Synthetic peptide directed towards the N terminal region of human SURF4
Działania biochem./fizjol.
SURF4 is a conserved integral membrane protein containing multiple putative transmembrane regions. In eukaryotic cells, protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non-clathrin-coated vesicular coat proteins (COPs). The specific function of this protein has not been determined but its yeast homolog is directly required for packaging glycosylated pro-alpha-factor into COPII vesicles. This gene is located in the surfeit gene cluster, which is comprised of very tightly linked housekeeping genes that do not share sequence similarity. The encoded protein is a conserved integral membrane protein containing multiple putative transmembrane regions. In eukaryotic cells, protein transport between the endoplasmic reticulum and Golgi compartments is mediated in part by non-clathrin-coated vesicular coat proteins (COPs). The specific function of this protein has not been determined but its yeast homolog is directly required for packaging glycosylated pro-alpha-factor into COPII vesicles. This gene uses multiple polyadenylation sites, resulting in transcript length variation. The existence of alternatively spliced transcript variants has been suggested, but their validity has not been determined.
Sekwencja
Synthetic peptide located within the following region: GQNDLMGTAEDFADQFLRVTKQYLPHVARLCLISTFLEDGIRMWFQWSEQ
Postać fizyczna
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
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Accumulating evidence suggests that protein S-nitrosylation is enzymatically regulated and that specificity in S-nitrosylation derives from dedicated S-nitrosylases and denitrosylases that conjugate and remove S-nitrosothiols, respectively. Here, we report that mice deficient in the protein denitrosylase SCoR2 (S-nitroso-Coenzyme A Reductase
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