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HSPA8 encodes a member of the heat shock protein 70 family, which contains both heat-inducible and constitutively expressed members. Additionally we are shipping HSPA8 Antibodies (266) and HSPA8 Kits (30) and many more products for this protein.
Showing 10 out of 25 products:
Human HSPA8 Protein expressed in Escherichia coli (E. coli) - ABIN1686679
DeLuca-Flaherty, McKay, Parham, Hill: Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. in Cell 1990
Show all 10 Pubmed References
Human HSPA8 Protein expressed in Escherichia coli (E. coli) - ABIN2215709
Thirunavukarasu, Shi: An RNA aptamer specific to Hsp70-ATP conformation inhibits its ATPase activity independent of Hsp40. in Nucleic acid therapeutics 2015
Show all 2 Pubmed References
Human HSPA8 Protein expressed in Wheat germ - ABIN1307208
Chow, Mok, Xiao, Khalouei, Brown: Heteromeric complexes of heat shock protein 70 (HSP70) family members, including Hsp70B', in differentiated human neuronal cells. in Cell stress & chaperones 2010
hsp72 (show HSPA1A Proteins) was more potent than hsc73 in generating protective immune responses against the class Ia-negative 15/0 tumors.
Engagement of the oligomer by LAP1 (show ANPEP Proteins) 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.
Downregulation of Hsc70, Hsp70 (show HSP70 Proteins), and IL-15 (show IL15 Proteins) expression at gene and/or protein levels might support the retention of fertilization products in cases of missed abortion and blighted ovum.
STRO-1 binds to immune-precipitated HSC70 and siRNA-mediated knock down of HSPA8 reduced STRO-1 binding.
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.
study demonstrates a critical role of Hsc70 in SV40 endoplasmic reticulum-to-cytosol penetration and reveal how SGTA (show SGTA Proteins) controls Hsc70 to impact this process
In fact, DnaJC5 (show DNAJC5 Proteins) 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.
HSPA1A (show HSPA1A Proteins) and HSPA8 have roles in parturition through stimulating immune inflammatory and estrogen response
These results suggest that Bag1 (show BAG1 Proteins) and Bag3 (show BAG3 Proteins) 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.
While cerebrospinal fluid Nrf2 (show GABPA Proteins) and HSPA8 do not appear to offer diagnostic biomarkers for Parkinson's disease (PD), the associations between Nrf2 (show GABPA Proteins) levels and UPDRS scores in LRRK2 (show LRRK2 Proteins) + PD patients merit further investigation
HSPA8 maintains pluripotency of human pluripotent stem cells by binding to the master pluripotency regulator OCT4 (show POU5F1 Proteins) and facilitating its DNA-binding activity.
Single-particle fluorescence imaging tracks the dynamics of Hsc70 and its clathrin substrate in real time.
The interaction of the molecular chaperone (show HSP90AA1 Proteins) Hsc70 (HSPA8) with recombinant PrP (show PRNP Proteins) was investigated.
Structure of clathrin coat with bound Hsc70 and auxilin (show DNAJC6 Proteins).
specific association between HSP73 and gentamicin may reduce the chaperone activity of HSP73 in vitro and/or in vivo
report role of HSC70 in the regulation of NMT
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
Coats assembled from recombinant clathrin are good substrates for ATP- and auxilin (show DNAJC6 Proteins)-dependent, Hsc70-catalyzed uncoating.
The structure of an Hsp110 (show HSPH1 Proteins):Hsc70 nucleotide exchange complex, is reported.
analysis of the formation of a stable complex between chaperonin-containing TCP-1 (show CCT6A Proteins) (CCT (show TCP1 Proteins)) and Hsc70
Elevated expression of bovine heat shock cognate (hsc)70 protein increases diabetes and inflammation following islet beta cell damage in a transgenic mouse model.
Hsc70 interacts with FILIP to mediate its effects on non-muscle myosin IIb and to regulate spine morphology
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.
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.
C terminus of the hsc-70 LID domain as the structural interface interacting with endosomal Phosphatidylserine
the association of MNSFbeta (show FAU Proteins) with HSPA8 may promote RANKL (show TNFSF11 Proteins)-induced osteoclastogenesis.
Hspa8 plays a vital role in genetic differences in responses to stress and ethanol and their interactions
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.
mass spectrometry-based proteomic analysis identified heat shock cognate 70 (HSC70) as a novel binding protein of FSP27 (show CIDEC Proteins)
This gene encodes a member of the heat shock protein 70 family, which contains both heat-inducible and constitutively expressed members. This protein belongs to the latter group, which are also referred to as heat-shock cognate proteins. It functions as a chaperone, and binds to nascent polypeptides to facilitate correct folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
LPS-associated protein 1
, N-myristoyltransferase inhibitor protein 71
, constitutive heat shock protein 70
, heat shock 70kd protein 10
, heat shock cognate 71 kDa protein
, heat shock cognate protein 54
, lipopolysaccharide-associated protein 1
, Hsc70 ATPase
, heat shock 70 kDa protein 8
, heat shock 70kd protein 10 (HSC71)
, heat shock cognate 71 kD protein
, Heat shock cognate protein 70
, heat shock 70kD protein 8
, heat shock protein 8
, heat shock protein A8
, heat shock cognate 70
, heat shock cognate 71 kDa protein-like protein
, heat shock protein 70 cognate
, heat shock cognate hsc73
, heat shock protein cognate 70
, heat shock 70kDa protein 8
, heat shock cognate 71-kd protein