Recombinant Human Endoplasmic Reticulum Chaperone Bip (HSPA5) Protein (His)

Name: Recombinant Human Endoplasmic Reticulum Chaperone Bip (HSPA5) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02368P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Endoplasmic Reticulum Chaperone Bip (HSPA5) 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	P11021
Target Symbol	HSPA5
Synonyms	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
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	EDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVE
Expression Range	25-293aa
Protein Length	Partial
Mol. Weight	33.6kDa
Research Area	Others
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.
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	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.
Subcellular Location	Endoplasmic reticulum lumen. Melanosome. Cytoplasm. Cell surface.
Protein Families	Heat shock protein 70 family
Database References	HGNC: 5238 OMIM: 138120 KEGG: hsa:3309 STRING: 9606.ENSP00000324173 UniGene: PMID: 29024602 Cell surface GRP78 promotes cancer stemness, whereas drives cells toward a non-stemlike phenotype when it chaperones Progranulin. PMID: 29323121 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 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 High GRP78 expression is associated with radioresistance in nasopharyngeal carcinoma. PMID: 30015969 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 the physiological role played by the complex KCTD15-GRP78 in the adipogenesis PMID: 29665387 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 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 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 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 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 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 this study demonstrates the reaction of placental GRP78 with sera from women with multiple sclerosis PMID: 29276183 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 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 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 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 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 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 GRP78 overexpression decreased advanced glycation end product levels and rescued the cells from Ribosome-induced cytotoxicity. PMID: 29410209 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 GRP78 silencing promoted lung epithelial cell apoptosis during hyperoxia, via regulation of the CHOP pathway. PMID: 28586043 GRP78 role in dengue virus infection. PMID: 27779201 Overexpression of GRP78 is a novel predictor of favorable outcomes in patients with advanced thymic carcinoma. who receive combination chemotherapy. PMID: 28550415 GRP78 is an autoantigen that could stimulate autoimmune responses and serve as a potential marker for recurrent and metastatic progression in HCC. PMID: 28186997 These results identify GRP78 antibodies as a potential component of Neuromyelitis optica pathogenesis. PMID: 28679661 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 an endoplasmic reticulum complex of resident chaperones that includes HSP47, FKBP65, and BiP regulating the activity of LH2. PMID: 28177155 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 P4HB promotes hepatocellular carcinoma progression by down-regulating GRP78 expression and subsequently promoting epithelial-to-mesenchymal transition. PMID: 28052026 analysis of the effects of triptolide on cell proliferation, cell cycle and the expression of GRP78 in nasopharyngeal carcinoma PMID: 27391061 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 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 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 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 GRP78 affects p53 localization which in turn regulates autophagy. PMID: 27814589 candidate genes that modulate Hspa5 expression in the retina, were examined. PMID: 27881906 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 this study provided mechanistic evidences to support the positive regulatory function of FOXM1 in HSPA5 expression in colorectal cancer PMID: 27034162 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 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 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 GRP78 role in the resistance to cisplatin in the nasopharyngeal carcinoma cells. PMID: 27254284 High expression of GRP78 is associated with nonalcoholic steatohepatitis. PMID: 28951310 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 HSPA5/BIP has roles in endoplasmic reticulum stress, autophagy and apoptosis; inhibitors of HSPA5 could be useful in cancer treatment PMID: 27791469 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 GRP78 inhibition enhances ATF4-induced cell death by the deubiquitination and stabilization of CHOP in human osteosarcoma cells. PMID: 28947141 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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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.

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