Recombinant Human Endoplasmin (HSP90B1) Protein (His)

Name: Recombinant Human Endoplasmin (HSP90B1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08323P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) HSP90B1.

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Product Overview

Description	Recombinant Human Endoplasmin (HSP90B1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P14625
Target Symbol	HSP90B1
Synonyms	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)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	VDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVLDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEEETAKESTAE
Expression Range	27-799aa
Protein Length	Partial
Mol. Weight	93.1kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10.
Subcellular Location	Endoplasmic reticulum lumen. Sarcoplasmic reticulum lumen. Melanosome.
Protein Families	Heat shock protein 90 family
Database References	HGNC: 12028 OMIM: 191175 KEGG: hsa:7184 STRING: 9606.ENSP00000299767 UniGene: PMID: 29852388 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 Overexpressed miR-150 attenuates hypoxia-induced human cardiomyocyte cell apoptosis by targeting GRP94. PMID: 29328381 Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90beta as a molecular model for myotonia congenita has been described. PMID: 27580824 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 HSP-gp96 promotes T cell response, enhances DC antigen presentation and induces cytokine secretion in human gastric cancer cell lines. PMID: 28706421 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 High GRP94 expression is associated with endometrioid adenocarcinoma. PMID: 26910913 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 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 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 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 High HSP90B1 expression is associated with non-small-cell lung cancer. PMID: 27599983 data suggest that the GRP94/CCT8/c-Jun/EMT signaling cascade might be a new therapeutic target for HCC PMID: 26718209 We filtered four OSCC genes including SERPINB9, SERPINE2, GAK, and HSP90B1 through the gene global prioritization score (P < 0.005). PMID: 26318431 Our results demonstrated that GRP94 is a key molecule in Hepatocellular carcinoma (HCC) progression that modulates the AKT pathway and eNOS levels PMID: 26493996 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 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 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 Our results indicate that GRP94 and TRAP1 might contribute more to the carcinogenesis or biology of SCLC than HSP90alpha and HSP90beta PMID: 26464709 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 data suggest a role of infection-induced Gp96 shedding in the protection of the chlamydial replicative niche PMID: 26235316 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 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 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 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 HSP gp96-positive expression is closely correlated with poor survival in gallbladder cancer. PMID: 25973087 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 High HSP90B1 expression is associated with bone metastasis in renal cell carcinoma. PMID: 26115722 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 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 NF-kB significantly increased the gp96 expression by binding to the NF-kappaB binding site. PMID: 25803899 GRP94 does not play a direct role in endoplasmic reticulum associated degradation. PMID: 24899641 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 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 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 role of HSP72 and gp96 in gastroenterological cancers PMID: 23266770 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 glucose-regulated protein 94 is new potential discriminator for diffuse large B cell lymphoma. PMID: 22938940 Grp94 triages mutant myocilin through endoplasmic reticulum-associated degradation. PMID: 23035116 The Listeria-induced surface expression of Gp96 and the topology of its insertion on the plasma membrane, is reported. PMID: 23109341 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 Patients with high Gp96 expression levels were significantly more resistant to radiotherapy in nasopharyngeal carcinoma. PMID: 22653265 Chaperone gp96-independent inhibition of endotoxin response by chaperone-based peptide inhibitors. PMID: 22532561 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 gp96 is critical for both TLR9 egress from the ER, and for protein conformational stability in the endosomal compartment. PMID: 22554506 higher expression in recurrent breast cancer promotes cancer cell proliferation and migration PMID: 22245095 These analyses identified decorin (DCN) and endoplasmin (HSP90B1) which play important roles regulating the tumour microenvironment and in pathways related to tumorigenesis. PMID: 22363530 GRP94, FN14, and inhibin have roles in brain and non-brain metastases in ErbB-2+ and ErbB-2- breast neoplasms PMID: 21708117 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.