibility to degradation (2).
The eukaryotic proteasome 19S RP contains six ATPases-associated-with-different-cellular-activities (AAA) proteins (PSMC1-PSMC6) that bind directly to the 20S CP α-ring. These 19S RP ATPases are thought to assemble into a heterohexameric, pore-like structure that forms part of the substrate translocation channel. Energy derived from ATP hydrolysis by the AAA-ATPases is utilized for substrate unfolding and translocation, which is required for degradation of ubiquitinated folded proteins within the central chamber of the 20S CP formed by β-subunits (3-5). Thyroid hormone receptor-interacting protein 1 (PSMC5, TRIP1) is a 19S AAA-ATPase subunit involved in the negative regulation of gene transcription. Recruitment of PSMC5 to liganded VDR (6) and RARγ2 (7) facilitates their degradation via the proteasome.
- Finley, D. (2009) Annu Rev Biochem 78, 477-513.
- Lee, M.J. et al. (2011) Mol Cell Proteomics 10, R110.003871.
- Groll, M. et al. (2000) Nat Struct Biol 7, 1062-7.
- Braun, B.C. et al. (1999) Nat Cell Biol 1, 221-6.
- Liu, C.W. et al. (2002) J Biol Chem 277, 26815-20.
- Masuyama, H. and MacDonald, P.N. (1998) J Cell Biochem 71, 429-40.
- Giannì, M. et al. (2002) EMBO J 21, 3760-9.
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