Flow Cytometry (FACS), Immunoprecipitation (IP), Immunocytochemistry (ICC), Cytometry by Time of Flight (CyTOF)
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.
FOLH1
Reactivity: Human, Mouse, Rat, Dog, Monkey
WB, IF
Host: Mouse
Monoclonal
2E1
unconjugated
Application Notes
Flow cytometry: Recommended dilution: 1-4 μg/mL.
Restrictions
For Research Use only
Concentration
1 mg/mL
Buffer
Phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice
Do not freeze.
Storage
4 °C
Storage Comment
Store at 2-8°C. Do not freeze.
Tykvart, Navrátil, Sedlák, Corey, Colombatti, Fracasso, Koukolík, Ba?inka, Sácha, Konvalinka: "Comparative analysis of monoclonal antibodies against prostate-specific membrane antigen (PSMA)." in: The Prostate, Vol. 74, Issue 16, pp. 1674-90, (2014) (PubMed).
Sácha, Zámecník, Barinka, Hlouchová, Vícha, Mlcochová, Hilgert, Eckschlager, Konvalinka: "Expression of glutamate carboxypeptidase II in human brain." in: Neuroscience, Vol. 144, Issue 4, pp. 1361-72, (2007) (PubMed).
Barinka, Sácha, Sklenár, Man, Bezouska, Slusher, Konvalinka: "Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity." in: Protein science : a publication of the Protein Society, Vol. 13, Issue 6, pp. 1627-35, (2004) (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,