| Source: |
Escherichia coli |
| Molecular Weight: |
Approximately 56.6 kDa, a single non-glycosylated polypeptide chain containing 502 amino acids. (MRGSGSHHHHHH-PDI). |
| AA Sequence: |
MRGSGSHHHH HHAPEEEDHV LVLRKSNFAE ALAAHKYLLV EFYAPWCGHC KALAPEYAKA AGKLKAEGSE IRLAKVDATE ESDLAQQYGV RGYPTIKFFR NGDTASPKEY TAGREADDIV NWLKKRTGPA ATTLPDGAAA ESLVESSEVA VIGFFKDVES DSAKQFLQAA EAIDDIPFGI TSNSDVFSKY QLDKDGVVLF KKFDEGRNNF EGEVTKENLL DFIKHNQLPL VIEFTEQTAP KIFGGEIKTH ILLFLPKSVS DYDGKLSNFK TAAESFKGKI LFIFIDSDHT DNQRILEFFG LKKEECPAVR LITLEEEMTK YKPESEELTA ERITEFCHRF LEGKIKPHLM SQELPEDWDK QPVKVLVGKN FEDVAFDEKK NVFVEFYAPW CGHCKQLAPI WDKLGETYKD HENIVIAKMD STANEVEAVK VHSFPTLKFF PASADRTVID YNGERTLDGF KKFLESGGQD GAGDDDDLED LEEAEEPDME EDDDQKAVKD EL |
| Purity: |
> 95% by SDS-PAGE and HPLC analyses. |
| Physical Appearance: |
Sterile filtered white lyophilized (freeze-dried) powder. |
| Formulation: |
Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH7.0. |
| Endotoxin: |
Less than 1 EU/µg of rHuPDI as determined by LAL method. |
| Reconstitution: |
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions. |
| Stability & Storage: |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
1 month, 2 to 8°C under sterile conditions after reconstitution.
3 months, -20 to -70°C under sterile conditions after reconstitution. |
| Synonyms: |
Cellular Thyroid Hormone-binding Protein, Prolyl 4-hydroxylase Subunit beta, p55 |
| Background: |
Protein disulfide isomerases (PDIs) form a family of enzymes with similar structures, active in catalyzing the formation, reduction, or rearrangement of disulfide bonds in newly synthesized proteins within the endoplasmic reticulum (ER). Acting also as chaperones, they contribute to the quality control system ensuring proper protein folding within this cellular compartment. Recombinant Human Protein Disulfide Isomerase plays a crucial role in both the formation and rearrangement of disulfide bonds in proteins, as well as in their reduction. in vitro studies have shown that recombinant PDI moderately enhances the rate of oxidative protein folding by approximately 25-fold. |
