Recombinant Human Protein disulfide-isomerase(P4HB)

Code CSB-EP017342HU
Size US$1726
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names P4HB
Uniprot No. P07237
Research Area Cancer
Alternative Names Cellular thyroid hormone binding protein; Cellular thyroid hormone-binding protein; Collagen prolyl 4 hydroxylase beta; Disulphide Isomerase; DSI; EC 5.3.4.1; Endoplasmic reticulum resident protein 59; ER protein 59; ERBA2L; ERp59; GIT; Gltathione insulin transhydrogenase; Glutathione insulin transhydrogenase; P4HB; P4Hbeta; p55; PDI; PDIA1; PDIA1_HUMAN; PDIR; PHDB; PO4DB; PO4HB; Procollagen proline 2 oxoglutarate 4 dioxygenase (proline 4 hydroxylase) beta polypeptide (protein disulfide isomerase associated 1); Procollagen proline 2 oxoglutarate 4 dioxygenase beta subunit; PROHB; Prolyl 4 hydroxylase beta polypeptide; Prolyl 4 hydroxylase beta subunit; Prolyl 4 hydroxylase subunit beta; Prolyl 4-hydroxylase subunit beta; Protein disulfide isomerase associated 1; Protein disulfide isomerase, family A, member 1; Protein disulfide isomerase/oxidoreductase; Protein disulfide-isomerase; Protocollagen hydroxylase; Thbp; Thyroid hormone binding protein p55 ; Thyroid hormone binding protein p55 cellular; V erb a avian erythroblastic leukemia viral oncogene homolog 2 like
Species Homo sapiens (Human)
Source E.coli
Expression Region 18-508aa
Target Protein Sequence DAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 59.3kDa
Protein Length Full Length of Mature Protein
Tag Info N-terminal 6xHis-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

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
Gene References into Functions
  1. Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase. PMID: 29191937
  2. Overexpression of HIF-1alpha and P4HB is associated with poor prognosis in patients with gastric cancer. PMID: 29904245
  3. Study demonstrated that the expression of P4HB is frequently upregulated at the mRNA and protein levels in diffuse gliomas. Its high expression was significantly correlated with high Ki-67, more TP53 mutations and poor survival outcome. These findings imply that high expression of P4HB plays an important role in diffuse glioma progression. PMID: 29207176
  4. identify a potent and selective PDIA1 inhibitor, KSC-34, with 30-fold selectivity for the a site over the a' site. KSC-34 displays time-dependent inhibition of PDIA1 reductase activity in vitro with a kinact/ KI of 9.66 x 10(3) M(-1) s(-1) and is selective for PDIA1 over other members of the PDI family, and other cellular cysteine-containing proteins. PMID: 29521097
  5. P4HB promotes hepatocellular carcinoma progression by down-regulating GRP78 expression and subsequently promoting epithelial-to-mesenchymal transition. PMID: 28052026
  6. analysis of antiplatelet activity of CxxC through binding to Cys400 in the PDI a0 domain, which can be further exploited as a model for sitedriven antithrombotic agent development PMID: 28109047
  7. Current findings indicate that thiol isomerase-mediated disulfide bond modification in receptors and plasma proteins is an important layer of control of thrombosis and vascular function more generally. PMID: 28598864
  8. DIA1 was robustly secreted by physiological levels of arterial laminar shear in endothelial cells and supported alpha 5 integrin thiol oxidation. PMID: 28034831
  9. Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates. PMID: 28364042
  10. a mechanism of dual Ero1alpha regulation by dynamic redox interactions between PDI and the two Ero1alpha flexible loops that harbor the regulatory cysteines. PMID: 27703014
  11. analysis of how redox affects human protein disulfide isomerase regulate binding affinity of 17 beta-estradiol PMID: 28257787
  12. These findings improve our understanding of PDI-protected aggregation of wild-type alpha-Syn and its H50Q familial mutant. PMID: 27142583
  13. Association of P4HB polymorphisms with sporadic amyotrophic lateral sclerosis susceptibility in the Chinese Han population. PMID: 26000911
  14. the effect of the endoplasmic reticulum chaperone protein disulfide isomerase (PDI) on beta-cell dysfunction, was examined. PMID: 26607804
  15. Amyotrophic lateral sclerosis-linked PDIA1 mutations disrupt motor neuron connectivity. PMID: 26869642
  16. direct binding of PDIA1 to VWF, is reported. PMID: 26670633
  17. Selective sequestration of PDI1A in a calcium depletion-mediated complex with the abundant chaperone calreticulin attenuates the effective concentration of this major lumenal thiol oxidant. PMID: 25575667
  18. Cole-Carpenter syndrome is caused by a specific de novo mutation in P4HB that impairs the disulfide isomerase activity of protein disulfide isomerase. PMID: 25683117
  19. PDI has a role as a competent regulator and a specific substrate of Ero1alpha govern efficient and faithful oxidative protein folding and maintain the ER redox homeostasis PMID: 25258311
  20. The crystal structure of the dimeric form of noncatalytic bb' domains of human PDIA1 determined to 2.3 A resolution revealed that the formation of dimers occludes the substrate binding site. PMID: 24549644
  21. Elevated P4HB expression is associated with temozolomide resistance in malignant glioma. PMID: 23444257
  22. ). The results suggest that P4HB is a modifier gene inamyotrophic lateral sclerosis susceptibility and may represent a potential therapeutic target for amyotrophic lateral sclerosis . PMID: 23337974
  23. A mixed disulfide complex was formed with the catalytic domain A1 from human PDI consistent with a model for cotranslational oxidative protein folding wherein PDI acts as a placeholder that is relieved by the pairing of cysteines caused by substrate folding. PMID: 23141538
  24. TPM4, PDIA and SRC8 were also localized to the trophoblast cells, further highlighting the importance of these cytoskeletal remodelling proteins in early pregnancy PMID: 21373848
  25. these data revealed a redox-regulated chaperone function of PDI in delivering antigenic peptides from TAP to MHC-I. PMID: 21299467
  26. Functional PDI is rapidly secreted from human umbilical vein endothelial cells in culture upon activation with thrombin or after laser-induced stimulation. PMID: 20668226
  27. domain c is required for the stabilization and maintenance of the chaperone function of PDI under extreme conditions PMID: 15358778
  28. data indicate that binding sites in three PDI domains, a, b', and a', contribute to efficient C-P4H tetramer assembly PMID: 15590633
  29. PDI can be S-nitrosated and PDI-SNO can be denitrosated by PDI suggesting that this enzyme could be intimately involved in the transport of intracellular NO equivalents to the cell surface. PMID: 15611098
  30. Data show that protein disulfide isomerase can switch its conformation from dimer to tetramer in its functions as a foldase. PMID: 15695804

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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
Database Links

HGNC: 8548

OMIM: 112240

KEGG: hsa:5034

STRING: 9606.ENSP00000327801

UniGene: Hs.464336

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