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The protein encoded by HM13, 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 Histocompatibility (Minor) 13 Antibodies (46) and Histocompatibility (Minor) 13 Proteins (4) and many more products for this protein.
This study identifies that SPP 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 [SPP]
identified human signal peptide peptidase as a polytopic membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases [SPP]
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 ELISA Kits)]
widespread expression of SPP in many tissues
signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor
IMP1 (show IMPA1 ELISA Kits) is a bi-aspartic polytopic protease capable of cleaving transmembrane proteins such as presenilin 2 (show PSEN2 ELISA Kits).
The peptide structure corresponding to the C-terminal residues from H13 ribosomal protein was determined using magnetic resonance spectroscopy.
SPP, SPPL2a, -2b, -2c, and -3 probably cleave type II-oriented substrate peptides as shown by consensus analysis
data implicate SPP in the US2 (show USH2A ELISA Kits) pathway and indicate the possibility of a previously unknown function for this intramembrane-cleaving aspartic protease in dislocation from the endoplasmic reticulum
silencing of SPP and its family member SPPL2a led to a general reduction of surface peptide-MHC-I complexes, underlining the involvement of these enzymes in Ag processing and presentation.
structural analysis of H13 peptides lacking MHC binding anchor motifs determines self-nonself discrimination
widespread expression of SPP in many tissues; a distinct pattern of expression in the mature murine brain and during development indicates that SPP plays an important role in the establishment and maintenance of the nervous system
A single minor histocompatibility antigen mismatch at the polymorphic H13 allele plays a role in chronic allograft rejection of solid organs such as obliterative airway disease development following murine tracheal transplantation.
new splice variant,signal peptide peptidase (SPP)beta, with an additional in-frame exon inserted between exons 11 and 12 of SPPalpha
Results show that two genetic systems show that alleles lacking methylation generate truncated H13 transcripts that undergo internal polyadenylation.
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.
, signal peptide peptidase
, intramembrane aspartyl protease
, histocompatibility (minor) 13
, minor histocompatibility antigen 13
, minor histocompatibility antigen H13
, minor histocompatibility antigen H13-like
, intramembrane protease 1
, presenilin-like protein 3
, signal peptide peptidase beta
, signal peptide peptidase like 1
, presenilin-like aspartyl protease