Specification
| Organism | Homo sapiens (Human) |
| Expression Host | E.Coli |
| Tag Info | N-terminal 6xHis-tagged |
| Purity | >95% as determined by SDS-PAGE and HPLC. |
| Uniprot ID | P07237 |
| Uniprot Entry Name | PDIA1_HUMAN |
| Gene Names | P4HB,ERBA2L,PDI,PDIA1,PO4DB |
| Alternative Names | PDI, Cellular thyroid hormone-binding protein, Prolyl 4-hydroxylase subunit beta, p55, |
| Expression Region | Partial (19-508aa) |
| Molecular Weight | 56.6 kDa |
| Endotoxin | Less than 1.0 EU/µg as determined by LAL method. |
| Sequence | MRGSGSHHHHHH+ APEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL |
| Product Form | Lyophilized powder (Lyophilized from a 0.2 µm filtered PBS, pH 7.0) |
| Reconstitution | Please reconstitute protein in deionized sterile water and we recommend that briefly centrifuge thevial prior to opening the vial .We recommend aliquot for long-term storage at -20℃/-80℃. |
Background
| 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. {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:12485997}. |
| 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 | Cole-Carpenter syndrome 1 (CLCRP1) |
| Subcellular Location | Endoplasmic reticulum, Endoplasmic reticulum lumen, Melanosome, Cell membrane, Peripheral membrane protein |
| Protein Families | Protein disulfide isomerase family |
| Tissue Specificity | |
| Pathway | Proteinprocessinginendoplasmicreticulum |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |