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  4. Recombinant Human Endoplasmic reticulum chaperone BiP (HSPA5), partial

Recombinant Human Endoplasmic reticulum chaperone BiP (HSPA5), partial

In Stock
  • 货号：
    CSB-EP010827HU1
  • 规格：
    ￥1344
  • 图片：
    • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • 其他：

产品详情

  • 纯度：
    Greater than 90% as determined by SDS-PAGE.
  • 基因名：
  • Uniprot No.：
  • 别名：
    78 kDa glucose regulated protein; 78 kDa glucose-regulated protein; AL022860; AU019543; BIP; D2Wsu141e; D2Wsu17e; Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78; Endoplasmic reticulum lumenal Ca2+ binding protein grp78; Epididymis secretory sperm binding protein Li 89n; FLJ26106; Glucose Regulated Protein 78; Glucose Regulated Protein 78kDa; GRP 78; GRP-78; GRP78; GRP78_HUMAN; Heat shock 70 kDa protein 5; Heat Shock 70kDa Protein 5; Heat shock protein family A (Hsp70) member 5; HEL S 89n; Hsce70; HSPA 5; HSPA5; Immunoglobulin Heavy Chain Binding Protein; Immunoglobulin heavy chain-binding protein; mBiP; MIF2; Sez7
  • 种属：
    Homo sapiens (Human)
  • 蛋白长度：
    Partial
  • 来源：
    E.coli
  • 分子量：
    33.6kDa
  • 表达区域：
    25-293aa
  • 氨基酸序列
    EDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVE
    Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
  • 蛋白标签：
    N-terminal 6xHis-tagged
  • 产品提供形式：
    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.
  • 缓冲液：
    Tris-based buffer,50% glycerol
  • 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：
    3-7 business days
  • 注意事项：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • 产品描述：

    The process of expressing this Human HSPA5 recombinant protein in E.coli expression system requires the following steps: use of competent E. coli cells to take up DNA sequence of interest, the exogenous plasmid is transferred into the cell, and the transcription and translation are directly replicated in the cell, selection of transformed E. coli using a selection marker, expansion of selected E. coli to a higher scale in appropriate culture media, such as classic LB options Growth Systems and lastly isolation and purification.And we finally get a partial HSPA5 protein with N-terminal 6xHis tag and it is determined by SDS-PAGE with a purity of 90%+.

    HSPA5 is a protein coding gene that encodes Endoplasmic reticulum chaperone BiP. According to some studies, HSPA5 may have the following features.
    HSPA5 regulates sideroblast death in cancer cells. Inhibition of SIRT1/2 results in HSPA5 acetylation and dissociation from EIF2AK3, leading to an ER stress response followed by upregulation of ATF4 and DDIT4, triggering autophagy. Hspa5 plays a crucial role in the formation of the pronephros, which is partly mediated through RA signaling during early embryonic development. Post-translational regulation of HSPA5 protein is critical for the metastatic properties of HSPA5-mediated breast cancer.

  • Datasheet & COA：
    Please contact us to get it.

产品评价

靶点详情

  • 功能：
    Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1. Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation.; (Microbial infection) Plays an important role in viral binding to the host cell membrane and entry for several flaviruses such as Dengue virus, Zika virus and Japanese encephalitis virus. Acts as a component of the cellular receptor for Dengue virus serotype 2/DENV-2 on human liver cells.; (Microbial infection) Acts as a receptor for CotH proteins expressed by fungi of the order mucorales, the causative agent of mucormycosis, which plays an important role in epithelial cell invasion by the fungi. Acts as a receptor for R.delemar CotH3 in nasal epithelial cells, which may be an early step in rhinoorbital/cerebral mucormycosis (RCM) disease progression.
  • 基因功能参考文献：
    1. the in-vitro anti-proliferative and pro-apoptotic effects in colorectal cancer cells that were induced by silencing cell migration inducing hyaluronan binding protein may be associated with GRP78 repression and UPR attenuation PMID: 29024602
    2. Cell surface GRP78 promotes cancer stemness, whereas drives cells toward a non-stemlike phenotype when it chaperones Progranulin. PMID: 29323121
    3. We showed that GRP78 is elevated in diabetic macular edema patients. In addition, there is a correlation between GRP78 and VEGF levels in aqueous humor. However, GRP78 levels were not associated with the responsiveness of anti-VEGF in diabetic macular edema patients. PMID: 30407281
    4. Data suggest that prostatic tumor GRP78 expression correlates with disease stage; anti-GRP78 autoantibody levels parallel prostate-specific antigen concentrations in patient-derived serum samples. PMID: 29066620
    5. High GRP78 expression is associated with radioresistance in nasopharyngeal carcinoma. PMID: 30015969
    6. Data suggest a complex but functional interplay of ER chaperone GRP78 and steroid hormones, working together for cell survival and proliferation in the context of reproduction. PMID: 29932125
    7. the physiological role played by the complex KCTD15-GRP78 in the adipogenesis PMID: 29665387
    8. Concomitant high expression of ERalpha36, GRP78 and GRP94 is associated with aggressive papillary thyroid cancer behavior and may be used as a predictor for extrathyroid extension, lymph node metastasis, and distant metastasis. PMID: 29368272
    9. We found that downregulation of GRP78 led to inhibition of autophagy, cell cycle arrest in the G0/G1 phase, and activation of caspase-7-induced apoptosis, and this was affected by the initial autophagy level. PMID: 29749510
    10. GRP78 promotes cigarette smoke-induced inflammatory response and mucus hyperproduction in airway epithelial cells, likely through upregulation of necroptosis and subsequent activation of NF-kappaB and AP-1 pathways. PMID: 29445274
    11. Data suggested that GRP78 silencing increased chemo-sensitivity and improved the effects of cisplatin-induced apoptosis in SiHa cells. Moreover, inhibition of GRP78 could upregulate caspase-3 and CHOP expression and downregulate Bcl-2 expression. PMID: 29650944
    12. Upon IgM expression, its levels temporarily eclipse those of the endoplasmic reticulum chaperone BiP, leading to acute, full-geared unfolded protein response activation. Once BiP is in excess again, the unfolded protein response transitions to chronic, submaximal activation, indicating that the unfolded protein response senses endoplasmic reticulum stress in a ratiometric fashion. PMID: 29251598
    13. GRP78 binds to and acts in concert with a glycosylphosphatidylinositol-anchored protein, CD109, in blocking TGF-beta signaling by promoting the routing of the TGF-beta receptor to the caveolae, thereby disrupting its binding to and activation of Smad2. PMID: 29654145
    14. this study demonstrates the reaction of placental GRP78 with sera from women with multiple sclerosis PMID: 29276183
    15. This meta-analysis shows that BiP or anti-BiP antibodies have a moderate accuracy for the diagnosis of rheumatoid arthritis with a moderate sensitivity and high specificity. It can be an efficient supplement to the existing diagnostic method. [Meta-Analysis] PMID: 29185956
    16. the expression of three cytokines for the pathogenesis of osteoarthritis (OA). which include IL-1beta, MMP14 and GRP78 was decreased by the various concentrations of icariin. These preliminary results imply that icariin might be an effective compound for the treatment of OA disease. PMID: 29292760
    17. In a retrospective cervical cancer cohort, high GRP78 expression was correlated with poor survival. miR-181a suppressed cervical cancer development via downregulating GRP78. PMID: 28245171
    18. We revealed that DAL-1 was downregulated while HSPA5 was upregulated in NSCLC and found the protein of DAL-1 and HSPA5 co-localized in the cytoplasm and nucleus. We demonstrated that DAL-1 can suppress the expression of HSPA5 on mRNA and protein levels, and decrease EMT, migration, invasion and proliferation abilities by down-regulating HSPA5 PMID: 29048640
    19. We found that inhibiting the function of surface GRP78 suppressed cancer cell survival and growth proving that the surface-expressed GRP78 is a vital receptor involved in the proliferation of high-grade glioma. PMID: 27713511
    20. BiP/GRP78 is significantly associated with tumor aggressiveness and progression. The increased expression of BiP/GRP78 was identified as an independent factor for predicting poor OS in patients with early stage of disease. PMID: 28854502
    21. GRP78 overexpression decreased advanced glycation end product levels and rescued the cells from Ribosome-induced cytotoxicity. PMID: 29410209
    22. This study established a macrophage polarization model with human monocytes and found that the conditioned medium from M2 macrophages increased GRP78 expression in tumor cells and facilitated tumor cell migration. PMID: 28629783
    23. GRP78 silencing promoted lung epithelial cell apoptosis during hyperoxia, via regulation of the CHOP pathway. PMID: 28586043
    24. GRP78 role in dengue virus infection. PMID: 27779201
    25. Overexpression of GRP78 is a novel predictor of favorable outcomes in patients with advanced thymic carcinoma. who receive combination chemotherapy. PMID: 28550415
    26. GRP78 is an autoantigen that could stimulate autoimmune responses and serve as a potential marker for recurrent and metastatic progression in HCC. PMID: 28186997
    27. These results identify GRP78 antibodies as a potential component of Neuromyelitis optica pathogenesis. PMID: 28679661
    28. HSPA5 (GRP78) and GEP were identified to interact. Clinical analysis showed that expression of GRP78 was up-regulated in hepatocellular carcinoma tumor and correlated with GEP expression. PMID: 28601093
    29. an endoplasmic reticulum complex of resident chaperones that includes HSP47, FKBP65, and BiP regulating the activity of LH2. PMID: 28177155
    30. The present study indicates that GRP78 is increased in BALF in cigarette smokers; that HAEC secrete GRP78; and that GRP78 secretion by HAEC is augmented by cigarette smoke particulates. Enhanced secretion of GRP78 by lung cells makes it a potential biomarker of cigarette smoke-induced lung injury. PMID: 28464871
    31. P4HB promotes hepatocellular carcinoma progression by down-regulating GRP78 expression and subsequently promoting epithelial-to-mesenchymal transition. PMID: 28052026
    32. analysis of the effects of triptolide on cell proliferation, cell cycle and the expression of GRP78 in nasopharyngeal carcinoma PMID: 27391061
    33. Antibodies targeting GRP78 exhibited antitumor activity and enhanced the efficacy of radiation in Non-small cell lung cancer and glioblastoma multiforme both in vitro and in vivo GRP78 is a promising novel target, and anti-GRP78 antibodies could be used as an effective cancer therapy alone or in combination with ionizing radiation PMID: 27815359
    34. Novel finding of the current study is that the level of GRP78/BiP was greatly increased in the Parkinson's disease dementia and dementia with Lewy bodies patients compared with people with Alzheimer's disease in cingulate gyrus and parietal cortex. PMID: 26202523
    35. Bisdemethoxycurcumin promotes apoptosis through a GRP78-dependent pathway and mitochondrial dysfunctions, and potentiates the antitumor effect of gemcitabine in human pancreatic cancer cells. PMID: 27845899
    36. Results identified GRP78 and HSP90a as binding partners of PRDM14 in triple-negative breast cancer cells, and all participate in cancer regulation. The interactions were direct and required the C-terminal region including the zinc finger motifs of PRDM14. PMID: 29178343
    37. GRP78 affects p53 localization which in turn regulates autophagy. PMID: 27814589
    38. candidate genes that modulate Hspa5 expression in the retina, were examined. PMID: 27881906
    39. Overexpression or knockdown demonstrated that GRP78 promoted proliferation and anti-apoptosis of clear cell renal cell carcinoma cells, and the oncogenic activity of GRP78 resulting in by miR-30a-5p overexpression. PMID: 29073630
    40. this study provided mechanistic evidences to support the positive regulatory function of FOXM1 in HSPA5 expression in colorectal cancer PMID: 27034162
    41. Cancer-associated fibroblasts induced GRP78 expression in A549 and SPCA-1 cells to facilitate Non-Small Cell Lung Cancer cell migration and invasion PMID: 27016417
    42. results suggest that the cooperative effects of radiotherapy and cetuximab could be further improved by inhibiting GRP78 in non-responsive oropharyngeal carcinoma patients PMID: 29232380
    43. Study reports that the endoplasmic reticulum luminal co-chaperone ERdj4/DNAJB9 is a selective IRE1 repressor that promotes a complex between the luminal Hsp70 BiP and the luminal stress-sensing domain of IRE1alpha. PMID: 29198525
    44. GRP78 role in the resistance to cisplatin in the nasopharyngeal carcinoma cells. PMID: 27254284
    45. High expression of GRP78 is associated with nonalcoholic steatohepatitis. PMID: 28951310
    46. Data show that cancer-associated fibroblasts (CAFs)-derived hepatocyte growth factor (HGF) or recombinant HGF activated c-Met/phosphoinositide 3-kinase (PI3K)/Akt and glucose-regulated protein 78 (GRP78) signalling pathways in ovarian cancer cells. PMID: 28258248
    47. HSPA5/BIP has roles in endoplasmic reticulum stress, autophagy and apoptosis; inhibitors of HSPA5 could be useful in cancer treatment PMID: 27791469
    48. Immunohistochemical analysis showed that STAT3, GRP78 and BAX protein levels in the combination group were significantly higher than those in STAT3 group and CDDP group (P<0.05). Exogenous STAT3 and CDDP may synergistically inhibit the xenograft tumour growth through up-regulation of BAX protein via GRP78. PMID: 27129294
    49. GRP78 inhibition enhances ATF4-induced cell death by the deubiquitination and stabilization of CHOP in human osteosarcoma cells. PMID: 28947141
    50. the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD against PDI-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 inhibition. PMID: 28949004

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  • 相关疾病：
    Autoantigen in rheumatoid arthritis.
  • 亚细胞定位：
    Endoplasmic reticulum lumen. Melanosome. Cytoplasm. Cell surface.
  • 蛋白家族：
    Heat shock protein 70 family
  • 数据库链接：

    HGNC: 5238

    OMIM: 138120

    KEGG: hsa:3309

    STRING: 9606.ENSP00000324173

    UniGene: Hs.743241