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

Name: Recombinant Mouse Endoplasmic Reticulum Chaperone Bip (HSPA5) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03365P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Endoplasmic Reticulum Chaperone Bip (HSPA5) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P20029
Target Symbol	HSPA5
Synonyms	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)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTSEKDEL
Expression Range	20-655aa
Protein Length	Full Length of Mature Protein
Mol. Weight	72.5kDa
Research Area	Tags & Cell Markers
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	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.
Subcellular Location	Endoplasmic reticulum lumen. Melanosome. Cytoplasm. Cell surface.
Protein Families	Heat shock protein 70 family
Database References	KEGG: mmu:14828 STRING: 10090.ENSMUSP00000028222 UniGene: 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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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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