Recombinant Mouse Endoplasmic reticulum chaperone BiP(Hspa5)

In Stock
Code CSB-YP010827MO
Size US$1916
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details


The recombinant endoplasmic reticulum chaperone BiP (Hspa5) was produced as a fusion protein with an N-terminal 6xHis tag in the yeast cells. The encoding sequence contains 20-655aa of mouse Hspa5 protein. The purity of this full-length of mature Hspa5 protein reached up to 90% determined by SDS-PAGE. It migrated to a molecular mass band of 78-90 kDa on the gel. The slightly higher result is attributed to glycosylation. This recombinant Hspa5 protein can induce immune reactions in the immunized animals to thus get specific antibodies. Besides, it also may find uses in the tags and cell markers research area.

Heat shock protein family A member 5 (Hspa5), also known as GRP78 or Bip, is a member of heat shock proteins (HSPs) that are involved in proper protein folding, assembly of multiprotein complexes, as well as protein transport and degradation. In response to the accumulation of misfolded proteins in the ER, endoplasmic chaperone protein Hspa5 dissociates from ATF6-IRE1-PERK complex and then translocates into the lumen of the ER. This process unlocks the activity of the signal transducers previously blocked, which leads to the activation of the UPR signaling pathways. Recently, surface HSPA5 has been reported to be a potential receptor of some viruses, including the novel SARS-CoV-2.

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/-80°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 3-7 business days
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

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.
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

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

KEGG: mmu:14828

STRING: 10090.ENSMUSP00000028222

UniGene: Mm.330160

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