Recombinant Mouse Endoplasmic reticulum chaperone BiP(Hspa5)

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Code CSB-YP010827MO
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names Hspa5
Uniprot No. P20029
Research Area Tags & Cell Markers
Alternative Names Hspa5; Grp78; Endoplasmic reticulum chaperone BiP; EC; 78 kDa glucose-regulated protein; GRP-78; Binding-immunoglobulin protein; BiP; Heat shock protein 70 family protein 5; HSP70 family protein 5; Heat shock protein family A member 5; Immunoglobulin heavy chain-binding protein
Species Mus musculus (Mouse)
Source Yeast
Expression Region 20-655aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 72.5kDa
Protein Length Full Length of Mature Protein
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 If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
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.
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 3-7 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.
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.

Target Data

Function Plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum
Gene References into Functions
  1. GRP78 regulates insulin resistance and macrophage polarization with selective IL-6 secretion in diet-induced obesity. PMID: 29242277
  2. These results uncover a novel role of GRP78 in reducing prion pathogenesis, suggesting that modulating its levels/activity may offer a novel opportunity for designing therapeutic approaches for these diseases. PMID: 28333162
  3. Endoplasmic reticulum stress leads to de novo biosynthesis of non-trimethylated GRP78, whereas homeostatic, METTL21A-dependent lysine 585-trimethylated GRP78 is reduced. PMID: 28912266
  4. GRP78 haploinsufficiency for up to 2 years of age has no major deleterious effect in rodents of different genetic background. PMID: 28145503
  5. 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
  6. siRNA of Grp78 disturbed the fusion of mouse palate cultured in vitro, suggesting a role in the palate development during embryogenesis.. PMID: 29233047
  7. prolonged endoplasmic reticulum stress promotes apoptosis via a p53-dependent inhibition of BiP expression PMID: 28622297
  8. role in acinar-to-ductal metaplasia and pancreatic ductal adenocarcinoma PMID: 28461470
  9. analysis of the effects of triptolide on cell proliferation, cell cycle and the expression of GRP78 in nasopharyngeal carcinoma PMID: 27391061
  10. candidate genes that modulate Hspa5 expression in the retina, were examined. PMID: 27881906
  11. These results indicate that GRP78, but not nutritional status, is a potent up-regulator of hepatic PTC-mRNA levels during induction of ER stress in vivo. PMID: 28383761
  12. Data suggest that activation of GRP78/Ire1/Xbp1 pathway of ER stress-unfolded protein response is involved in mouse decidualization. PMID: 27283502
  13. These results demonstrate a key role for GRP78 in alveolar epithelial cell survival. PMID: 26816051
  14. These results indicate that GRP78, an endoplasmic reticulum chaperon of the HSP70 family, is a novel host factor involved at multiple steps of the Japanese encephalitis virus life cycle and could be a potential therapeutic target. PMID: 28053106
  15. Genetic or pharmacologic inhibition of the HSPA5-GPX4 pathway enhanced gemcitabine sensitivity by disinhibiting ferroptosis in vitro and in both subcutaneous and orthotopic animal models of PDAC. PMID: 28130223
  16. Endoplasmic reticulum stress gene GRP78 is involved in signaling pathway during hepatitis B virus-mediated hepatocarcinogenesis. PMID: 26567840
  17. data show that Med inhibits ER stress-induced apoptosis and promotes osteoblast cell survival by targeting GRP78. PMID: 27316719
  18. These results suggested the important roles of endoplasmic reticulum-related chaperons, Bip and SIL1, in Alzheimer's disease-like tau hyperphosphorylation. PMID: 25575678
  19. We show that chronic VPA treatment did not modify the ATXN3 inclusion load and astrogliosis in affected brain regions However, VPA chronic treatment was able to increase GRP78 protein levels at 30 weeks of age, one of its known neuroprotective effects PMID: 26505994
  20. these findings reveal a novel critical role of GRP78 in regulating ER stress-mediated apoptosis in cartilage development and the molecular mechanisms involved. PMID: 26370957
  21. ISM is a novel vascular permeability inducer that functions through cell-surface GRP78-mediated Src activation as well as induction of apoptosis PMID: 25952901
  22. BIP increased surface CD19 molecule expression intensity and IL-10(+), PD-L1(hi) and FasL(hi) B cells induced by BIP share the CD19(hi) phenotype PMID: 26655428
  23. These studies demonstrate that BiP is critical for myelinating cell survival and contributes to the protective response of oligodendrocyte against inflammatory demyelination. PMID: 26631473
  24. These studies imply GRP78, but not GRP94, is required for mammary gland development. PMID: 24953136
  25. A highly specific monoclonal antibody against GRP78 suppressed AKT activation and increased apoptosis in the cPten(f/f) tumors. PMID: 25684138
  26. AdGRP78 reduced expression of lipogenic genes and plasma triglycerides in the db/db strain. Both G5 and G8 protein levels increased as did total biliary cholesterol PMID: 26365598
  27. Heterozygous mutant BiP mice revealed motor disabilities in aging. PMID: 25405877
  28. findings underscore the specific and prominent role of SKIP and GRP78 in the regulation of insulin-dependent PI 3-kinase signaling in skeletal muscle PMID: 26376412
  29. STZ injection i.p. rapidly induced up-regulation of the ER stress marker, the prosurvival chaperone glucose-regulated protein 78. With the development of diabetes, the expression of GRP78 decreases. PMID: 25529350
  30. Downregulation of GRP78 abolishes the activity of exogenous Syn, indicating that it is the primary target of Syn. PMID: 25124556
  31. high glucose induced astrocytic activation in both in vivo and in vitro diabetic models, in which modulation of GRP78 would be an important event in this activation PMID: 24056253
  32. This study showed that that inflammation leads to citrullination of GRP78 in beta-cells; opening new avenues for biomarker development and therapeutic intervention. PMID: 25204978
  33. Systemic gene transfer of binding immunoglobulin protein (BiP) prevents disease progression in murine collagen-induced arthritis. PMID: 25228326
  34. Data suggest that the balance between Cripto and Grp78 expression levels might be crucial in cancer development and may account for the increased tumorigenesis in Cripto heterozygous mice. PMID: 24805056
  35. Deficiency of the BiP cochaperone ERdj4 causes constitutive endoplasmic reticulum stress and metabolic defects. PMID: 24336520
  36. GRP78 might play an important role during the process of mouse embryo implantation, and GRP78 expression was mainly regulated by active blastocysts and maternal oestrogen. PMID: 24242779
  37. there is a causal link between a humoral response to GRP78 and the progression of cancer in a murine melanoma model PMID: 21164368
  38. GRP78 is a novel regulator for PTEN-loss-mediated liver injury and cancer progression. PMID: 24141775
  39. Matrin 3 interacts specifically with the heat shock proteins glucose-regulated protein 78, GRP75 and glutathione S-transferase pi isoform 2. PMID: 24491357
  40. Reg2 induces glucose-regulated peptide 78 (GRP78) expression via the Akt-mTORC1 axis. PMID: 24801175
  41. downregulated miR-181b induces neuroprotection against ischemic injury through negatively regulating HSPA5 and UCHL1 protein levels PMID: 23900885
  42. the interaction of amelogenin with Grp78/Bip contributed to cell proliferation, rather than correlate with the osteogenic differentiation PMID: 24167599
  43. IRE1alpha dissociates from BiP and inhibits ER stress-mediated apoptosis in the process of cartilage development. PMID: 23816533
  44. Data indicate that GRP78 is expressed in metastatic mammary tumors. PMID: 23470966
  45. Data suggest that transgenic mice that overproduce GRP78 in pancreatic beta cells are leaner than non-transgenic littermates and are protected against development of glucose intolerance, insulin resistance, and endoplasmic reticulum stress in islets. PMID: 23475366
  46. Knockdown of GRP78/BiP increased the accumulation of AR aggregates and significantly higher levels of caspase-3 activity and cell apoptosis. PMID: 23618905
  47. BiP was particularly observed in the pathological vasculature and retinal microvascular endothelial cells, and the increase of BiP expression was correlated with retinal neovascularization. PMID: 23544152
  48. These findings demonstrate a sensitive requirement for the endoplasmic reticulum chaperone BiP/GRP78 during axon outgrowth and pathfinding in the developing mammalian brain. PMID: 22821687
  49. GRP78 is required for adipocyte differentiation, glucose homeostasis, and balanced secretion of adipokines. PMID: 23180827
  50. NPGPx is essential for releasing excessive ER stress by enhancing GRP78 chaperone activity to maintain physiological homeostasis. PMID: 23123197
  51. Data suggest that vaspin is a ligand for cell-surface GRP78/MTJ-1 (DnaJ-like protein 1) complex; subsequent signal transduction exerts beneficial effects on endoplasmic reticulum stress-induced metabolic dysfunctions as seen in obesity. PMID: 22837305
  52. Suggest that lipid accumulation in macrophages and/or ER stress increased GRP78 and scavenger receptor A-mediated secretion of TNF-alpha. PMID: 19473344
  53. these studies demonstrate that GRP78 plays a pleiotropic role in BM cells and contributes to HSC survival and the maintenance of the lymphoid lineage. PMID: 22723926
  54. The Escherichia coli subtilase cytotoxin A subunit specifically cleaves cell-surface GRP78 protein and abolishes COOH-terminal-dependent signaling. PMID: 22851173
  55. GRP-78 is localized in the nucleus of mesenchymal cells and that the cell surface GRP-78 is not associated with the G-protein Galphaq in mesenchymal cells. PMID: 22527697
  56. ADP ribosylation adapts a BiP ER chaperone response to short-term fluctuations in unfolded protein load PMID: 22869598
  57. These results indicate that Anks4b is a HNF4alpha target gene that regulates endoplasmic reticulum stress in beta-cells by interacting with GRP78, thus suggesting that HNF4alpha is involved in maintenance of the ER. PMID: 22589549
  58. we show that overexpressing GRP78 protects N2a cells against mutant huntingtin proteins, reduces formation of mutant huntingtin aggregates, inhibits caspase-12 activation and blocks cell death PMID: 22490889
  59. Report suppression of murine melanoma growth with monoclonal antibody directed against the carboxyl-terminal domain of GRP78. PMID: 22495669
  60. BiP is involved in the homeostasis of endoplasmic reticulum function in the vasopressin neurons in the anterior hypothalamus. PMID: 22230548
  61. Hypoxia increases cell surface expression of GRP78 in neurons, GRP78 could be a potential therapeutic target for neuroprotection. PMID: 22120956
  62. the ER chaperone GRP78 is crucial for synoviocyte proliferation and angiogenesis, the pathological hallmark of rheumatoid arthritis. PMID: 22430489
  63. These data suggest that Cripto/GRP78 signaling is an important pathway that regulates hematopoietic stem cell quiescence. PMID: 21982233
  64. These results suggest that decreased GRP78 expression may induce resistance to insulin by inhibiting the AKT activation, and plays an important role in the development of type 2 diabetes. PMID: 22155243
  65. these results demonstrate that reduction of ER stress by chemical chaperones or glucose-response protein 78 (Grp78) overexpression does not improve palmitate-induced IR in skeletal muscle cells. PMID: 22177958
  66. We demonstrate by protease protection assays that the molecular chaperone GRP78 mediates the unfolding of the Lethal Factor fusion protein LFnDTA and Lethal Factor at neutral pH. PMID: 21797942
  67. Liver-specific loss of glucose-regulated protein 78 perturbs the unfolded protein response and exacerbates a spectrum of liver diseases in mice. PMID: 21503947
  68. GRP78/BiP conditional knockout mice demonstrated complete postnatal Purkinje cell degeneration and impaired eyeblink conditioning. PMID: 21517144
  69. Authors created conditional heterozygous knockout of GRP78 in the host endothelial cells and showed severe reduction of tumor angiogenesis and metastatic growth, with minimal effect on normal tissue MVD. PMID: 21467168
  70. The tumor-derived secreted form of BiP is capable of inducing antitumor CD8-positive T cell responses in vitro. PMID: 21339366
  71. Stress chaperone GRP-78 functions in mineralized matrix formation. PMID: 21239500
  72. Grp78 heterozygosity regulates ER chaperone balance, in dietary- and genetic background-dependent manners, and improved ER protein folding capacity might be protective against pancreatitis. PMID: 20971738
  73. Data show that cardiomyocytes under hypoxia show a significant increase in cell surface GRP78 in addition to gene expression and total protein. PMID: 20664993
  74. Endoplasmic reticulum stress induced inositol 1,4,5-trisphosphate receptor R1 dysfunction through an impaired IP(3)R1-GRP78 interaction. PMID: 21145001
  75. FoxO1 targeted GRP78 gene for trans-activation via selective binding to an insulin responsive element in the GRP78 promoter. PMID: 20501674
  76. Results uncover a novel link between GRP78 depletion and reduction in cytosolic ubiquitination and establish a novel mouse model of accelerated cerebellar degeneration with basic and clinical applications. PMID: 19816510
  77. Hig-fat diet-induced obesity and type 2 diabetes are improved in Grp78 heterozygoous mice. PMID: 19808896
  78. Tolbutamide has no significant effect on the expression of this protein in embryonic heart. PMID: 11835228
  79. ATPase activity of BiP is stimulated by DNAJ homolog, ERdj4 PMID: 11836248
  80. Reactions of the BiP chaperone cycle for a natural substrate protein domain in its soluble, stably unfolded conformation. This unfolded antibody domain forms a binary complex with BiP in the absence of ATP. PMID: 12054809
  81. BiP retains ATF6 in the endoplasmic reticulum by inhibiting its Golgi location signals; dissociation of BiP during ER stress allows ATF6 to be transported to the Golgi. PMID: 12110171
  82. Grp 78 is essential for alpha(2)macroglobulin-induced signal transduction. PMID: 12194978
  83. There were increased numbers of GRp78-immunoreactive cells in the dorsal and lateral cortex during sleep deprivation. PMID: 12535952
  84. Kinetic constants of the reactions of the ATPase cycle were determined without substrate, in the presence of a binding peptide and the antibody domain. We show that the non-native protein domain decelerates the rate limiting hydrolysis of the ATPase cycle PMID: 12818208
  85. activation of the Grp78 promoter by ATF4 through an upstream ATF/CRE site independent of the endoplasmic reticulum stress elements. PMID: 12871976
  86. mFKBP23 binds, to immunoglobulin binding protein (mBiP, Hsp70); the binding of the C-terminus is Ca(2+)-dependent and the switch point is between 2 and 3 mM, no binding being detected at high concentration of calcium PMID: 14960307
  87. GRP78 might perform an important function in the process of spermatogenesis. PMID: 15064947
  88. Grp78 is the alpha2M* signalling receptor. PMID: 15157672
  89. TFII-I is required for optimal induction of Grp78 by ER stress PMID: 15664986
  90. GRP78 and DnaJ-like protein 1 (MTJ-1) are colocalized in the plasma membrane of murine peritoneal macrophages. PMID: 15699139
  91. The insulin-induced, elevated expression of GRP78 was comparable with that observed with tunicamycin, a classical inducer of ER stress. PMID: 15845644
  92. Grp78 negatively regulates tissue factor functional activity via direct binding to and functional inhibition of TF PMID: 15947236
  93. Data indicate that folding efficiency of transthyretin is inversely correlated to BiP capture. PMID: 16376939
  94. During early heart organogenesis, Grp78 can be activated through cooperation between the cell type-specific transcription factors and the endoplasmic reticulum stress response elements. PMID: 16452489
  95. Bip is critical for coordinating estrogen-elicited biphasic responses and serves as a molecular link between ERalpha-independent and -dependent estrogenic responses in the uterus. PMID: 16574737
  96. In myocardial ischemia/reperfusion(I/R) levels of GRP78 and GRP94 were increased, consistent with I/R-mediated unfolded protein response activation in heart. PMID: 16601230
  97. Results provide the first evidence that GRP78 is essential for embryonic cell growth and pluripotent cell survival. PMID: 16847323
  98. BiP is a master regulator of endoplasmic reticulum function, and its cleavage by subtilase cytotoxin represents a previously unknown trigger for cell death PMID: 17024087
  99. Serum deprivation enhances the expression of a well-known marker of ER stress, the glucose-regulated protein-78 (GRP-78). PMID: 17399692
  100. binds to fkbp23 in endoplasmic reticulu. PMID: 17425118

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Subcellular Location Endoplasmic reticulum lumen, Melanosome, Cytoplasm
Protein Families Heat shock protein 70 family
Database Links

KEGG: mmu:14828

STRING: 10090.ENSMUSP00000028222

UniGene: Mm.330160

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