Heat Shock 70kDa Protein 8 (HSPA8) ELISA Kits

Xenopus laevis Heat Shock 70kDa Protein 8 (HSPA8) interaction partners

1. hsp72 was more potent than hsc73 in generating protective immune responses against the class Ia-negative 15/0 tumors.

Human Heat Shock 70kDa Protein 8 (HSPA8) interaction partners

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)

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.

3. Hsp70participated in PINK1-mediated mitophagy by stabilizing PINK1.

4. These results demonstrate not only an important mechanism of Hsc70 in facilitating EV-A71 replication, but also a target for antiviral drug development.

5. Post-transcriptional inhibition of HSPA8 expression leads to synaptic vesicle cycling defects in multiple models of amyotrophic lateral sclerosis.

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.

7. The roles of the E3 ubiquitin ligase, carboxy-terminus Hsc70 interacting protein (CHIP) in various types of cancers.

8. Hsc70/Hsp90 chaperones contribute to the conformational and functional maintenance of DeltaF508-CFTR at 37 degrees C.

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.

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.

11. STRO-1 binds to immune-precipitated HSC70 and siRNA-mediated knock down of HSPA8 reduced STRO-1 binding.

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.

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

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.

15. HSPA1A and HSPA8 have roles in parturition through stimulating immune inflammatory and estrogen response

16. 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.

17. 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

18. HSPA8 maintains pluripotency of human pluripotent stem cells by binding to the master pluripotency regulator OCT4 and facilitating its DNA-binding activity.

19. heat shock cognate 70 (HSC70) is an essential component of Aes foci in colorectal cancer cells.

20. 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.

Cow (Bovine) Heat Shock 70kDa Protein 8 (HSPA8) interaction partners

1. Single-particle fluorescence imaging tracks the dynamics of Hsc70 and its clathrin substrate in real time.

2. The interaction of the molecular chaperone Hsc70 (HSPA8) with recombinant PrP was investigated.

3. Structure of clathrin coat with bound Hsc70 and auxilin.

4. specific association between HSP73 and gentamicin may reduce the chaperone activity of HSP73 in vitro and/or in vivo

5. report role of HSC70 in the regulation of NMT

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

7. Coats assembled from recombinant clathrin are good substrates for ATP- and auxilin-dependent, Hsc70-catalyzed uncoating.

8. The structure of an Hsp110:Hsc70 nucleotide exchange complex, is reported.

9. analysis of the formation of a stable complex between chaperonin-containing TCP-1 (CCT) and Hsc70

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.

Mouse (Murine) Heat Shock 70kDa Protein 8 (HSPA8) interaction partners

1. Post-transcriptional inhibition of HSPA8 expression leads to synaptic vesicle cycling defects in multiple models of amyotrophic lateral sclerosis.

2. 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.

3. Hsc70 interacts with FILIP to mediate its effects on non-muscle myosin IIb and to regulate spine morphology

4. HSPA1A and HSPA8 have roles in parturition through stimulating immune inflammatory and estrogen response

5. 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.

6. 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.

7. C terminus of the hsc-70 LID domain as the structural interface interacting with endosomal Phosphatidylserine

8. the association of MNSFbeta with HSPA8 may promote RANKL-induced osteoclastogenesis.

9. Hspa8 plays a vital role in genetic differences in responses to stress and ethanol and their interactions

10. 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.

11. mass spectrometry-based proteomic analysis identified heat shock cognate 70 (HSC70) as a novel binding protein of FSP27

12. These findings indicate that wild type ILK and the non-oncogenic ILK(R211A) mutation comprise a cardioprotective module with Hsp/c70.

13. these data provide evidence for Hsc70 as a novel neuronal interactor of NF-kappaB p65.

14. 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.

15. 70-kDa heat shock cognate protein hsc70 mediates calmodulin-dependent nuclear import of the sex-determining factor SRY.

16. Hsc70, Hdj1 and Hdj2 interact with soluble and fibrillar alpha-synuclein

17. BAG3 and Hsc70 interact with actin capping protein CapZ to maintain myofibrillar integrity under mechanical stress.

18. 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.

19. 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.

20. Heat shock protein 70 (Hsc70) plays a significant role in vascular endothelial cells via the phosphatidylinositol 3-kinase/Akt pathway.