HM13 Antibody, FITC conjugated

1. Preproinsulin signal peptide epitopes are processed by SPP and loaded for HLA-guided immune recognition via pathways that are enhanced during type 1 diabetes pathogenesis. PMID: 29343547
2. Though far from complete, our knowledge on pathophysiological functions of SPP/SPPL proteases, in particular based on studies in mice, has been significantly increased over the last years. Based on this, inhibition of distinct SPP/SPPL proteases has been proposed as a novel therapeutic concept e.g. for the treatment of autoimmunity and viral or protozoal infections, as we will discuss in this review. PMID: 28624439
3. The domains involved in HO-1 translocation have been identified, and it was shown that SPP-mediated HO-1 cleavage is isoform-specific (HO-1 vs HO-2) and independent of heme oxygenase activity. PMID: 29155886
4. 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. PMID: 28198167
5. structure of human SPP [SPP] PMID: 21636854
6. identified human signal peptide peptidase as a polytopic membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases [SPP] PMID: 12077416
7. 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] PMID: 12139484
8. widespread expression of SPP in many tissues PMID: 12972007
9. signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor PMID: 14704149
10. IMP1 is a bi-aspartic polytopic protease capable of cleaving transmembrane proteins such as presenilin 2. PMID: 14741365
11. The peptide structure corresponding to the C-terminal residues from H13 ribosomal protein was determined using magnetic resonance spectroscopy. PMID: 14988012
12. data implicate SPP in the US2 pathway and indicate the possibility of a previously unknown function for this intramembrane-cleaving aspartic protease in dislocation from the endoplasmic reticulum PMID: 16738546
13. Upon isolation of membranes and solubilization with detergent, the biochemical characteristics of SPP are remarkably similar to gamma-secretase. PMID: 16834339
14. Compares a variant from the mouse ortholog to the human gene. PMID: 16730383

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HGNC: 16435

OMIM: 607106

KEGG: hsa:81502

UniGene: Hs.373741