Recombinant Rat 78 kDa glucose-regulated protein (Hspa5)

中文名稱：

大鼠Hspa5重組蛋白
貨號：

CSB-YP010827RA
說明書：

MSDS Datasheet
規格：
來源：

Yeast
其他：

中文名稱：

大鼠Hspa5重組蛋白
貨號：

CSB-EP010827RA
說明書：

MSDS Datasheet
規格：
來源：

E.coli
其他：

中文名稱：

大鼠Hspa5重組蛋白
貨號：

CSB-EP010827RA-B
說明書：

MSDS Datasheet
規格：
來源：

E.coli
共軛：

Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
其他：

中文名稱：

大鼠Hspa5重組蛋白
貨號：

CSB-BP010827RA
說明書：

MSDS Datasheet
規格：
來源：

Baculovirus
其他：

中文名稱：

大鼠Hspa5重組蛋白
貨號：

CSB-MP010827RA
說明書：

MSDS Datasheet
規格：
來源：

Mammalian cell
其他：

產品詳情
產品評價
靶點詳情

產品詳情

純度：

>85% (SDS-PAGE)
基因名：

Hspa5
Uniprot No.：

P06761
別名：

Hspa5; Grp78Endoplasmic 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; Steroidogenesis-activator polypeptide
種屬：

Rattus norvegicus (Rat)
蛋白長度：

Full Length of Mature Protein
表達區域：

19-654
氨基酸序列

EE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV EIIANDQGNR ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG RTWNDPSVQQ DIKFLPFKVV EKKTKPYIQV DIGGGQTKTF APEEISAMVL TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG VFEVVATNGD THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS SQHQARIEIE SFFEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD LKKSDIDEIV LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV QAGVLSGDQD TGDLVLLDVC PLTLGIETVG GVMTKLIPRN TVVPTKKSQI FSTASDNQPT VTIKVYEGER PLTKDNHLLG TFDLTGIPPA PRGVPQIEVT FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER MVNDAEKFAE EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSPED KETMEKAVEE KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSGGP PPTGEEDTSE KDEL
蛋白標簽：

Tag?type?will?be?determined?during?the?manufacturing?process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
產品提供形式：

Lyophilized powder Warning: in_array() expects parameter 2 to be array, null given in /www/web/cusabio_cn/public_html/caches/caches_template/default/content/show_product_protein.php on line 662
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.
復溶：

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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
儲存條件：

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
保質期：

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.
貨期：

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
注意事項：

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet ：

Please contact us to get it.

產品評價

靶點詳情

功能：

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.
基因功能參考文獻：
1. GRP78 is an acute regulator of steroidogenesis at the mitochondria-associated ER membrane, regulating the intermediate folding of StAR that is crucial for its activity. PMID: 28275724
2. Findings provide evidence that autophagy regulated by Bip expression after ER stress suppressed Cd-induced neuronal senescence. PMID: 27905509
3. High expression of GRP78 is associated with nonalcoholic steatohepatitis. PMID: 28951310
4. Bag5 protein expression is significantly increased in the ER during ER stress and that this in turn modulates GRP78 protein stability and reduces ER stress. PMID: 26729625
5. Increased expression of GRP78 promotes cardiomyocyte apoptosis in rats with cirrhotic cardiomyopathy. PMID: 26464674
6. In rats with severe acute pancreatitis, the apoptosis rate of neutrophils reduced over time, which may be associated to the stress induced expression of GRP78 and subsequent activation of Mcl-1 resulting in suppression of neutrophil apoptosis over time. PMID: 26464680
7. that Bip, an endoplasmic reticulum (ER) chaperone, selectively interacted with GluN2A and mediated the neuronal activity-induced assembly and synaptic incorporation of the GluN2A-containing N-methyl-D-aspartate receptor PMID: 26088419
8. Age-related decline in expression of the ER chaperone glucose-regulated protein 78 (GRP78) could be related to the development of Parkinson's disease. PMID: 25863526
9. These results suggest that ischemic preconditioning - induced GRP78 upregulation is involved in autophagy activation, and hence exerts protection against ischemic injury in neural cells. PMID: 25885223
10. 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
11. miR-376a potentially negatively regulates GRP78 protein expression through translational repression at an early stage transition from the follicular phase to luteinization. PMID: 25279841
12. Lipoxin A4 could play a role in myocardial protection via a mechanism related to downregulation of GRP-78 and caspase-12, and inhibition of apoptosis. PMID: 24129401
13. GRP78 suppresses lipid peroxidation and promotes cellular antioxidant levels in oxidatively stressed glial cells. PMID: 24475200
14. GRP78 may exert anti-apoptotic actions in ischemia-reperfusion retina. PMID: 24880098
15. GRP78 plays an anti-apoptotic role in regulating the cell death response during acute pancreatitis. PMID: 24643222
16. Over-expression of GRP78 in lungs may be the critical pathogenic factor for hepatopulmonary syndrome.GRP78 may play a crucial role in promoting the pulmonary microvascular remodeling in a rat model of hepatopulmonary syndrome. PMID: 24768185
17. Studied polyubiquitinated proteins during inflammatory response in intestinal epithelial cells; found Grp75 and Grp78 differentially ubiquitinated between control and inflammation; results confirmed in HCT-8 cells and in TNBS induced colitis in rats. PMID: 24030972
18. The increased GRP78 expression is indicative of endoplasmic reticulum stress response during hepatopulmonary syndrome. PMID: 24334118
19. Myocardial GRP78 activation and protein degradation occurs due to synergistic, not individual, cold and hypoxic stress. PMID: 23816873
20. hypothermia significantly attenuates brain I/R injury, as shown by reduction in cell apoptosis, CHOP expression, and increase in GRP78 expression PMID: 23301071
21. Hypertension can aggravate global cerebral IR injury by decreasing GRP78 expression and increasing the loss of nerve cells. PMID: 23174603
22. Data suggest that vascular activity of penile/cavernosal tissue is impaired by upregulation of Bip/Hspa5 and p66Shc (SHC [Src homology 2 domain-containing] transforming protein 1) in diabetic corpus cavernosum/penis leading to erectile dysfunction. PMID: 23215692
23. Protein chaperone Hspa5 is involved in copper homeostasis in astrocytes but not as a copper storage protein. PMID: 22342161
24. GRP78 expression was associated with apoptosis and the severity of cerulein-induced pancreatic inflammation. PMID: 22640899
25. study to determine stage of apoptosis in lungs initiated through inflammatory response from the small intestine; analyzed changes in mRNA of Gadd153 and Grp78 in the small intestine and lung; in lung lower level of expression Grp78 was detected; suggests ischemic attack and reperfusion did not promote ER stress in lungs through induction of Gadd153 in small intestine PMID: 22083547
26. data suggest an essential role of Bip in GSK-3beta dependent tau hyperphosphorylation in endoplasmic reticulum stress by promoting the binding of GSK-3beta to tau PMID: 22460328
27. Data conclude that BiP decrease is a signature of the degenerating process, as its overexpression led to an increase in motoneurons survival after root avulsion. PMID: 21436843
28. GRP78 expression is upregulated following ER stress and has protects injured glial cells from cell death. PMID: 21970967
29. Edaravone increased expression of GRP78 and decreased expression of caspase-12 in hippocampus rat with pilocarpine-induced seizures, reducing neuronal apoptosis. PMID: 21429313
30. The expression of GRP78 was increased in the inner ear tissue of aging rats. PMID: 20235454
31. Up-regulation of GRP78 induced by 2DG counteracts primary cellular damage in fetal rat cerebral neurons caused by endoplasmic reticulum stress in utero. PMID: 18953869
32. Endoplamic reticulum stress-related markers, GRP78 and GADD153, are elevated after retinal detachment. PMID: 19218986
33. H2S could effectively ameliorate HHcy-induced cardiomyocytic injury along with decreased expressions of GRP78, CHOP, and caspase 12 in rats with hyperhomocysteinemia PMID: 19769458
34. HSP70 and GRP78 induced by endothelin-1 pretreatment enhance tolerance to hypoxia in cultured neonatal rat cardiomyocytes. PMID: 15838258
35. The ER-resident chaperone GRP78 (BIP) can be retargeted to mitochondria and thereby may be involved in correlating unfolded protein release signalling between these two organelles. PMID: 16433633
36. the induction of GRP78 partially mediates the late hypoxic preconditioning (HPC), suggesting that GRP78 is a novel mechanism responsible for the late cytoprotection of HPC. PMID: 17854840
37. Identify HSPA5 in the stress response of glomerular mesangial cells and implicate regulatory mechanisms that are distinct from those involved in thapsigargin inducibility. PMID: 17915553
38. GRP78 and caspase-12 had enhanced expression at protein and mRNA levels in diastolic failing heart PMID: 18787714
39. a role for both GRP78 and PDI in insulin biosynthesis, although an excess of PDI disrupts normal proinsulin processing. PMID: 19103594
40. GRP78 inhibits both insulin-dependent and ER stress-dependent SREBP-1c proteolytic cleavage and explain the role of ER stress in hepatic steatosis in obese rodents. PMID: 19363290
41. Knockdown of ERp57 confers cellular protection against hyperoxia- or tunicamycin-induced apoptosis by inhibition of caspase-3 activation and stimulation of BiP/GRP78 induction. PMID: 19411306
42. Report stress protein response and oxidative damage in a renal derived cell line exposed to inorganic mercury and lead. PMID: 19720107
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亞細胞定位：

Endoplasmic reticulum lumen. Melanosome. Cytoplasm. Cell surface.
蛋白家族：

Heat shock protein 70 family
數據庫鏈接：

KEGG: rno:25617

STRING: 10116.ENSRNOP00000025064

UniGene: Rn.11088