Key features and details
- PE Mouse monoclonal [GCP-05] to PSMA
- Suitable for: Flow Cyt
- Reacts with: Human
- Conjugation: PE. Ex: 488nm, Em: 575nm
- Isotype: IgG1
Product namePE Anti-PSMA antibody [GCP-05]
See all PSMA primary antibodies
DescriptionPE Mouse monoclonal [GCP-05] to PSMA
ConjugationPE. Ex: 488nm, Em: 575nm
Specificityab77228 recognizes extracellular domain of PSMA, expressed mainly in tumour neovasculatures, nervous system and jejunum, which is an important prostate tumour marker.
Tested applicationsSuitable for: Flow Cytmore details
Species reactivityReacts with: Human
Recombinant fragment, corresponding to amino acids 44-750 of Human PSMA
The antibody is conjugated with R-Phycoerythrin (PE) under optimum conditions.
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In preparation for this, we have started to update the applications & species that this product is Abpromise guaranteed for.
We are also updating the applications & species that this product has been “predicted to work with,” however this information is not covered by our Abpromise guarantee.
Applications & species from publications and Abreviews that have not been tested in our own labs or in those of our suppliers are not covered by the Abpromise guarantee.
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Storage instructionsShipped at 4°C. Store at +4°C.
Storage bufferpH: 7.4
Preservative: 0.097% Sodium azide
Constituents: 0.2% BSA, PBS
Concentration information loading...
Our Abpromise guarantee covers the use of ab77228 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ab91357 - Mouse monoclonal IgG1, is suitable for use as an isotype control with this antibody.
FunctionHas both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression.
Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.
Tissue specificityHighly expressed in prostate epithelium. Detected in urinary bladder, kidney, testis, ovary, fallopian tube, breast, adrenal gland, liver, esophagus, stomach, small intestine, colon and brain (at protein level). Detected in the small intestine, brain, kidney, liver, spleen, colon, trachea, spinal cord and the capillary endothelium of a variety of tumors. Expressed specifically in jejunum brush border membranes. In the brain, highly expressed in the ventral striatum and brain stem. Also expressed in fetal liver and kidney. Isoform PSMA' is the most abundant form in normal prostate. Isoform PSMA-1 is the most abundant form in primary prostate tumors. Isoform PSMA-2 is also found in normal prostate as well as in brain and liver. Isoform PSMA-9 is specifically expressed in prostate cancer.
Sequence similaritiesBelongs to the peptidase M28 family. M28B subfamily.
DomainThe NAALADase activity is found in the central region, the dipeptidyl peptidase IV type activity in the C-terminal.
modificationsThe first two amino acids at the N-terminus of isoform PSMA' appear to be cleaved by limited proteolysis.
The N-terminus is blocked.
Cellular localizationCytoplasm and Cell membrane.
- Information by UniProt
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ab77228 has been referenced in 5 publications.
- Minn I et al. Imaging CAR T cell therapy with PSMA-targeted positron emission tomography. Sci Adv 5:eaaw5096 (2019). PubMed: 31281894
- Sácha P et al. Expression of glutamate carboxypeptidase II in human brain. Neuroscience 144:1361-72 (2007). PubMed: 17150306
- Barinka C et al. Amino acids at the N- and C-termini of human glutamate carboxypeptidase II are required for enzymatic activity and proper folding. Eur J Biochem 271:2782-90 (2004). PubMed: 15206943
- Barinka C et al. Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity. Protein Sci 13:1627-35 (2004). PubMed: 15152093
- Barinka C et al. Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II. J Neurochem 80:477-87 (2002). PubMed: 11905994