Recombinant Human PNAD protein
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Recombinant Human PNAD protein is a Human Full Length protein, in the 1 to 310 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
Protein N-terminal asparagine amidohydrolase, Protein NH2-terminal asparagine amidohydrolase, Protein NH2-terminal asparagine deamidase, PNAA, PNAD, Protein N-terminal Asn amidase, Protein N-terminal asparagine amidase, Protein NTN-amidase, NTAN1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human PNAD protein (AB165200)
ab165200 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
PNAd mediates the adhesion of lymphocytes to HEVs a critical step in the immune response promoting the recirculation of lymphocytes throughout the body. PNAd does not function as an independent entity often part of a multiprotein complex involving various glycoproteins and ligands that collectively ensure efficient immune surveillance. Its interaction with L-selectin is an essential event in lymphocyte adhesion under shear flow conditions seen in blood circulation.
Pathways
PNAd plays a role in the lymphocyte signaling pathways particularly associated with leukocyte extravasation. This pathway is integral for lymphocyte migration involving key signaling molecules and interactions with proteins like ICAM-1 and VCAM-1. PNAd's function in this pathway reflects its importance for maintaining effective immune system balance and proper lymphocyte distribution.
Specifications
Form
Liquid
General info
Function
N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.
Target data
Product promise
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