Recombinant Cricetulus griseus Protein disulfide-isomerase(P4HB) CSB-YP823188DXU
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Prolyl 4-hydroxylase subunit beta p58
Species: (Organism)
Chinese hamster
Gene Names:
P4HB
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
DAPEEEDNVLVLKKSNFAEALAAHNYLLVEFYAPWCGHCKALAPEYAKAAAKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLSDTAAAETLIDSSEVAVIGFFKDVESDSAKQFLLAAEAVDDIPFGITSNSGVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLGNFKKAAEGFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIIIAKMDSTANEVEAVKVHSFPTLKFFPATADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDVDLEEALEPDMEEDDDQKAVKDEL
Expression Region:
20-509aa
Subcellular Location:
Endoplasmic reticulum, Endoplasmic reticulum lumen, Melanosome, Cell membrane, Peripheral membrane protein
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
57 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Signal Transduction
Function:
This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration.
Involvement in disease:
Relevance:
This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration.
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Protein disulfide isomerase family
Reference:
"Protein-disulfide isomerase is a component of an NBD-cholesterol monomerizing protein complex from hamster small intestine."Cai T.-Q., Guo Q., Wong B., Milot D., Zhang L., Wright S.D.Biochim. Biophys. Acta 1581:100-108(2002)
