Human Tripeptidyl Peptidase 1 ELISA Kit

This Human Tripeptidyl Peptidase 1 ELISA Kit from Innovative Research is intended for quantitative detection of human TPP1 in cell culture supernates, serum and plasma (heparin, EDTA). Strip well format. Reagents for up to 96 tests.

This human TPP1 ELISA Kit is based on standard sandwich enzyme-linked immune-sorbent assay technology. A monoclonal antibody from mouse specific for TPP1 has been precoated onto 96-well plates. Standards(Expression system for standard: NSO, Immunogen sequence: L196-P563) and test samples are added to the wells, a biotinylated detection polyclonal antibody from goat specific for TPP1 is added subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex is added and unbound conjugates are washed away with PBS or TBS buffer. HRP substrate TMB are used to visualize HRP enzymatic reaction. TMB is catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the human TPP1 amount of sample captured in plate.

• Detection Target: Tripeptidyl Peptidase 1
• Uniprot ID: O14773)
• Reactivity: Human
• Cross-Reactivity: There is no detectable cross-reactivity with other relevant proteins.
• Range: 156pg/ml-10000pg/ml
• Sensitivity: <50pg/ml
• Storage Conditions: Store at 4?C for 6 months, at -20?C for 12 months. Avoid multiple freeze-thaw cycles. (Shipped with wet ice)

Additional Information: The capture antibody is a monoclonal antibody from mouse, the detection antibody is a biotinylated polyclonal antibody from goat. Expression system for standard: Tripeptidyl-peptidase 1, also known as Lysosomal pepstatin-insensitive protease, is an enzyme that in humans is encoded by the TPP1 gene. The human gene TPP1 encodes a member of the sedolisin family of serine proteases. The human gene has 13 exons and locates at the chromosome band 11p15. This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome.; Immunogen sequence: 369