The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
IHC-P: Ready to use for 30 min at room temperature. Staining of formalin fixed tissues requires boiling tissue sections in 10mM citrate buffer, pH 6.0 for 10 min followed by cooling at room temperature for 20 min.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
Has 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.
Highly 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.
Belongs to the peptidase M28 family. M28B subfamily.
The NAALADase activity is found in the central region, the dipeptidyl peptidase IV type activity in the C-terminal.
The first two amino acids at the N-terminus of isoform PSMA' appear to be cleaved by limited proteolysis. The N-terminus is blocked.