Recombinant Mouse Heat Shock Cognate 71 Kda Protein (HSPA8) Protein (His&Myc)

Name: Recombinant Mouse Heat Shock Cognate 71 Kda Protein (HSPA8) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06971P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Heat Shock Cognate 71 Kda Protein (HSPA8) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P63017
Target Symbol	HSPA8
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	SKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIISWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
Expression Range	2-646aa
Protein Length	Full Length of Mature Protein
Mol. Weight	78.2 kDa
Research Area	Signal Transduction
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	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.
Subcellular Location	Cytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane.
Protein Families	Heat shock protein 70 family
Database References	KEGG: mmu:15481 STRING: 10090.ENSMUSP00000015800 UniGene: Mm.290774
Tissue Specificity	Ubiquitous.

Gene Functions References

Post-transcriptional inhibition of HSPA8 expression leads to synaptic vesicle cycling defects in multiple models of amyotrophic lateral sclerosis. PMID: 28978466
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
Hsc70 interacts with FILIP to mediate its effects on non-muscle myosin IIb and to regulate spine morphology PMID: 28234934
HSPA1A and HSPA8 have roles in parturition through stimulating immune inflammatory and estrogen response PMID: 28025138
intracellular Salmonella recruit the host proteins LAMP-2A and Hsc73, key components of the host protein turnover pathway known as chaperone-mediated autophagy involved in transport of cytosolic proteins to the lysosome for degradation. PMID: 27932462
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
C terminus of the hsc-70 LID domain as the structural interface interacting with endosomal Phosphatidylserine PMID: 27405763
Hspa8 plays a vital role in genetic differences in responses to stress and ethanol and their interactions PMID: 26780340
PTEN-like domains of GAK and auxilin are not essential for Hsc70-dependent chaperoning and uncoating of clathrin, but depending on the tissue, these domains appear to increase the efficiency of these co-chaperones. PMID: 26345367
mass spectrometry-based proteomic analysis identified heat shock cognate 70 (HSC70) as a novel binding protein of FSP27 PMID: 25315694
These findings indicate that wild type ILK and the non-oncogenic ILK(R211A) mutation comprise a cardioprotective module with Hsp/c70. PMID: 24260102
these data provide evidence for Hsc70 as a novel neuronal interactor of NF-kappaB p65. PMID: 23762333
In heat stress conditions, Hsp73 is mobilized to prevent apoptosis in the testes and epididymis, and assists Hsp72 in the repair of stress-altered protein conformations. PMID: 23352621
Hsc70, Hdj1 and Hdj2 interact with soluble and fibrillar alpha-synuclein PMID: 21832061
In this study, we report an identification of Hsc70 (Heat shock cognate protein 70) as a critical mediator of RGS9-2 expression that is specifically recruited to the intrinsically disordered C-terminal domain of RGS9-2 following dissociation from R7BP. PMID: 20095651
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
Heat shock protein 70 (Hsc70) plays a significant role in vascular endothelial cells via the phosphatidylinositol 3-kinase/Akt pathway. PMID: 20018937
surface located Hsc70 on trophoblast giant cells mediates the uptake of pathogenic bacteria and proteins containing the TPR domain inhibit the function of Hsc70 by binding to its EEVD motif PMID: 20003465
Data show that ezrin associates with Hsc70 that locates on the membrane of TG cells and participates in the bacterial uptake by TG cells. PMID: 19737422
Differential acquisition of antigenic peptides by Hsp70 and Hsc70 under oxidative condition. PMID: 12114509
HSC70 has a specific tetratricopeptide repeat motif that enables it to bind to mSTI1 PMID: 12482845
Hsc70 attenuates Dbl activity by maintaining an inactive conformation in which the amino terminus is "folded over" the catalytic DH-PH domain PMID: 15802271
Results suggest an important role for KLF4 as a novel regulator of the constitutive expression of HSP73, but not HSP72. PMID: 18379898
Data show that although Hsp70 and Hsc70 are both basally synthesized they have different cellular distributions, suggesting different Hsp70 activity with respect to Hsc70. PMID: 18841484
Brucella abortus infection of trophoblast giant cells in placenta is mediated by Hsc70. PMID: 19055850
These results imply the 70-kDa heat shock cognate protein-Toll-like receptor 4 interaction is a novel mechanism underlying the myocardial chemokine response to global ischemia-reperfusion PMID: 19448144

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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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