The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Specific Activity: 5 U/µg. One unit will hydrolyze 1 nmol p-nitrophenyl phosphate per minute at pH 7.4 and 30°C. Assay buffer: 50 mM HEPES, pH 7.4, 2 mM EDTA, 3mM DTT, 100 mM NaCl, 50 mM pNPP. The specific activity of PTPN13 was determined using pNPP. Enzyme reaction condition: 20 mM pNPP, 5 min incubation at 30°C, 1µg enzyme.
Concentration information loading...
Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
APO1/CD95 (Fas) associated phosphatase
Fas associated phosphatase 1
Fas associated protein tyrosine phosphatase 1
Protein tyrosine phosphatase 1 Fas associated
protein tyrosine phosphatase 1E
Protein tyrosine phosphatase non receptor type 13
Protein tyrosine phosphatase nonreceptor type 13
Protein tyrosine phosphatase PTPL1
protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase)
Tyrosine protein phosphatase non receptor type 13
PTPN13 is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP is a large protein that possesses a PTP domain at C-terminus, and multiple noncatalytic domains, which include a domain with similarity to band 4.1 superfamily of cytoskeletal associated proteins, a region consisting of five PDZ domains, and a leucine zipper motif. This PTP was found to interact with, and dephosphorylate Fas receptor, as well as I-kappa-B-alpha through the PDZ domains, which suggested its role in Fas mediated programmed cell death. This PTP was also shown to interact with GTPase-activating protein, and thus may function as a regulator of Rho signaling pathway.
Recombinant human PTPN13 protein (ab42581)参考文献
has not yet been referenced specifically in any publications.