Anti-PSMA Purified

Anti-PSMA Purified
Regulatory status
RUO
Antigen
PSMA
Clone
GCP-05
Format
Purified
Reactivity
Human
Application
IP, MC (CyTOF), FC (QC tested), ICC
Variant
0.1 mg
11-539-C100
In stock

0.025 mg
11-539-C025
Out of stock
Variant
0.1 mg
11-261-C100
In stock

0.1 mg
11-261-C100
In stock
Product details
Images
References
Isotype
Mouse IgG1
Specificity
The mouse monoclonal antibody GCP-05 recognizes extracellular domain (preferentially in native form) of glutamate carboxypeptidase II (NAALADase, FOLH1, PSMA), an approximately 95-110 kDa transmembrane glycoprotein expressed mainly in tumour neovasculatures, nervous system and jejunum, which is an important prostate tumour marker.
Application
IP, MC (CyTOF), FC (QC tested), ICC
Reactivity
Human
Immunogen
amino acids 44-750 of human GCPII
Other names
Glutamate carboxypeptidase 2, GCPII, GCP2, NAALADase I, PGGCP, FGGCP, FGCP, Folate hydrolase 1, Prostate-specific membrane antigen
Concentration
1 mg/ml
Preparation
Purified by protein-A affinity chromatography
Formulation
Phosphate buffered saline (PBS) solution with 15 mM sodium azide
Storage and handling
Store at 2-8°C. Do not freeze. Do not use after expiration date stamped on vial label.
Exbio licence note
Unless indicated otherwise, all products are For Research Use Only and not for diagnostic use. In vivo diagnostic or therapeutic applications are strictly forbidden. Products shall not be used for resale or transfer to third parties either as a stand-alone product or as a manufacture component of another product without written consent of EXBIO Praha, a.s. EXBIO Praha, a.s. will not be held responsible for patent infringement or any other violations of intellectual property rights that may occur with the use of the products. Orders for all products are accepted subject to the Term and Conditions available at www.exbio.cz. EXBIO, EXBIO Logo, and all other trademarks are property of EXBIO Praha, a.s. © 2019 EXBIO Praha, a.s. All rights reserved.
11-539 FC
Flow cytometry analysis (surface staining) of GCPII / PSMA using anti-GCPII (GCP-05) and goat anti-mouse-PE on LNCaP cell line (positive, green) and HeLa cells (negative, blue).
11-539 MC
Mass cytometry (surface staining) of LNCaP cell line using anti-GCPII (GCP-05) 173Yb. Gated on singlets.

General references:

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 U S A. 2003 Aug 5;100(16):9554-9.
PubMed
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, 25: 1375-1384
PubMed
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
PubMed

Product specific references:

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
PubMed
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
PubMed
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 Dec;74(16):1674-90.
PubMed
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
PubMed
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
PubMed
Variant
0.1 mg
11-539-C100
In stock

0.025 mg
11-539-C025
Out of stock
Variant
0.1 mg
11-261-C100
In stock

0.1 mg
11-261-C100
In stock