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The protein encoded by IMP1, which localizes to the endoplasmic reticulum, catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. Additionally we are shipping Imprintor 1 Proteins (1) and many more products for this protein.
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structure of human SPP (show SPEB Antibodies) [SPP (show SPEB Antibodies)]
identified human signal peptide peptidase as a polytopic membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases [SPP (show SPEB Antibodies)]
identification and molecular cloning; expression analysis of the hIMP1 gene (located on chromosome 20) was performed in human cell tissues and transfected cell cultures [IMP1 (show IMPA1 Antibodies)]
widespread expression of SPP (show SPEB Antibodies) in many tissues
signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor
IMP1 (show IMPA1 Antibodies) is a bi-aspartic polytopic protease capable of cleaving transmembrane proteins such as presenilin 2 (show PSEN2 Antibodies).
The peptide structure corresponding to the C-terminal residues from H13 ribosomal protein was determined using magnetic resonance spectroscopy.
SPP (show SPEB Antibodies), SPPL2a (show SPPL2A Antibodies), -2b, -2c, and -3 probably cleave type II-oriented substrate peptides as shown by consensus analysis
data implicate SPP (show SPEB Antibodies) in the US2 (show USH2A Antibodies) pathway and indicate the possibility of a previously unknown function for this intramembrane-cleaving aspartic protease in dislocation from the endoplasmic reticulum
Upon isolation of membranes and solubilization with detergent, the biochemical characteristics of SPP (show SPEB Antibodies) are remarkably similar to gamma-secretase.
The protein encoded by this gene, which localizes to the endoplasmic reticulum, catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein. This activity is required to generate signal sequence-derived human lymphocyte antigen-E epitopes that are recognized by the immune system, and to process hepatitis C virus core protein. The encoded protein is an integral membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases. Multiple transcript variants encoding several different isoforms have been found for this gene.
, intramembrane protease 1
, minor histocompatibility antigen 13
, minor histocompatibility antigen H13
, presenilin-like protein 3
, signal peptide peptidase beta
, signal peptide peptidase like 1