特異性

The mouse monoclonal antibody GCP-05 recognizes extracellular domain (preferentially in native form) of GCPII (PSMA), a 95-110 kDa transmembrane glycoprotein expressed mainly in tumor neovasculatures, nervous system and jejunum, which is an important prostate tumour marker.

抗原情報

Glutamate carboxypeptidase II (GCPII), also known as N-acetyl-α-linked acidic dipeptidase I (NAALADase I), folate hydrolase (FOLH1) and prostate-specific membrane antigen (PSMA), is an approximately 95-110 kDa type II transmembrane glycoprotein expressed in various tissues. In nervous system GCPII cleaves abundant N-acetylaspartylglutamate, which is released from neurons in a calcium-dependent manner, to N-acetylaspartate and glutamate. As immoderate glutamate concentration is neurotoxic, GCPII contributes to pathological conditions regarding e.g. Alzheimer´s disease, Huntington´s disease, epilepsy, schizophrenia, stroke or neuropathic pain and appears to be an interesting therapeutic target. In jejunum GCPII hydrolyzes pteroylpoly-γ-glutamate to folate and glutamate, enabling folate to be absorbed by gastrointestinal tract. GCPII, which is present in a number of tissues at low levels, is overexpressed in neovasculature of most solid tumors and is a target enzyme for diagnosis and treatment of prostate cancer. Normal human prostate express more mRNA coding for a cytosolic GCPII form truncated at the N-terminus (PSM´) than mRNA for membrane-bound GCPII, and this ratio is reversed upon malignant transformation.

利用方法

保存方法

Avoid prolonged exposure to light. Store in the dark at 2-8°C. Do not freeze.

安定性情報

Do not use after expiration date stamped on vial label.

レファレンス

• Barinka C, Mlcochova P, Sacha P, Hilgert I, Majer P, Slusher BS, Horejsi V, Konvalinka J: Amino acids at the N‑ and C‑termini of human glutamate carboxypeptidase II are required for enzymatic activity and proper folding. Eur·J·Biochem. 2004; 271:2782‑2790. <·PMID:·15206943·>
• Barinka C, Rinnova M, Sacha P, Rojas C, Majer P, Slusher BS, Konvalinka J: Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II. J·Neurochem. 2002; 80:477‑487. <·PMID:·11905994·>
• Barinka C, Sacha P, Sklenar J, Man P, Bezouska K, Slusher BS, Konvalinka J: Identification of the N‑glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity. Protein·Sci. 2004; 13:1627‑1635. <·PMID:·15152093·>
• Davis MI, Bennett MJ, Thomas LM, Bjorkman PJ: Crystal structure of prostate‑specific membrane antigen, a tumor marker and peptidase. Proc·Natl·Acad·Sci·USA. 2005; 102:5981‑5986. <·PMID:·15837926·>
• Ghadge GD, Slusher BS, Bodner A, Canto MD, Wozniak K, Thomas AG, Rojas C, Tsukamoto T, Majer P, Miller RJ, Monti AL, Roos RP: Glutamate carboxypeptidase II inhibition protects motor neurons from death in familial amyotrophic lateral sclerosis models. Proc·Natl·Acad·Sci·USA. 2003·Aug·5; 100(16):9554‑9. <·PMID:·12876198·>
• Mesters JR, Barinka C, Li W, Tsukamoto T, Majer P, Slusher BS, Konvalinka J, Hilgenfeld R: Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer. EMBO·J. 2006; 1375‑1384. <·PMID:·16467855·>
• Sacha P, Zamecnik J, Barinka C, Hlouchova K, Vicha A, Mlcochova P, Hilgert I, Eckschlager T, Konvalinka J: Expression of glutamate carboxypeptidase II in human brain. Neuroscience. 2007; 144:1361‑1372. <·PMID:·17150306·>
• Tykvart J, Navrátil V, Sedlák F, Corey E, Colombatti M, Fracasso G, Koukolík F, Bařinka C, Sácha P, Konvalinka J: Comparative analysis of monoclonal antibodies against prostate‑specific membrane antigen (PSMA). Prostate. 2014·Sep·27; <·PMID:·26629066·>