Exbio — Research products — Antibodies — CD and related antigens — Anti-PSMA Alexa Fluor<sup>®</sup> 488

Anti-PSMA Alexa Fluor^® 488

Regulatory status

RUO

Antigen

PSMA

Clone

GCP-05

Format

Alexa Fluor^® 488

Reactivity

Human

Application

FC (QC tested), ICC

Excitation laser

blue (488 nm)

Variant

0.1 mg

A4-539-C100

In stock

360.00 USD

0.025 mg

A4-539-C025

Delivery 1 week

180.00 USD

Variant

0.1 mg

A4-539-C100

In stock

360.00 USD

0.025 mg

A4-539-C025

Delivery 1 week

180.00 USD

Contact distributor

Product details

Description

Images

References

SDS download

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

FC (QC tested), ICC

Application details

Flow cytometry: Recommended dilution: 5 μg/ml.

Reactivity

Human

Immunogen

amino acids 44-750 of human GCPII

Concentration

1 mg/ml

Preparation

Purified antibody is conjugated with Alexa Fluor^® 488 NHS ester under optimum conditions and unconjugated antibody and free fluorochrome are removed by size-exclusion chromatography.

Formulation

Phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide

Storage and handling

Store at 2-8°C. Protect from prolonged exposure to light. Do not freeze.

The product is intended For Research Use Only. 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.

Alexa Fluor^®, Pacific Blue™ and Pacific Orange™ are registered trademarks of Life Technologies Corporation.

This product is provided under an intellectual property license from Life Technologies Corporation. The transfer of this product is conditioned on the buyer using the purchased product solely in research conducted by the buyer, excluding contract research or any fee for service research, and the buyer must not (1) use this product or its components for (a) diagnostic, therapeutic or prophylactic purposes; (b) testing, analysis or screening services, or information in return for compensation on a per-test basis; or (c) manufacturing or quality assurance or quality control, and/or (2) sell or transfer this product or its components for resale, whether or not resold for use in research. For information on purchasing a license to this product for purposes other than as described above, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@lifetech.com.

Other names

GCP2, FOLH1, NAALADase I, PGGCP, FGGCP, FGCP,

Antigen description

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.

Entrez Gene ID 2346

UniProt ID Q04609

Flow cytometry analysis (surface staining) of GCPII / PSMA using anti-GCPII (GCP-05) Alexa Fluor® 488 on LNCaP cell line.

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