Recombinant Rat Heat shock cognate 71 kDa protein(Hspa8)

Code CSB-YP010829RA
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Source Yeast
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Code CSB-EP010829RA
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Source E.coli
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Code CSB-EP010829RA-B
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Source E.coli
Conjugate 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.
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Code CSB-BP010829RA
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Source Baculovirus
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Code CSB-MP010829RA
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names Hspa8
Uniprot No. P63018
Alternative Names Hspa8; Hsc70; Hsc73; Heat shock cognate 71 kDa protein; Heat shock 70 kDa protein 8
Species Rattus norvegicus (Rat)
Expression Region 2-646
Target Protein Sequence 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 LDKCNEIISW LDKNQTAEKE EFEHQQKELE KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
Protein Length Full Length of Mature Protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
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.
Form Lyophilized powder
Buffer before Lyophilization 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℃/-80℃. 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 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 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.
Notes 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.

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Target Data

Function 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
Gene References into Functions
  1. 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
  2. these data demonstrate a novel interaction between Hsc70 and TH that regulates the activity and localization of the enzyme to synaptic vesicles, suggesting an important role for Hsc70 in dopamine homeostasis. PMID: 27365397
  3. Pulsed electromagnetic wave exposure induced ultrastructural damage and the overexpression of HSP70 in the nuclei in the adenohypophysis. PMID: 25891763
  4. These findings demonstrate that Hsc70 chaperone activity is required for Rac1 activation by Trio and this function underlies netrin-1/DCC-dependent axon outgrowth and guidance. PMID: 26323693
  5. these data provide evidence for Hsc70 as a novel neuronal interactor of NF-kappaB p65. PMID: 23762333
  6. The level of 70 kDa heat shock cognate (HSC70) expression was greater in the diencephalon of the 3 ppm Fe group. PMID: 21811788
  7. this rearch suggests that the protective effect of Hsc70 on the cardiomyocytes against oxidative stress is partly associated with its interaction with alpha-enolase. PMID: 21958194
  8. Hsc70 binding appears highly sensitive to the duration of its binding cycle, which is in turn governed by the integrated expression of regulatory cochaperones PMID: 21697503
  9. A sequential mechanism for clathrin cage disassembly by 70-kDa heat-shock cognate protein (Hsc70) and auxilin. PMID: 21482805
  10. BAG3 and Hsc70 interact with actin capping protein CapZ to maintain myofibrillar integrity under mechanical stress. PMID: 20884878
  11. data demonstrate for the first time that HSP70 overexpression with adenovirus injection prevented the lipopolysaccharide-induced increase in tumor necrosis factor-alpha and IL-6 levels in rats. PMID: 19551494
  12. Trafficking of axonal K+ channels: potential role of Hsc70 PMID: 11891788
  13. A novel alphaGDI complex from synaptic membranes contains three chaperone components: Hsp90, Hsc70 and cysteine string protein (CSP). The complex is dissociated in response to Ca(2+)-induced neurotransmitter release. PMID: 12426384
  14. alpha-helical region of the 10-kDa subdomain of Hsc70 dictates the chaperone self-association PMID: 12773536
  15. HSC70 binds to a brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein PMID: 12878599
  16. specific association between HSP73 and gentamicin may reduce the chaperone activity of HSP73 in vitro and/or in vivo PMID: 14966137
  17. analysis of expression of Hsp70 isoforms in rat liver after in vivo heat stress PMID: 15543931
  18. Analysis of constitutively expressed heat shock proteins revealed variable levels of Hsc70 and Hsp27 in different classes of neurons in the adult rat brain. PMID: 17441507
  19. 70-kDa heat shock proteins as a AQP2 interactors and have shown for hsc70 that this interaction is involved in AQP2 trafficking. PMID: 17636261
  20. alphaD-alphaE helices and the conserved interdomain linker are two interfaces essential not only for the self-association but also for the functional properties of rat HSC70. PMID: 17979815
  21. ASIC2-Hsc70 interactions may play a role in vascular smooth muscle cell migration and contribute to vasculogenesis and remodeling. PMID: 18310515
  22. The results suggest that the involvement of NF-kappaB p65 in nuclear translocation of Ku70 may be mediated by Hsc70 degradation, which may play a key role in cell proliferation of pancreatic acinar AR42J cells. PMID: 18378183
  23. Extracellular HSC70 plays a critical role in regulating the myocardial innate immune response and cardiac function after ischemia-reperfusion. PMID: 18441202
  24. structural basis of HSC70 oligomerization; 2 non-contiguous regions, located at both ends of the C-terminal domain, appear to form the contact interface in the oligomers & may interact in dynamic fashion leading to formation of several coexisting species PMID: 19388598
  25. A purified Hsc70 fragment that binds vesicular monoamine transporter-2 (VMAT2) inhibits VMAT2 activity in synaptic vesicles. PMID: 19457116

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Subcellular Location Cytoplasm, Melanosome, Nucleus, nucleolus, Cell membrane
Protein Families Heat shock protein 70 family
Database Links

KEGG: rno:24468

STRING: 10116.ENSRNOP00000058593

UniGene: Rn.120392

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