Synonyms
|
Cellular Thyroid Hormone-binding Protein, Prolyl 4-hydroxylase Subunit beta, p55
|
Species
|
Human
|
Source
|
Escherichia coli.
|
Molecular Weight
|
Approximately 56.6 kDa, a single non-glycosylated polypeptide chain containing 502 amino acids. (MRGSGSHHHHHH-PDI).
|
Quantity
|
20µg/100µg/1000µg
|
AA Sequence
|
重组人类蛋白二硫键异构酶蛋白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
|
重组人类蛋白二硫键异构酶蛋白> 95 % by SDS-PAGE and HPLC analyses.
|
Thiol proteinReductase activity
|
Thiol Protein Reductase Activity is 0.001 Δ650nm/ min-2, determined by measuring the turbidity increase at 650 nm due to insulin reduction. The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag time.
|
Isomerase activity
|
Isomerase Activity is 0.5 µmol active RNase A min-1 µmol PDI-1, according to the re-activation of reduced and denatured RNase A.
|
Physical Appearance
|
Sterile Filtered White lyophilized (freeze-dried) powder.
|
Formulation
|
重组人类蛋白二硫键异构酶蛋白Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.0.
|
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.
|
Storage
|
This lyophilized preparation is stable at 2-8 °C, but should be kept at -20 °C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8 °C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20 °C to -70 °C. Avoid repeated freeze/thaw cycles.
|
重组人类蛋白二硫键异构酶蛋白
|
|
SDS-PAGE
|
|
Reference
|
1. Pihlajaniemi, T., T. Helaakoski, K. Tasanen, et al. 1987. EMBO J, 6: 643-9.
2. Tasanen, K., T. Parkkonen, L.T. Chow, et al. 1988. J Biol Chem, 263: 16218-24.
3. Wilkinson, B., and H.F. Gilbert. 2004. Biochim Biophys Acta, 1699: 35-44.
|
Background
|
Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.
|