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anti-Human MBTPS1 Antibodies:
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rs11642644 associated with facial profile
In the absence of S1P, the catalytically inactive alpha/beta-subunit precursor of GlcNAc-1-phosphotransferase fails to be activated and results in missorting of newly synthesized lysosomal enzymes, and lysosomal accumulation of non-degraded material, which are biochemical features of defective GlcNAc-1-phosphotransferase subunits and the associated pediatric lysosomal diseases mucolipidosis type II and III.
Results suggest that (pro)renin receptor (s(P)RR) is generated by sequential processing by site-1 protease (S1P) and furin protein.
primordial SKI-1/S1P likely contained a simpler prodomain consisting of the highly conserved AB fragment that represents an independent folding unit
S1P substrate-dependent regulatory mechanisms for lipid synthesis and biogenesis of lysosomes are different
The interaction between S1P and C5a plays an important role in neutrophils for antineutrophil cytoplasmic antibody -mediated activation
Incompletely matured forms of SKI-1/S1P further process cellular and viral substrates in distinct subcellular compartments.
We show that SKI-1 is constitutively expressed in human pigment cells with higher SKI activity in seven out of eight melanoma cell lines compared with normal melanocytes.
Diabetic high-density lipoprotein carries higher levels of S1P compared with normal high-density lipoprotein.
Y285 of SKI-1 is crucial for the efficient processing of envelope glycoproteins from Old World and clade C New World arenavirus.
The role of MBTPS1 (SKI-1/S1P) peptides in cancer and approaches used to inhibit SKI-1/S1P were studied.
study found that the N-acetylglucosamine-1-phosphotransferase alpha/beta-subunit precursor is cleaved by S1P that activates sterol regulatory element-binding proteins in response to cholesterol deprivation; S1P functions in the biogenesis of lysosomes
S1P has a role in reducing the size of the luminal domain to prepare ATF6 to be an optimal S2P substrate
enzymatic activity of S1P is not calcium dependent, but can be modulated by a variety of mono- and divalent cations. S1P displayed pronounced positive cooperativity with a substrate derived from the viral coat glycoprotein of the lassa virus.
SKI-1/S1P inhibition resulted in reduced cholesterol synthesis and mRNA levels of the rate-limiting enzymes, HMG-CoA reductase and squalene epoxidase, in the cholesterol synthetic pathway.
Complementation of SKI-1/S1P-deficient cells with a SKI-1/S1P expression vector restored release of infectious Crimean-Congo hemorrhagic fever virus (>106 PFU/ml), confirming that SKI-1/S1P processing is required for incorporation of viral glycoproteins.
Site 1 protease is required for proteolytic processing of the glycoproteins of the South American hemorrhagic fever viruses Junin, Machupo, and Guanarito.
The encoded protein has a central role in the regulation of lipid metabolism in cells. It is a sterol-regulated subtilisin-like serine protease that cleaves ER membrane-bound sterol regulatory element-binding proteins (SREBPs), a reaction that initiates the two-step proteolytic process by which transcriptionally active fragments of SREBPs are released from the membrane for translocation to the nucleus. The gene product is an integral membrane ER protein, with the bulk located in the ER lumen. It is synthesized as an inactive preproprotein that is self-activated by an intramolecular cleavage that generates the mature protein.
, membrane-bound transcription factor site-1 protease
, site-1 protease
, subtilisin/kexin isozyme-1
, S1P endopeptidase
, membrane-bound transcription factor protease, site 1
, sterol-regulated luminal protease
, subtilisin/kexin isozyme 1
, subtilisin/kexin isozyme SKI-1