Recombinant Human HSC70 Protein (His Tag)

Name: Recombinant Human HSC70 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-2459
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	P11142
Synonym	HEL-33, HEL-S-72p, HSC54, HSC70, HSC71, HSP71, HSP73, HSPA10, LAP-1, LAP1, NIP71
Background	HSPA8, also known as HSC7, is a member of the heat shock protein family due to homology with other heat shock proteins. The heat shock protein 7 family is comprised by both heat-inducible and constitutively expressed members. The latter are called heat-shock cognate proteins. HSPA8 belongs to the heat-shock cognate subgroup. Members of the human heat-shock protein multigene family have several highly conserved proteins with structural and functional properties in common, but vary in the extent of their inducibility in response to metabolic stress. HSPA8 is constitutively expressed and performs functions related to normal cellular processes. This protein binds to nascent polypeptides to facilitate correct protein folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Two alternatively spliced variants have been characterized to date. HSPA8 acts as a repressor of transcriptional activation. It inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Isoform 2 may function as an endogenous inhibitory regulator of HSC7 by competing the co-chaperones. It also is a ATPase that works with auxilin to remove clathrin coated vesicles. In neurons, synaptojanin is also an important protein involved in vesicle uncoating.
Description	A DNA sequence encoding the human HSPA8 (P11142-1) (Met 1-Asp 646) was expressed, with a His tag at the N-terminus.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Met 1-Asp 646
Molecular Weight	The recombinant human HSPA8 consisting of 657 a.a. and has a calculated molecular mass of 72.4 kDa. The apparent molecular mass of the protein is approximately 65 kDa in SDS-PAGE under reducing conditions.
Purity	>90% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, 10% glycerol, pH 7.5.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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. 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.
Protein Families	Heat shock protein 70 family
Database References	HGNC: 5241 OMIM: 600816 KEGG: hsa:3312 STRING: 9606.ENSP00000227378 UniGene: Hs.180414
Tissue Specificity	Ubiquitous.

Gene Functions References

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
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
Hsp70participated in PINK1-mediated mitophagy by stabilizing PINK1. PMID: 29107085
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
Post-transcriptional inhibition of HSPA8 expression leads to synaptic vesicle cycling defects in multiple models of amyotrophic lateral sclerosis. PMID: 28978466
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
The roles of the E3 ubiquitin ligase, carboxy-terminus Hsc70 interacting protein (CHIP) in various types of cancers. PMID: 28731191
Hsc70/Hsp90 chaperones contribute to the conformational and functional maintenance of DeltaF508-CFTR at 37 degrees C. PMID: 28855508
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
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
STRO-1 binds to immune-precipitated HSC70 and siRNA-mediated knock down of HSPA8 reduced STRO-1 binding. PMID: 28026090
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
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
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
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
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
HSPA8 maintains pluripotency of human pluripotent stem cells by binding to the master pluripotency regulator OCT4 and facilitating its DNA-binding activity. PMID: 26549849
heat shock cognate 70 (HSC70) is an essential component of Aes foci in colorectal cancer cells. PMID: 26229111
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
serum HSC71 was identified as a novel serum biomarker of renal cell carcinoma, particularly useful in early diagnosis of clear-cell type. PMID: 26425554
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
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
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
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
detailed and systematic investigation to characterize if there are significant differences in the CHIP in vitro ubiquitination of human Hsp70 and Hsc70. PMID: 26010904
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
LAP1 mutations are associated with severe dystonia, cerebellar atrophy and cardiomyopathy. PMID: 26596547
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
CHIP docks onto Hsp70/Hsc70 and defines a bipartite mode of interaction between TPR domains and their binding partners. PMID: 25684577
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
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
LAP1 and LULL1 regulate Torsin ATPase activity through an active site complementation mechanism. PMID: 25352667
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
the endogenous DNAJC12 and Hsc70 proteins interact in LNCaP cells. PMID: 24122553
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
Results identify a systemic hsc70 reduction in Parkinson's disease patients. PMID: 24361989
Hsp73 sustains Hsp90 chaperone function and critically contributes to cell survival in multiple myeloma patients. PMID: 23065523
These findings indicate that wild type ILK and the non-oncogenic ILK(R211A) mutation comprise a cardioprotective module with Hsp/c70. PMID: 24260102
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
HSP8A polymorphism is associated with drug-naive schizophrenia. PMID: 24548631
Cx43-Hsc70 interaction probably plays a critical role during G1/S progression. PMID: 24056538
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
Altered expression of Hsc70 and eIF5A-1 may cause defects in nucleocytoplasmic transport and play a role in esophageal carcinogenesis. PMID: 23539416
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
GLIPR1 interacts with Hsc70, and GLIPR1 overexpression or Hsc70 knockdown leads to transcriptional suppression of AURKA and TPX2. PMID: 23333597
PKCiota knockdown sensitized cells to oxidative stress-induced apoptosis, whereas forced PKCiota expression counteracted the oxidative stress-induced apoptosis via Hsc70. PMID: 23224638
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
LAP1 and LULL1 as regulatory cofactors that are responsible for the activation of TorA's ATPase activity. PMID: 23569223
70-kDa heat shock cognate protein hsc70 mediates calmodulin-dependent nuclear import of the sex-determining factor SRY. PMID: 23235156
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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