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 3.6.4.10; 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

Target Protein Sequence

EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTSEKDEL
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

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.

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/-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.

Description

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.

Target Background

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.

Gene References into Functions

GRP78 regulates insulin resistance and macrophage polarization with selective IL-6 secretion in diet-induced obesity. PMID: 29242277
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
Endoplasmic reticulum stress leads to de novo biosynthesis of non-trimethylated GRP78, whereas homeostatic, METTL21A-dependent lysine 585-trimethylated GRP78 is reduced. PMID: 28912266
GRP78 haploinsufficiency for up to 2 years of age has no major deleterious effect in rodents of different genetic background. PMID: 28145503
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
siRNA of Grp78 disturbed the fusion of mouse palate cultured in vitro, suggesting a role in the palate development during embryogenesis.. PMID: 29233047
prolonged endoplasmic reticulum stress promotes apoptosis via a p53-dependent inhibition of BiP expression PMID: 28622297
role in acinar-to-ductal metaplasia and pancreatic ductal adenocarcinoma PMID: 28461470
analysis of the effects of triptolide on cell proliferation, cell cycle and the expression of GRP78 in nasopharyngeal carcinoma PMID: 27391061
candidate genes that modulate Hspa5 expression in the retina, were examined. PMID: 27881906
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
Data suggest that activation of GRP78/Ire1/Xbp1 pathway of ER stress-unfolded protein response is involved in mouse decidualization. PMID: 27283502
These results demonstrate a key role for GRP78 in alveolar epithelial cell survival. PMID: 26816051
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
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
Endoplasmic reticulum stress gene GRP78 is involved in signaling pathway during hepatitis B virus-mediated hepatocarcinogenesis. PMID: 26567840
data show that Med inhibits ER stress-induced apoptosis and promotes osteoblast cell survival by targeting GRP78. PMID: 27316719
These results suggested the important roles of endoplasmic reticulum-related chaperons, Bip and SIL1, in Alzheimer's disease-like tau hyperphosphorylation. PMID: 25575678
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
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
ISM is a novel vascular permeability inducer that functions through cell-surface GRP78-mediated Src activation as well as induction of apoptosis PMID: 25952901
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
These studies demonstrate that BiP is critical for myelinating cell survival and contributes to the protective response of oligodendrocyte against inflammatory demyelination. PMID: 26631473
These studies imply GRP78, but not GRP94, is required for mammary gland development. PMID: 24953136
A highly specific monoclonal antibody against GRP78 suppressed AKT activation and increased apoptosis in the cPten(f/f) tumors. PMID: 25684138
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
Heterozygous mutant BiP mice revealed motor disabilities in aging. PMID: 25405877
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
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
Downregulation of GRP78 abolishes the activity of exogenous Syn, indicating that it is the primary target of Syn. PMID: 25124556
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
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
Systemic gene transfer of binding immunoglobulin protein (BiP) prevents disease progression in murine collagen-induced arthritis. PMID: 25228326
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
Deficiency of the BiP cochaperone ERdj4 causes constitutive endoplasmic reticulum stress and metabolic defects. PMID: 24336520
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
there is a causal link between a humoral response to GRP78 and the progression of cancer in a murine melanoma model PMID: 21164368
GRP78 is a novel regulator for PTEN-loss-mediated liver injury and cancer progression. PMID: 24141775
Matrin 3 interacts specifically with the heat shock proteins glucose-regulated protein 78, GRP75 and glutathione S-transferase pi isoform 2. PMID: 24491357
Reg2 induces glucose-regulated peptide 78 (GRP78) expression via the Akt-mTORC1 axis. PMID: 24801175
downregulated miR-181b induces neuroprotection against ischemic injury through negatively regulating HSPA5 and UCHL1 protein levels PMID: 23900885
the interaction of amelogenin with Grp78/Bip contributed to cell proliferation, rather than correlate with the osteogenic differentiation PMID: 24167599
IRE1alpha dissociates from BiP and inhibits ER stress-mediated apoptosis in the process of cartilage development. PMID: 23816533
Data indicate that GRP78 is expressed in metastatic mammary tumors. PMID: 23470966
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
Knockdown of GRP78/BiP increased the accumulation of AR aggregates and significantly higher levels of caspase-3 activity and cell apoptosis. PMID: 23618905
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
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
GRP78 is required for adipocyte differentiation, glucose homeostasis, and balanced secretion of adipokines. PMID: 23180827
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

Code	CSB-YP010827MO
Abbreviation	Recombinant Mouse Hspa5 protein
MSDS	MSDS Datasheet
Size	$368
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Mouse Endoplasmic reticulum chaperone BiP (Hspa5)

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