PSMA1 (Alpha + Beta) antibody

Details for Product No. ABIN153064
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Antigen
Reactivity
Human, Mouse (Murine), Yeast
Host
Rabbit
Clonality
Polyclonal
Application
Western Blotting (WB), Immunohistochemistry (IHC), Immunoprecipitation (IP)
Pubmed 5 references available
Quantity 0.05 mL
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Catalog No. ABIN153064
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Immunogen A proteasomal preparation isolated from human red blood cells.
Specificity This detects a combination of alpha and beta proteasome subunits.
Cross-Reactivity Saccharomyces cerevisiae (S. cerevisiae)
Purification Whole antisera
Background 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.
Gene Symbol: PSMA1
Gene ID 5682, 26440
Application Notes Western blotting - The antibody has been characterized by single dimension SDS-PAGE using both purified human and yeast 20S proteasome and a number of tissue/cell preparations including a human placental proteasome preparation, a HeLa cell lysate, a RSV 3T3 mouse fibroblast cell lysate, and a yeast whole cell extract.
Recommended dilutions: Immunohistochemistry 1:10-1:500, Immunoprecipitation 1:10-1:500, Western Blot 1:1000-1:10000
Restrictions For Research Use only
Format Liquid
Buffer PBS, Sodium Azide
Preservative Sodium azide
Precaution of Use WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.
Handling Advice Avoid freeze-thaw cycles
Storage 4 °C
Storage Comment 4 °C short term. Aliquot and store at -20 °C long term.
Supplier Images
anti-PSMA1 (Alpha + Beta) antibody 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).
General 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).

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