重组人蛋白二硫键异构酶（Human PDI） 现货
Recombinant Human Protein Disulfide Isomerase

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• 技术参数
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技术参数

技术参数技术参数

FAQs

FAQsFAQs

Synonyms

Cellular Thyroid Hormone-binding Protein, Prolyl 4-hydroxylase Subunit beta, p55

Synonyms

Synonyms

Cellular Thyroid Hormone-binding Protein, Prolyl 4-hydroxylase Subunit beta, p55

Cellular Thyroid Hormone-binding Protein, Prolyl 4-hydroxylase Subunit beta, p55

Source

Escherichia coli.

Source

Source

Escherichia coli.

Escherichia coli.

Molecular Weight

Approximately 56.6 kDa, a single non-glycosylated polypeptide chain containing 502 amino acids. (MRGSGSHHHHHH-PDI).

Molecular Weight

Molecular Weight

Approximately 56.6 kDa, a single non-glycosylated polypeptide chain containing 502 amino acids. (MRGSGSHHHHHH-PDI).

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

AA Sequence

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

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.

Purity

Purity

> 95 % by SDS-PAGE and HPLC analyses.

> 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.

Thiol proteinReductase activity

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.

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.

Isomerase activity

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.

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.

Physical Appearance

Physical Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation

Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.0.

Formulation

Formulation

Lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.0.

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.

Endotoxin

Endotoxin

Less than 1 EU/µg of rHuPDI as determined by LAL method.

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.

Reconstitution

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.

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.

Stability & Storage

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.

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.

Usage

NOT FOR HUMAN USE.

Usage

Usage

NOT FOR HUMAN USE.

NOT FOR HUMAN USE.

SDS-PAGE

SDS-PAGE

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.

Reference

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.

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.

background

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.

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.