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|+1 888 205 9894 (TF)|
PSMA1 (alpha + beta) antibody
Immunohistochemistry (Frozen Sections) (IHC (fro)), Immunoprecipitation (IP), Western Blotting (WB)
|5 references available|
|Price||Product not available in this region.|
|Gene ID||5682, 26440|
|Immunogen||A proteasomal preparation isolated from human red blood cells.|
|Cross-Reactivity||Human, Mouse (Murine), Yeast|
|Description||The proteasome is widely recognised as the central enzyme of non-lysosomal proteindegradation. It is responsible for intracellular protein turnover and it is also criticallyinvolved in many regulatory processes and, in higher eukaryotes, in antigen processing.The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway ofprotein degradation. The catalytic core of this unusually large (2000kDa, 450A in length)complex is formed by the 20S proteasome, a barrel shaped structure shown by electronmicroscopy to comprise of four rings each containing seven subunits.Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may beclassified into two groups, alpha and beta, each group having distinct structural andfunctional roles. The alpha-subunits comprise the outer rings and the beta-subunits theinner rings of the 20S proteasome. Observations of the eukaryotic proteasome andanalysis of subunit sequences indicate that each ring contains seven different subunits(alpha 7 beta 7 beta 7 alpha 7) with a member of each sub-family represented in eachparticle. Each subunit is located in a unique position within the alpha- or beta-rings (ref1).20S Proteasomes degrade only unfolded proteins in an energy-independent manner,whereas 26S proteasomes degrade native and ubiquitinylated proteins in anATP-dependent manner. The native protein substrates are recognised by subunits,some with ATP binding sites, of the outer 19S caps of the 26S proteasome (ref 2). Alternate Names: Anti-30 kDa prosomal protein antibody, anti- HC 2 antibody, anti- Macropain antibody,anti- Macropain subunit nu antibody.|
|Specificity||This antibody detects a combination of alpha and beta proteasome subunits. Species Reactivity: Cross-reacts with Human, Mouse and S. cerevisiae proteasomes. Not yet tested inother species. Localization: Cytoplasmic and Nuclear.|
|Application Notes||Suggested working dilutions: immunohistochemistry - Use at an assay dependent dilution. ,immunoprecipitation - Use at an assay dependent dilution. ,Western Blot - 1/1000 - 1/10000. Positive Controls: Human and yeast 20S proteasome and human placental proteasome preps|
|Buffer||PBS. Preservative: 0.01M Sodium Azide.|
|Storage||Store at 4 C short term or -20 C long term.|
|Restrictions||For Research Use only|
|Luminograph of human erythrocyte-derived 20S proteasome lysate after SDS-PAGE followed by blotting onto PVDF and probing with antibody PW 8155. Antibody dilution 1:1000 using ECL procedure (1 min exposure).|
Kopp, Hendil, Dahlmann et al.: "Subunit arrangement in the human 20S proteasome." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, Issue 7, pp. 2939-44, 1997 (PubMed).
Funakoshi, Sasaki, Nishimoto et al.: "Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 2, pp. 745-50, 2002 (PubMed).
Lelouard, Gatti, Cappello et al.: "Transient aggregation of ubiquitinated proteins during dendritic cell maturation." in: Nature, Vol. 417, Issue 6885, pp. 177-82, 2002 (PubMed).
Xie, Varshavsky: "UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis." in: Nature cell biology, Vol. 4, Issue 12, pp. 1003-7, 2002 (PubMed).
Laporte, Salin, Daignan-Fornier et al.: "Reversible cytoplasmic localization of the proteasome in quiescent yeast cells." in: The Journal of cell biology, Vol. 181, Issue 5, pp. 737-45, 2008 (PubMed).