Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Immunocytochemistry (ICC)
Specificité
The mouse monoclonal antibody GCP-04 recognizes amino acids 100-104 of extracellular domain of denaturated glutamate carboxypeptidase II (PSMA, NAALADase, FOLH1), an approximately 95-110 kDa transmembrane glycoprotein.
Réactivité croisée (Details)
Human, Porcine, Mouse, Rat, Other not determined
Purification
Purified by protein-A affinity chromatography.
Pureté
> 95 % (by SDS-PAGE)
Immunogène
Recombinant fragment of human GCPII (amino acids 44-750) produced in S2 cells
FOLH1
Reactivité: Humain, Souris, Rat, Chien, Singe
WB, IF
Hôte: Souris
Monoclonal
2E1
unconjugated
Indications d'application
Western blotting: Recommended dilution: 1 μg/mL, positive control: LNCaP cell line. Sample preparation: Resuspend approx. 50 mil. cells in 1 mL cold lysis buffer (1 % NP-40). Incubate 30 min on ice. Mix lysate with non-reducing/reducing Laemmli SDS-PAGE sample buffer. Both reducing and non-reducing conditions.
Restrictions
For Research Use only
Concentration
1 mg/mL
Buffer
Phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Conseil sur la manipulation
Do not freeze.
Stock
4 °C
Stockage commentaire
Store at 2-8°C. Do not freeze.
Wächter, Di Fazio, Maurer, Manoharan, Keber, Pfestroff, Librizzi, Bartsch, Luster, Eilsberger: "Prostate-Specific Membrane Antigen in Anaplastic and Poorly Differentiated Thyroid Cancer-A New Diagnostic and Therapeutic Target?" dans: Cancers, Vol. 13, Issue 22, (2021) (PubMed).
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Gao, Xu, Cui, Zhang, Lin, Cai, Wang, Luo, Zheng, Wang, Luo, Jiang, Neale, Zhong: "Mice lacking glutamate carboxypeptidase II develop normally, but are less susceptible to traumatic brain injury." dans: Journal of neurochemistry, Vol. 134, Issue 2, pp. 340-53, (2015) (PubMed).
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Sácha, Zámecník, Barinka, Hlouchová, Vícha, Mlcochová, Hilgert, Eckschlager, Konvalinka: "Expression of glutamate carboxypeptidase II in human brain." dans: Neuroscience, Vol. 144, Issue 4, pp. 1361-72, (2007) (PubMed).
Barinka, Mlcochová, Sácha, Hilgert, Majer, Slusher, Horejsí, Konvalinka: "Amino acids at the N- and C-termini of human glutamate carboxypeptidase II are required for enzymatic activity and proper folding." dans: European journal of biochemistry / FEBS, Vol. 271, Issue 13, pp. 2782-90, (2004) (PubMed).
Barinka, Sácha, Sklenár, Man, Bezouska, Slusher, Konvalinka: "Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity." dans: Protein science : a publication of the Protein Society, Vol. 13, Issue 6, pp. 1627-35, (2004) (PubMed).
Barinka, Rinnová, Sácha, Rojas, Majer, Slusher, Konvalinka: "Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II." dans: Journal of neurochemistry, Vol. 80, Issue 3, pp. 477-87, (2002) (PubMed).
Folate hydrolase 1,Glutamate carboxypeptidase II (GCPII), also known as N-acetyl-alpha-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-gamma-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 tumours 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.,GCP2, FOLH1, NAALADase I, PGGCP, FGGCP, FGCP,