Puromycin Sensitive Aminopeptidase (PSA) also known as cytosol alanyl aminopeptidase or alanine aminopeptidase (AAP) is used as a biomarker to detect damage to the kidneys, and that may be used to help diagnose certain kidney disorders. It is found at high levels in the urine when there are kidney problems. PSA has been proposed to function in a variety of processes, including metabolism of neuropeptidase, regulation of the cell cycle, and hydrolysis of proteasomal products to amino acids. Besides, Protein Disulfide Isomerase A3 (PDIA3) has been identified as an interactor of PSA, thus a binding ELISA assay was conducted to detect the interaction of recombinant human PSA and recombinant human PDIA3. Briefly, PSA were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 μl were then transferred to PDIA3-coated microtiter wells and incubated for 2h at 37ºC. Wells were washed with PBST and incubated for 1h with anti-PSA pAb, then aspirated and washed 3 times. After incubation with HRP labelled secondary antibody, wells were aspirated and washed 3 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37ºC. Finally, add 50 μl stop solution to the wells and read at 450nm immediately. The binding activity of PSA and PDIA3 was in a dose dependent manner.
Lyophilized from 20 mM Tris (pH 8.0) with 150 mM NaCl, 1 mM EDTA, 1 mM DTT, 0.01% SKL, 5% Trehalose, Proclin300. Reconstitute with 20 mM Tris and 150 mM NaCl (pH 8.0) to a concentration of 0.1-1.0 mg/mL. Do not vortex.
For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, store at -20ºC or below. After reconstitution, keep as concentrated solution.Avoid freeze-thaw cycles.
N-terminal His-Tag; Gly584~Gln793 (NP_001317186.1)
< 1 EU/μg
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
aminopeptidase puromycin sensitive,AAP-S,MP100,PSA
This gene encodes the puromycin-sensitive aminopeptidase, a zinc metallopeptidase which hydrolyzes amino acids from the N-terminus of its substrate. The protein has been localized to both the cytoplasm and to cellular membranes. This enzyme degrades enkaphalins in the brain, and studies in mouse suggest that it is involved in proteolytic events regulating the cell cycle. [provided by RefSeq, Jul 2008]