Recombinant Human Endoplasmin(HSP90B1),partial

Code CSB-EP010814HU1
Size US$1726Purchase it in Cusabio online store
(only available for customers from the US)
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-RP108894h could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HSP90B1.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-RP108894h could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HSP90B1.
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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names HSP90B1
Uniprot No. P14625
Research Area Metabolism
Alternative Names 94 kDa glucose regulated protein; 94 kDa glucose-regulated protein; ECGP; Endoplasmin; Endothelial cell (HBMEC) glycoprotein; ENPL_HUMAN; Glucose regulated protein 94kDa; gp96; gp96 homolog; GRP 94; GRP-94; Heat shock protein 90 kDa beta member 1; heat shock protein 90kDa beta (Grp94); member 1; Heat shock protein; 90 kDa; beta; 1; HSP90B1; Stress inducible tumor rejection antigen GP96; TRA1; tumor rejection antigen (gp96) 1; Tumor rejection antigen 1; Tumor rejection antigen gp96; Tumor rejection antigen-1 (gp96)
Species Homo sapiens (Human)
Source E.coli
Expression Region 27-799aa
Target Protein Sequence VDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVLDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEEETAKESTAE
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 93.1kDa
Protein Length Partial
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 Tris-based buffer,50% glycerol
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 Basically, we can dispatch the products out in 1-3 working days after receiving your orders. 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.
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.

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Target Background

Function
(From Uniprot)
Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity.
Gene References into Functions
  1. Glucose-regulated protein GRP94 contributes to the development of an aggressive phenotype in breast cancer cells. PMID: 29852388
  2. 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
  3. Overexpressed miR-150 attenuates hypoxia-induced human cardiomyocyte cell apoptosis by targeting GRP94. PMID: 29328381
  4. Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90beta as a molecular model for myotonia congenita has been described. PMID: 27580824
  5. Study demonstrated that the lack of gp96 in both the human monocytic cell line MM6 and in macrophages from LysMcre-gp96 floxed mice neither leads to a complete loss of TLR 2 expression nor to a complete loss of TLR-induced signaling, but is associated with an impaired phosphorylation of ERK and p38. These results reveal for the first time a crucial role for gp96 in the regulation of ERK and p38 kinases. PMID: 29447283
  6. HSP-gp96 promotes T cell response, enhances DC antigen presentation and induces cytokine secretion in human gastric cancer cell lines. PMID: 28706421
  7. our results besides adding further evidence in support of Grp94 as the shared tumor antigen in tumors of the GI tract, prove that it can be measured in plasma as valuable diagnostic marker of disease in the form of complexes with IgG that also exert immune-modulating activities on circulating immune cells. PMID: 27662661
  8. High GRP94 expression is associated with endometrioid adenocarcinoma. PMID: 26910913
  9. Immuno-stimulating peptide derived from HMGB1 is more effective than the N-terminal domain of Gp96 as an endogenous adjuvant for improvement of protein vaccines. PMID: 28000571
  10. These data demonstrate the essential role of the gp96-TLR interaction in priming T cell immunity and provide further molecular basis for the coupling of gp96-mediated innate with adaptive immunity. PMID: 27183126
  11. mutations in GRP94 that affect its IGF chaperone activity represent a novel causal genetic mechanism that limits IGF biosynthesis, quite a distinct mechanism from the known genes in the GH/IGF signaling network. PMID: 26982636
  12. In this instance, the ATP5B/CALR/HSP90B1/HSPB1/HSPD1-signaling network was revealed as the predominant target which was associated with the majority of the observed protein-protein interactions. As a result, the identified targets may be useful in explaining the anticancer mechanisms of ursolic acid and as potential targets for colorectal cancer therapy. PMID: 28347227
  13. High HSP90B1 expression is associated with non-small-cell lung cancer. PMID: 27599983
  14. data suggest that the GRP94/CCT8/c-Jun/EMT signaling cascade might be a new therapeutic target for HCC PMID: 26718209
  15. We filtered four OSCC genes including SERPINB9, SERPINE2, GAK, and HSP90B1 through the gene global prioritization score (P < 0.005). PMID: 26318431
  16. Our results demonstrated that GRP94 is a key molecule in Hepatocellular carcinoma (HCC) progression that modulates the AKT pathway and eNOS levels PMID: 26493996
  17. Results indicate that FN14 and GRP94 are prediction/prognosis markers which open up new possibilities for preventing/treating brain metastasis in breast cancer patients. PMID: 26497551
  18. This study clarifies a Grp94-mediated ERAD pathway for GABAA receptors, which provides a novel way to finely tune their function in physiological and pathophysiological conditions. PMID: 26945068
  19. GRP94 knockdown cells are defective in intracellular transport and, consequently, negatively impact the trafficking of F-actin toward the cellular cortex, integrin alpha2 and integrin alphaL toward the cell membrane and filopodia PMID: 26872972
  20. Our results indicate that GRP94 and TRAP1 might contribute more to the carcinogenesis or biology of SCLC than HSP90alpha and HSP90beta PMID: 26464709
  21. These results demonstrated the pivotal role of HSP90B1 in the proliferation and survival of ovarian cells, suggesting a critical role for HSP90B1 in the pathogenesis of PCOS. PMID: 27046189
  22. data suggest a role of infection-induced Gp96 shedding in the protection of the chlamydial replicative niche PMID: 26235316
  23. Hsp90-beta protein was over-expressed in lung adenocarcinoma tissues and was associated with poor outcomes in early stage tumors and low pathological grade tumors. PMID: 26339394
  24. Data identified critical players in the pathogenesis of chronic lymphocytic leukemia (CLL) and shows that HSP90B1 expression is modulated by miR-223 in CLL tumor and cell lines and suggest that HSP90B1 overexpression as a new pathogenic mechanism of CLL. PMID: 25880332
  25. our findings establish GRP94 as progression markers and druggable targets in glioblastoma, relating their oncogenic effects to activation of the Wnt/b-catenin signaling pathway PMID: 26108996
  26. Grp94 was detected in plasma of type 1 diabetic but not control subjects and found linked with its N-terminus to the IgG heavy chain. PMID: 26167512
  27. HSP gp96-positive expression is closely correlated with poor survival in gallbladder cancer. PMID: 25973087
  28. High BCLC staging scores, advanced cirrhosis and the overexpression of HSPA12A and HSP90B1 might be associated with poor survival from HCC, whereas high levels of HSPA4, HSPA5 and HSPA6 might be associated with earlier recurrence of HCC PMID: 25798051
  29. High HSP90B1 expression is associated with bone metastasis in renal cell carcinoma. PMID: 26115722
  30. The interaction of Grp94 with myocilin aggregates can be manipulated by cellular environment and genetics; this process can be exploited with Grp94 inhibitors to promote the clearance of toxic forms of myocilin. PMID: 25027323
  31. Results suggest an important role for HSP90B1 protein GP96 during human herpesvirus 6 HHV-6 infection, which possibly supports the cellular degradation of the virus. PMID: 25470779
  32. NF-kB significantly increased the gp96 expression by binding to the NF-kappaB binding site. PMID: 25803899
  33. GRP94 does not play a direct role in endoplasmic reticulum associated degradation. PMID: 24899641
  34. Induction of gp96-expression was higher in in vitro differentiated dendritic cells (i.v.DCs) than in in vitro differentiated macrophages (i.v.MACs), whereas monocytes (MOs) expressed only low gp96 levels. PMID: 24146856
  35. Glucose-regulated protein 94 is a downstream effector of ER-alpha36-mediated oestrogen signalling, and may be involved in ER-alpha36 function during gastric carcinogenesis. PMID: 23829397
  36. The frequency of mutant CC genotype for HSP90AA1 (rs4947C/T), mutant AA genotype for HSP90AB1 (rs13296A/G) and mutant CC genotype for HSP90B1 (rs2070908 C/G) was significantly higher in the patient group than in controls. PMID: 24511009
  37. role of HSP72 and gp96 in gastroenterological cancers PMID: 23266770
  38. Hsp90B1 is a direct target of miR-223 and miR- 223 may have a tumor suppressor function in osteosarcoma through the PI3K/Akt/mTOR pathway. PMID: 23208072
  39. glucose-regulated protein 94 is new potential discriminator for diffuse large B cell lymphoma. PMID: 22938940
  40. Grp94 triages mutant myocilin through endoplasmic reticulum-associated degradation. PMID: 23035116
  41. The Listeria-induced surface expression of Gp96 and the topology of its insertion on the plasma membrane, is reported. PMID: 23109341
  42. Our study revealed a remarkable biochemical event of gp96 silencing in murine but not human basophils, highlighting the need for caution in using mouse models to infer the function of basophils in human immune response. PMID: 22724016
  43. Patients with high Gp96 expression levels were significantly more resistant to radiotherapy in nasopharyngeal carcinoma. PMID: 22653265
  44. Chaperone gp96-independent inhibition of endotoxin response by chaperone-based peptide inhibitors. PMID: 22532561
  45. Inhibition of the humoral response was the main effect of Grp94 that significantly reduced the synthesis and secretion of both IgG and IgE antibodies in preipheral blood mononuclear cells from patients with allergic asthma. PMID: 22270544
  46. gp96 is critical for both TLR9 egress from the ER, and for protein conformational stability in the endosomal compartment. PMID: 22554506
  47. higher expression in recurrent breast cancer promotes cancer cell proliferation and migration PMID: 22245095
  48. These analyses identified decorin (DCN) and endoplasmin (HSP90B1) which play important roles regulating the tumour microenvironment and in pathways related to tumorigenesis. PMID: 22363530
  49. GRP94, FN14, and inhibin have roles in brain and non-brain metastases in ErbB-2+ and ErbB-2- breast neoplasms PMID: 21708117
  50. Gp96 is bound by the C. albicans Als3 invasin, which induces the uptake of this organism by brain endothelial cells. PMID: 21998592

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Subcellular Location Endoplasmic reticulum lumen, Melanosome
Protein Families Heat shock protein 90 family
Database Links

HGNC: 12028

OMIM: 191175

KEGG: hsa:7184

STRING: 9606.ENSP00000299767

UniGene: Hs.192374

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