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HSPA8 encodes a member of the heat shock protein 70 family, which contains both heat-inducible and constitutively expressed members.
Showing 10 out of 340 products:
Hamster Polyclonal HSPA8 Primary Antibody for BI, ICC - ABIN361819
Boorstein, Ziegelhoffer, Craig: Molecular evolution of the HSP70 multigene family. in Journal of molecular evolution 1994
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Human Monoclonal HSPA8 Primary Antibody for AA, Bind - ABIN361800
Bork, Sander, Valencia: An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. in Proceedings of the National Academy of Sciences of the United States of America 1992
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Human Polyclonal HSPA8 Primary Antibody for FACS, IF - ABIN1944844
Tsukahara, Yoshioka, Muraki: Molecular and functional characterization of HSC54, a novel variant of human heat-shock cognate protein 70. in Molecular pharmacology 2000
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Human Polyclonal HSPA8 Primary Antibody for ELISA, WB - ABIN188549
Zhang, Fan, Becker, Graff, Lee, Francomano: Comparison of gene expression profile between human chondrons and chondrocytes: a cDNA microarray study. in Osteoarthritis and cartilage / OARS, Osteoarthritis Research Society 2006
Human Polyclonal HSPA8 Primary Antibody for IF (p), IHC (p) - ABIN709931
Almiñana, Corbin, Tsikis, Alcântara-Neto, Labas, Reynaud, Galio, Uzbekov, Garanina, Druart, Mermillod: Oviduct extracellular vesicles protein content and their role during oviduct-embryo cross-talk. in Reproduction (Cambridge, England) 2017
Fish Polyclonal HSPA8 Primary Antibody for WB - ABIN361860
Brown, Hong-Brown, Doxsey, Welch: Molecular chaperones and the centrosome. A role for HSP 73 in centrosomal repair following heat shock treatment. in The Journal of biological chemistry 1996
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hsp72 (show HSPA1A Antibodies) was more potent than hsc73 in generating protective immune responses against the class Ia-negative 15/0 tumors.
These results demonstrate not only an important mechanism of Hsc70 in facilitating EV-A71 replication, but also a target for antiviral drug development.
Post-transcriptional inhibition of HSPA8 expression leads to synaptic vesicle cycling defects in multiple models of amyotrophic lateral sclerosis.
Taken together, these data suggest hat (show MGEA5 Antibodies) the altered hydrogen bonding observed in the Hsc70 C17W mutant (where the connectivity between Mg2 (show MUC7 Antibodies)+.nucleotide and E175 is also disrupted) could bring about changes to Hsc70 domain communication, affecting peptide association while also limiting ATP hydrolysis.
The roles of the E3 ubiquitin ligase (show MUL1 Antibodies), carboxy-terminus Hsc70 interacting protein (show ST13 Antibodies) (CHIP) in various types of cancers.
Hsc70/Hsp90 (show HSP90 Antibodies) chaperones contribute to the conformational and functional maintenance of DeltaF508-CFTR (show CFTR Antibodies) at 37 degrees C.
Engagement of the oligomer by LAP1 (show ANPEP Antibodies) 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 Antibodies), and IL-15 (show IL15 Antibodies) 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 Antibodies) controls Hsc70 to impact this process
Single-particle fluorescence imaging tracks the dynamics of Hsc70 and its clathrin substrate in real time.
The interaction of the molecular chaperone (show HSP90AA1 Antibodies) Hsc70 (HSPA8) with recombinant PrP (show PRNP Antibodies) was investigated.
Structure of clathrin coat with bound Hsc70 and auxilin (show DNAJC6 Antibodies).
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 Antibodies)-dependent, Hsc70-catalyzed uncoating.
The structure of an Hsp110 (show HSPH1 Antibodies):Hsc70 nucleotide exchange complex, is reported.
analysis of the formation of a stable complex between chaperonin-containing TCP-1 (show CCT6A Antibodies) (CCT (show TCP1 Antibodies)) 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 (show FILIP1 Antibodies) to mediate its effects on non-muscle myosin IIb (show MYH10 Antibodies) and to regulate spine morphology
HSPA1A (show HSPA1A Antibodies) and HSPA8 have roles in parturition through stimulating immune inflammatory and estrogen response
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 Antibodies) with HSPA8 may promote RANKL (show TNFSF11 Antibodies)-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.
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