Recombinant Human Heat shock cognate 71 kDa protein (HSPA8)

中文名稱：

人HSPA8重組蛋白
貨號(hào)：

CSB-EP010829HU
說明書：

MSDS Datasheet
規(guī)格：
來源：

E.coli
其他：

中文名稱：

人HSPA8重組蛋白
貨號(hào)：

CSB-EP010829HU-B
說明書：

MSDS Datasheet
規(guī)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：

人HSPA8重組蛋白
貨號(hào)：

CSB-BP010829HU
說明書：

MSDS Datasheet
規(guī)格：
來源：

Baculovirus
其他：

中文名稱：

人HSPA8重組蛋白
貨號(hào)：

CSB-MP010829HU
說明書：

MSDS Datasheet
規(guī)格：
來源：

Mammalian cell
其他：

產(chǎn)品詳情
產(chǎn)品評(píng)價(jià)
相關(guān)產(chǎn)品
靶點(diǎn)詳情

產(chǎn)品詳情

純度：

>85% (SDS-PAGE)
基因名：

Name:HSPA8 Synonyms:HSC70, HSP73, HSPA10
Uniprot No.：

P11142
別名：

2410008N15Rik; Constitutive heat shock protein 70; Epididymis luminal protein 33; Epididymis secretory sperm binding protein Li 72p; Heat shock 70 kDa protein 8; Heat shock 70kD protein 10; Heat shock 70kD protein 8; Heat shock 70kDa protein 8; Heat shock cognate 71 kDa protein; Heat shock cognate protein 54; Heat shock cognate protein 71 kDa; Heat shock protein 8; Heat shock protein A8; Heat shock protein family A (Hsp70) member 8; Heat-shock70-KD protein 10, formerly; HEL 33; HEL S 72p; HSC54; HSC71; Hsc73; HSP71; HSP73; HSP7C_HUMAN; HSPA10; HSPA8; LAP1; Lipopolysaccharide associated protein 1; LPS associated protein 1; LPS associated protein; MGC102007; MGC106514; MGC114311; MGC118485; MGC131511; MGC29929; N-myristoyltransferase inhibitor protein 71; NIP71
種屬：

Homo sapiens (Human)
蛋白長(zhǎng)度：

Full Length of Mature Protein
表達(dá)區(qū)域：

2-646
氨基酸序列

SKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
蛋白標(biāo)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(chǎn)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(fù)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(chǔ)存條件：

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

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(chǎn)品評(píng)價(jià)

靶點(diǎn)詳情

功能：

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21.
基因功能參考文獻(xiàn)：
1. Data suggest that both the small heat shock protein HspB1/Hsp27 and the constitutive chaperone Hsc70/HspA8 interact with tau to prevent tau-fibril/amyloid formation. Hsc70 is highly efficient at preventing tau-fibril elongation, possibly by capping ends of tau-fibrils. (HspB1 = heat shock protein family B small member 1; Hsc70 = heat shock protein family A Hsp70) PMID: 29298892
2. This study demonstrated that particular distribution for HSC70 and PSMC4 in the cytoplasm and accumulation within Lewy body in the dopaminergic neurons of the substantia nigra in Parkinson patients. PMID: 29218503
3. Hsp70participated in PINK1-mediated mitophagy by stabilizing PINK1. PMID: 29107085
4. These results demonstrate not only an important mechanism of Hsc70 in facilitating EV-A71 replication, but also a target for antiviral drug development. PMID: 29180285
5. Post-transcriptional inhibition of HSPA8 expression leads to synaptic vesicle cycling defects in multiple models of amyotrophic lateral sclerosis. PMID: 28978466
6. Taken together, these data suggest hat the altered hydrogen bonding observed in the Hsc70 C17W mutant (where the connectivity between Mg2+.nucleotide and E175 is also disrupted) could bring about changes to Hsc70 domain communication, affecting peptide association while also limiting ATP hydrolysis. PMID: 29300467
7. The roles of the E3 ubiquitin ligase, carboxy-terminus Hsc70 interacting protein (CHIP) in various types of cancers. PMID: 28731191
8. Hsc70/Hsp90 chaperones contribute to the conformational and functional maintenance of DeltaF508-CFTR at 37 degrees C. PMID: 28855508
9. Engagement of the oligomer by LAP1 triggers ATP hydrolysis and rapid complex disassembly. Thus the Torsin complex is a highly dynamic assembly whose oligomeric state is tightly controlled by distinctively localized cellular cofactors. PMID: 28814508
10. Downregulation of Hsc70, Hsp70, and IL-15 expression at gene and/or protein levels might support the retention of fertilization products in cases of missed abortion and blighted ovum. PMID: 27225940
11. STRO-1 binds to immune-precipitated HSC70 and siRNA-mediated knock down of HSPA8 reduced STRO-1 binding. PMID: 28026090
12. Synapsin is part of a multiprotein complex enriched in chaperones/cochaperones including Hsc70. Hsc70 chaperone activity is required for the cytosolic slow axonal transport of synapsin. PMID: 28559423
13. study demonstrates a critical role of Hsc70 in SV40 endoplasmic reticulum-to-cytosol penetration and reveal how SGTA controls Hsc70 to impact this process PMID: 28356524
14. In fact, DnaJC5 overexpression induced tau release in cells, neurons, and brain tissue, but only when activity of the chaperone Hsc70 was intact and when tau was able to associate with this chaperone. PMID: 27261198
15. These results suggest that Bag1 and Bag3 control the stability of the Hsc70-client complex using at least two distinct protein-protein contacts, providing a previously under-appreciated layer of molecular regulation in the human Hsc70 system. PMID: 27474739
16. While cerebrospinal fluid Nrf2 and HSPA8 do not appear to offer diagnostic biomarkers for Parkinson's disease (PD), the associations between Nrf2 levels and UPDRS scores in LRRK2 + PD patients merit further investigation PMID: 26526034
17. HSPA8 maintains pluripotency of human pluripotent stem cells by binding to the master pluripotency regulator OCT4 and facilitating its DNA-binding activity. PMID: 26549849
18. heat shock cognate 70 (HSC70) is an essential component of Aes foci in colorectal cancer cells. PMID: 26229111
19. Cx43-Hsc70 interaction regulates cell cycle G1/S progression through a novel mechanism by which Cx43-Hsc70 interaction prevents the nuclear accumulation of p27 through controlling the nuclear translocation of cyclin D1-CDK4-p27 complex. PMID: 26481195
20. serum HSC71 was identified as a novel serum biomarker of renal cell carcinoma, particularly useful in early diagnosis of clear-cell type. PMID: 26425554
21. These findings provide further evidence that histatin 3 may be involved in the regulation of cell proliferation, particularly during G1/S transition, via the ubiquitin-proteasome system of p27(Kip1) and HSC70. PMID: 26775844
22. constitutive heat shock protein HSC70 forms granule-like structures in the cytoplasm of human cells several days after the exposure to heat stress PMID: 26335814
23. These results indicate that CHIP decreases the Kv1.5 protein level and functional channel by facilitating its degradation in concert with chaperone Hsc70 PMID: 26232501
24. Active Hsc70 requires active tau to regulate microtubule assembly in vivo, suggesting that tau acts in some ways as a co-chaperone for Hsc70 to coordinate microtubule assembly. PMID: 25882706
25. detailed and systematic investigation to characterize if there are significant differences in the CHIP in vitro ubiquitination of human Hsp70 and Hsc70. PMID: 26010904
26. HSP70 binds CD91 and TLR4 on decidual CD1a(+) dendritic cells, causes their maturation, and increases IL-15 in the context of Th1 cytokine/chemokine domination, which could support immune response harmful for ongoing pregnancy. PMID: 25737151
27. LAP1 mutations are associated with severe dystonia, cerebellar atrophy and cardiomyopathy. PMID: 26596547
28. HSC70 may serve as a molecular switch to modulate endocytic and autophagy pathways, impacting the source of antigens delivered for MHC class II presentation during cellular stress. (Review) PMID: 25953005
29. CHIP docks onto Hsp70/Hsc70 and defines a bipartite mode of interaction between TPR domains and their binding partners. PMID: 25684577
30. Hsc70 interacted with Rab1A in a chaperone-dependent mannerand Hsc70 knockdown decreased the level of Rab1A and increased the level of its ubiquitination under stress conditions. PMID: 24801886
31. Data suggest that nhibition of nestin and heat shock protein HSPA8/HSC71 may be a useful molecular target in the treatment of glioblastomas. PMID: 25527454
32. LAP1 and LULL1 regulate Torsin ATPase activity through an active site complementation mechanism. PMID: 25352667
33. H-ERG trafficking was impaired by H2O2 after 48 h treatment, accompanied by reciprocal changes of expression between miR-17-5p seed miRNAs and several chaperones (Hsp70, Hsc70, CANX, and Golga20) PMID: 24386440
34. the endogenous DNAJC12 and Hsc70 proteins interact in LNCaP cells. PMID: 24122553
35. Endoplasmic reticulum-associated degradation of Niemann-Pick C1: evidence for the role of heat shock proteins and identification of lysine residues that accept ubiquitin. PMID: 24891511
36. Results identify a systemic hsc70 reduction in Parkinson's disease patients. PMID: 24361989
37. Hsp73 sustains Hsp90 chaperone function and critically contributes to cell survival in multiple myeloma patients. PMID: 23065523
38. These findings indicate that wild type ILK and the non-oncogenic ILK(R211A) mutation comprise a cardioprotective module with Hsp/c70. PMID: 24260102
39. A significant downregulation of HSPA8 and HSPA9 was observed in AD across the three brain regions compared to the controls, suggesting their participation in AD pathogenesis. PMID: 23948933
40. HSP8A polymorphism is associated with drug-naive schizophrenia. PMID: 24548631
41. Cx43-Hsc70 interaction probably plays a critical role during G1/S progression. PMID: 24056538
42. These results demonstrate that Hsp70 recruits PP5 and activates its phosphatase activity which suggests dual roles for PP5 that might link chaperone systems with signaling pathways in cancer and development. PMID: 24327656
43. Altered expression of Hsc70 and eIF5A-1 may cause defects in nucleocytoplasmic transport and play a role in esophageal carcinogenesis. PMID: 23539416
44. the U-box mutation stimulated CHIP binding to Hsc70 while promoting CHIP oligomerization. CHIP binding to Hsc70 binding was also stimulated by the presence of an Hsc70 client with a preference for the ADP-bound state. PMID: 23990462
45. GLIPR1 interacts with Hsc70, and GLIPR1 overexpression or Hsc70 knockdown leads to transcriptional suppression of AURKA and TPX2. PMID: 23333597
46. PKCiota knockdown sensitized cells to oxidative stress-induced apoptosis, whereas forced PKCiota expression counteracted the oxidative stress-induced apoptosis via Hsc70. PMID: 23224638
47. Relaxation-based NMR experiments on the Hsc70-CHIP complex determined that the two partners move independently in solution, similar to "beads on a string PMID: 23865999
48. LAP1 and LULL1 as regulatory cofactors that are responsible for the activation of TorA's ATPase activity. PMID: 23569223
49. 70-kDa heat shock cognate protein hsc70 mediates calmodulin-dependent nuclear import of the sex-determining factor SRY. PMID: 23235156
50. Studies suggest that Hsc70 and lysosome-associated protein 2A (LAMP-2A) through chaperone-mediated autophagy (CMA) play a role in the clearance of Htt and suggest a novel strategy to target the degradation of mutant huntingtin (Htt). PMID: 23071649
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亞細(xì)胞定位：

Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.
蛋白家族：

Heat shock protein 70 family
組織特異性：

Ubiquitous.
數(shù)據(jù)庫(kù)鏈接：

HGNC: 5241

OMIM: 600816

KEGG: hsa:3312

STRING: 9606.ENSP00000227378

UniGene: Hs.180414