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  4. Recombinant Human Protein disulfide-isomerase A2 (PDIA2)

Recombinant Human Protein disulfide-isomerase A2 (PDIA2)

  • 货号：
    CSB-YP614390HU
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 货号：
    CSB-EP614390HU
  • 规格：
  • 来源：
    E.coli
  • 其他：
  • 货号：
    CSB-EP614390HU-B
  • 规格：
  • 来源：
    E.coli
  • 共轭：
    Avi-tag Biotinylated

    E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.

  • 其他：
  • 货号：
    CSB-BP614390HU
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 货号：
    CSB-MP614390HU
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
    PDIA2
  • Uniprot No.：
  • 别名：
    Pancreas specific protein disulfide isomerase; Pancreas-specific protein disulfide isomerase; Pancreatic protein disulfide isomerase; PDA2; PDI; PDIA2; PDIA2_HUMAN; PDIp; PDIR; Protein disulfide isomerase A2; Protein disulfide isomerase; Protein disulfide isomerase associated 2; Protein disulfide isomerase family A member 2; Protein disulfide isomerase pancreatic; Protein disulfide-isomerase A2; Rho GDP dissociation inhibitor gamma
  • 种属：
    Homo sapiens (Human)
  • 蛋白长度：
    Full Length of Mature Protein
  • 表达区域：
    22-525
  • 氨基酸序列
    QEQGARSPS EEPPEEEIPK EDGILVLSRH TLGLALREHP ALLVEFYAPW CGHCQALAPE YSKAAAVLAA ESMVVTLAKV DGPAQRELAE EFGVTEYPTL KFFRNGNRTH PEEYTGPRDA EGIAEWLRRR VGPSAMRLED EAAAQALIGG RDLVVIGFFQ DLQDEDVATF LALAQDALDM TFGLTDRPRL FQQFGLTKDT VVLFKKFDEG RADFPVDEEL GLDLGDLSRF LVTHSMRLVT EFNSQTSAKI FAARILNHLL LFVNQTLAAH RELLAGFGEA APRFRGQVLF VVVDVAADNE HVLQYFGLKA EAAPTLRLVN LETTKKYAPV DGGPVTAASI TAFCHAVLNG QVKPYLLSQE IPPDWDQRPV KTLVGKNFEQ VAFDETKNVF VKFYAPWCTH CKEMAPAWEA LAEKYQDHED IIIAELDATA NELDAFAVHG FPTLKYFPAG PGRKVIEYKS TRDLETFSKF LDNGGVLPTE EPPEEPAAPF PEPPANSTMG SKEEL
  • 蛋白标签：
    Tag type will be determined during the manufacturing process.
    The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
  • 产品提供形式：
    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.
  • 复溶：
    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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    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.
  • 货期：
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事项：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet ：
    Please contact us to get it.

产品评价

靶点详情

  • 功能：
    Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins.
  • 基因功能参考文献：
    1. Galectin-9, a soluble lectin expressed by T cells, endothelial cells and dendritic cells, binds to and retains PDI on the cell surface. PMID: 28810662
    2. PDI overexpression is associated with Multiple Myeloma. PMID: 27197150
    3. Tissue factor-regulated vascular smooth cell migration and microvessel formation is under the control of the ER-protein PDIA2. PMID: 25631539
    4. It was found that PDI interacts with dengue virus nonstructural protein 1 (NS1) intracellularly as well as on the surface in the lipid raft domain. PMID: 25664880
    5. Data show that cell surface disulfide isomerase (PDI) expression and function regulate the capacity of natriuretic peptides to generate cyclic guanosine monophosphate (cGMP) through interaction with their receptors. PMID: 25419565
    6. The redox-regulated open/closed conformational switch of hPDI endows the protein with versatile target-binding capacities for its enzymatic and chaperone functions. PMID: 22657537
    7. These results indicate that BPA, a widely distributed and potentially harmful chemical, inhibits Ero1-PDI-mediated disulfide bond formation. PMID: 25122773
    8. PDI appears to regulate cytoskeletal reorganization by the thiol-disulfide exchange in beta-actin via a redox-dependent mechanism. PMID: 24415753
    9. Data indicate that protein disulfide isomerase (PDI) and ERp44 dynamically localize Ero1alpha and peroxiredoxin 4 in early secretory compartment (ESC). PMID: 23979138
    10. GPx7 is an unusual CysGPx catalyzing the peroxidatic cycle by a one Cys mechanism in which GSH and PDI are alternative substrates. PMID: 23454490
    11. Human major histocompatibility complex class 1 antigens (HLA-A,B,C) are potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation. PMID: 23167757
    12. Data indicate that apoptosis induced by misfolded PrP proteins could be regulated by protein disulfide isomerase (PDI) via mitochondrial dysfunction. PMID: 22685557
    13. The hydrogen bond, formed between the 3-hydroxyl group of Estradiol (E(2)) (donor) and pancreas-specific protein disulfide isomerase's His278 (acceptor), is indispensable for its binding. PMID: 21080683
    14. PDI is required to support Nox1/redox and GTPase-dependent VSMC migration. PMID: 22773830
    15. PDI exhibits unfoldase activity for proinsulin, increasing retention of proinsulin within the ER of pancreatic beta-cells PMID: 22105075
    16. Data show that diabetic patients had a greater number of transferase-mediated dUTP nick-end labeling-positive cells than nondiabetic patients despite a greater myocardial protein disulfide isomerase (PDI)expression suggesting altered PDI function. PMID: 21637911
    17. surface-associated PDI is an important regulator of coagulation factor ligation to thrombin-stimulated platelets and of subsequent feedback activation of platelet thrombin generation PMID: 21929690
    18. mechanistic insights into the redox-regulated chaperone activity of human PDI. PMID: 22090031
    19. the intramolecular electron transfer from the a domain to the a' domain within PDI during its oxidation by ERO1alpha. PMID: 21757736
    20. tein disulfide isomerase redox-dependent association with p47(phox): evidence for an organizer role in leukocyte NADPH oxidase activation. PMID: 21791598
    21. Protein disulfide isomerase blocks CEBPA translation and is up-regulated during the unfolded protein response in acute myeloid leukemia. PMID: 21471526
    22. PDI knockdown-induced cell death is cell-line-dependent and involves apoptosis in MCF-7 cells. PMID: 21297336
    23. PDI is a major target of post-streptococcal autoimmunity. PMID: 20886095
    24. These results suggest that PDI could be a therapeutic target to prevent ER stress in neuronal cells in Alzheimer disease. PMID: 20550946
    25. PDI has a role in regulating tissue factor that involves FVIIa activity [review] PMID: 20163832
    26. Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3. PMID: 20562109
    27. Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance. PMID: 20516074
    28. new mechanism for PDI contribution to coagulation on endothelial cells, namely, the regulation of PS exposure, where PDI acts as a negative regulator of coagulation PMID: 20448108
    29. Among target genes of XBP-1, expression of protein disulfide isomerase (PDI), but not glucose- regulated protein 78 (GRP78), was increased in AD PMID: 20368688
    30. an appropriate Ero1alpha-PDI ratio is critical for regulating the binding-release cycle of CTA1 by PDI during retro-translocation, and PDI's redox state has a role in targeting it to the retro-translocon PMID: 20130085
    31. Selective expression of pancreas-specific protein disulfide-isomerase confers strong protection against heat shock and oxidative-stress-induced cell death. PMID: 20423326
    32. The absence of PDIp expression in pancreatic adenocarcinoma may serve as an additional biomarker for pancreatic cancer. PMID: 19821078
    33. A haplotype within the AXIN1-PDIA2 locus (p-value of 2.926x10(-06)) and a haplotype within the Endoglin gene (p-value of 5.881x10(-04)) were found to be strongly associated with bicuspid aortic valve PMID: 20098615
    34. The b domain of human PDI tends to form homodimers - both in isolation and in other contexts. This tendency is moderated by the adjacent x region, which can bind to a surface patch on the b domain. PMID: 19844948
    35. Evidence that protein disulfide isomerase (PDI) is involved in DNA-nuclear matrix anchoring. PMID: 11968009
    36. role of association with ubiquilin in the endoplasmic reticulum in stress-induced apoptotic cell death PMID: 12095988
    37. dissociation of PDI from substrates observed in the presence of glutathione disulfide can be explained by competition for the peptide-binding site on PDI PMID: 12485997
    38. PDI has a role in conferring resistance to apoptosis under hypoxia and a potential role in the oxygen-sensing apparatus PMID: 12766950
    39. study of the principal substrate binding site of PDI PMID: 14684740
    40. Low resolution structure of the entire PDI molecule in solution has been determined for the first time by the small angle X-ray scattering technique PMID: 16407203
    41. PDI stabilizes a peptide-receptive site by regulating oxidation state of the disulfide bond in MHC peptide-binding groove, an essential function for selecting optimal peptides; link between thiol-based redox regulation & antigen processing established PMID: 17055437
    42. These data indicate that cytosolic PDI is a substrate of caspase-3 and -7, and that it has an anti-apoptotic action. PMID: 17978580
    43. Study shows that SUMF1 interacts with protein disulfide isomerase (PDI) and ERp44, two thioredoxin family members residing in the early secretory pathway, and with ERGIC-53, a lectin that shuttles between the ER and the Golgi. PMID: 18508857
    44. Platelet microparticle-associated PDI promotes platelet aggregation and inactivates insulin. PMID: 18691554
    45. The x region of PDI can adopt alternative conformations during the functional cycle of PDI action and that these are linked to the ability of PDI to interact with folding substrates. PMID: 18801374
    46. a role for both GRP78 and PDI in insulin biosynthesis, although an excess of PDI disrupts normal proinsulin processing. PMID: 19103594
    47. structures and functions of human PDIp are redox-regulated through formation of an inter-subunit disulfide bond between two cysteine-4 residues PMID: 19150607
    48. the solution structure of the second and third domains of human protein disulfide isomerase (b and b', respectively) by triple-resonance NMR spectroscopy and molecular modeling PMID: 19187238
    49. PDIp can also serve as an effective modulator of the cellular levels and biological actions of endogenous estrogens in the pancreas where estrogen receptors alpha and beta and PDIp are co-present. PMID: 19429457
    50. The b' domain of PDI contributes to binding unfolded proteins; its structure is stabilized by the b domain. PMID: 19636846

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  • 亚细胞定位：
    Endoplasmic reticulum lumen.
  • 蛋白家族：
    Protein disulfide isomerase family
  • 组织特异性：
    Highly expressed in pancreas (at protein level).
  • 数据库链接：

    HGNC: 14180

    OMIM: 608012

    KEGG: hsa:64714

    STRING: 9606.ENSP00000219406

    UniGene: Hs.66581