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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 (265) and HSPA8 Proteins (25) and many more products for this protein.
Showing 6 out of 30 products:
Human HSPA8 ELISA Kit for Sandwich ELISA - ABIN2964823
Boĭko, Vetchinin, Sapozhnikov, Kovalenko: [Alterations in heat shock protein 70 kDa levels in human neutrophils under the heat shock conditions]. in Bioorganicheskaia khimiia 2015
Human HSPA8 ELISA Kit for Sandwich ELISA - ABIN415190
Mishra, Lobo, Joshi, Rathos, Kumar, Padigaru: Molecular mechanisms of anti-tumor properties of P276-00 in head and neck squamous cell carcinoma. in Journal of translational medicine 2013
Rat (Rattus) HSPA8 ELISA Kit for Sandwich ELISA - ABIN433381
Feng, Wang, Zhang, Gao, Tao, Ge, Zhu, Bi: Modulation of gut microbiota contributes to curcumin-mediated attenuation of hepatic steatosis in rats. in Biochimica et biophysica acta 2017
hsp72 (show HSPA1A ELISA Kits) was more potent than hsc73 in generating protective immune responses against the class Ia-negative 15/0 tumors.
Hsc70/Hsp90 (show HSP90 ELISA Kits) chaperones contribute to the conformational and functional maintenance of DeltaF508-CFTR (show CFTR ELISA Kits) at 37 degrees C.
Engagement of the oligomer by LAP1 (show ANPEP ELISA Kits) 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 ELISA Kits), and IL-15 (show IL15 ELISA Kits) 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 controls Hsc70 to impact this process
In fact, DnaJC5 (show DNAJC5 ELISA Kits) 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 ELISA Kits) and HSPA8 have roles in parturition through stimulating immune inflammatory and estrogen response
These results suggest that Bag1 and Bag3 (show BAG3 ELISA Kits) 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 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
Single-particle fluorescence imaging tracks the dynamics of Hsc70 and its clathrin substrate in real time.
The interaction of the molecular chaperone (show HSP90AA1 ELISA Kits) Hsc70 (HSPA8) with recombinant PrP (show PRNP ELISA Kits) was investigated.
Structure of clathrin coat with bound Hsc70 and auxilin.
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-dependent, Hsc70-catalyzed uncoating.
The structure of an Hsp110 (show HSPH1 ELISA Kits):Hsc70 nucleotide exchange complex, is reported.
analysis of the formation of a stable complex between chaperonin-containing TCP-1 (CCT) 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 (show MYH10 ELISA Kits) 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 ELISA Kits) with HSPA8 may promote RANKL (show TNFSF11 ELISA Kits)-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 ELISA Kits)
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