Recombinant Bovine Heat shock cognate 71 kDa protein(HSPA8) ,partial

Code CSB-YP010829BO
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Source Yeast
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Code CSB-EP010829BO
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Source E.coli
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Code CSB-EP010829BO-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-BP010829BO
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Source Baculovirus
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Code CSB-MP010829BO
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names HSPA8
Uniprot No. P19120
Alternative Names HSPA8; HSC70; Heat shock cognate 71 kDa protein; Heat shock 70 kDa protein 8
Species Bos taurus (Bovine)
Protein Length Partial
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. Single-particle fluorescence imaging tracks the dynamics of Hsc70 and its clathrin substrate in real time. PMID: 21278753
  2. The interaction of the molecular chaperone Hsc70 (HSPA8) with recombinant PrP was investigated. PMID: 20434583
  3. Structure of clathrin coat with bound Hsc70 and auxilin. PMID: 20033059
  4. specific association between HSP73 and gentamicin may reduce the chaperone activity of HSP73 in vitro and/or in vivo PMID: 14966137
  5. report role of HSC70 in the regulation of NMT PMID: 15156568
  6. studied the process of disassembly by using cryo-electron microscopy to identify the initial binding site of Hsc70 on clathrin-C58J baskets at pH 6, under which conditions disassembly does not proceed further. Hsc70 interactions involve two sites PMID: 15596443
  7. Coats assembled from recombinant clathrin are good substrates for ATP- and auxilin-dependent, Hsc70-catalyzed uncoating. PMID: 17978091
  8. The structure of an Hsp110:Hsc70 nucleotide exchange complex, is reported. PMID: 18550409
  9. analysis of the formation of a stable complex between chaperonin-containing TCP-1 (CCT) and Hsc70 PMID: 18660820
  10. Elevated expression of bovine heat shock cognate (hsc)70 protein increases diabetes and inflammation following islet beta cell damage in a transgenic mouse model. PMID: 19812207

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

KEGG: bta:281831

STRING: 9913.ENSBTAP00000017497

UniGene: Bt.12309

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