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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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This study identifies that SPP (show SPEB Antibodies) affects EGFRvIII secretion profiles and thus promotes tumor progression, providing further understanding of the formation of secreted vesicles and driving role of EGFRvIII in Glioblastoma.
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
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