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  • 产品名称：anti-Dipeptidase1(Renal)(DPEP1)(AA1-30),(N-Term)antibody

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简单介绍：
anti-Dipeptidase1(Renal)(DPEP1)(AA1-30),(N-Term)antibody
详情介绍：
Immunogen This DPEP1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human DPEP1.
Clone RB41566
Purification This antibody is purified through a protein A column, followed by peptide affinity purification. Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)
Alternative Name DPEP1 (DPEP1 Antibody Abstract)
Background DPEP1 (EC 3.4.13.11) is a kidney membrane enzyme that hydrolyzes a variety of dipeptides and is implicated in renal metabolism of glutathione and its conjugates, e.g., leukotriene D4 . DPEP1 is responsible for hydrolysis of the beta-lactam ring of antibiotics, such as penem and carbapenem. Earlier, beta-lactamase enzymes were thought to occur only in bacteria, where their probable function was in protecting the organisms against the action of beta-lactam antibiotics. These antibiotics exhibit selective toxicity against bacteria but virtual inertness against many eukaryotic cells.

Synonyms: DPEP1, MDP, RDP, Dipeptidase 1, Dehydropeptidase-I, Microsomal dipeptidase, Renal dipeptidase
NCBI Accession NP_004404, NP_001121613
UniProt P16444
Pathways Inositol Metabolic Process
Application Notes WB: 1:1000
Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/mL
Buffer Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) 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.
Supplier Images
Western Blotting (WB) image for anti-Dipeptidase 1 (Renal) (DPEP1) (AA 1-30), (N-Term) antibody (ABIN1881269) DPEP1 Antibody (N-term) (ABIN1881269) western blot analysis in A549 cell line lysates...
Background publications Paré, Chasman, Parker, Zee, Mälarstig, Seedorf, Collins, Watkins, Hamsten, Miletich, Ridker: "Novel associations of CPS1, MUT, NOX4, and DPEP1 with plasma homocysteine in a healthy population: a genome-wide evaluation of 13 974 participants in the Women's Genome Health Study." in: Circulation. Cardiovascular genetics, Vol. 2, Issue 2, pp. 142-50, 2009 (PubMed).

Nan, Kraft, Qureshi, Guo, Chen, Hankinson, Hu, Thomas, Hoover, Chanock, Hunter, Han: "Genome-wide association study of tanning phenotype in a population of European ancestry." in: The Journal of investigative dermatology, Vol. 129, Issue 9, pp. 2250-7, 2009 (PubMed).

Nitanai, Satow, Adachi, Tsujimoto: "Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis." in: Journal of molecular biology, Vol. 321, Issue 2, pp. 177-84, 2002 (PubMed).

Kera, Liu, Matsumoto, Sorimachi, Nagasaki, Yamada: "Rat and human membrane dipeptidase: tissue distribution and developmental changes." in: Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, Vol. 123, Issue 1, pp. 53-8, 1999 (PubMed).

Satoh, Ohtsuka, Keida, Kusunoki, Konta, Niwa, Kohsaka: "Gene structural analysis and expression of human renal dipeptidase." in: Biotechnology progress, Vol. 10, Issue 2, pp. 134-40, 1994 (PubMed).

Adachi, Tawaragi, Inuzuka, Kubota, Tsujimoto, Nishihara, Nakazato: "Primary structure of human microsomal dipeptidase deduced from molecular cloning." in: The Journal of biological chemistry, Vol. 265, Issue 7, pp. 3992-5, 1990 (PubMed).

Campbell, Forrester, Zahler, Burks: "Beta-lactamase activity of purified and partially characterized human renal dipeptidase." in: The Journal of biological chemistry, Vol. 259, Issue 23, pp. 14586-90, 1985 (PubMed).

Kozak, Tate: "Glutathione-degrading enzymes of microvillus membranes." in: The Journal of biological chemistry, Vol. 257, Issue 11, pp. 6322-7, 1982 (PubMed).