• DnaJ (Hsp40) homolog, subfamily C, member 9 is a protein that in humans is encoded by the DNAJC9 gene. (wikipedia.org)
  • Xenopus tropicalis DnaJ heat shock protein family (Hsp40) member B11 (dnajb11), mRNA. (genscript.com)
  • and DnaJ homologs dj1 (DjB1/Hsp40/hdj-1), dj2 (DjA1/HSDJ/hdj-2), dj3 (DjA2), and dj4 (DjA4), in the liver of CCl 4 -treated rats was analyzed. (bioone.org)
  • Manipulation of HSP70 and HSP40 chaperone levels has been shown to suppress aggregates in cellular models, prevent neuronal death in Drosoph-ila, and improve to some extent neurological symptoms in mouse models. (hal.science)
  • Furthermore, overexpression of both HSP70 and its co-factor HSP40/HDJ2 has never been investigated in mice. (hal.science)
  • Aim: To elucidate the role of human Lon and ClpXP proteases, and the Hsp70/Hsp40 chaperone system in the elimination of the core mitochondrial DNA replisome. (hhs.gov)
  • HSP70, together with the DNAJA2 member of HSP40 co-chaperones, is the main chaperone involved in IRES-mediated translation of the viral genome, while HSP90 may play some role as well. (wjgnet.com)
  • ATP-dependent dimerization of stress-inducible Hsp70 is necessary for its efficient interaction with Hsp40, as shown by experiments with dimerization-deficient mutants. (muni.cz)
  • Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. (enzolifesciences.com)
  • IMPORTANT: HSP40/DNAJB1 (Catalog # AP-110), or another suitable co-chaperone, is required for HSP70/HSPA1A activity and should be used at a concentration that is equimolar to HSP70/HSPA1A. (novusbio.com)
  • However, if either of these processes proceeds too slowly or fails, HSP70/HSPA1A can interact with the HSP40 co-chaperone protein and the CHIP/STUB1 Ubiquitin ligase (E3) to promote ubiquitination and degradation of the nascent polypeptide or denatured protein (3,4). (novusbio.com)
  • This assay has high sensitivity and excellent specificity for detection of Heat Shock Protein 40 (HSP40). (uscnk.com)
  • No significant cross-reactivity or interference between Heat Shock Protein 40 (HSP40) and analogues was observed. (uscnk.com)
  • Matrices listed below were spiked with certain level of recombinant Heat Shock Protein 40 (HSP40) and the recovery rates were calculated by comparing the measured value to the expected amount of Heat Shock Protein 40 (HSP40) in samples. (uscnk.com)
  • Intra-assay Precision (Precision within an assay): 3 samples with low, middle and high level Heat Shock Protein 40 (HSP40) were tested 20 times on one plate, respectively. (uscnk.com)
  • Inter-assay Precision (Precision between assays): 3 samples with low, middle and high level Heat Shock Protein 40 (HSP40) were tested on 3 different plates, 8 replicates in each plate. (uscnk.com)
  • The linearity of the kit was assayed by testing samples spiked with appropriate concentration of Heat Shock Protein 40 (HSP40) and their serial dilutions. (uscnk.com)
  • The microtiter plate provided in this kit has been pre-coated with an antibody specific to Heat Shock Protein 40 (HSP40). (uscnk.com)
  • Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody specific to Heat Shock Protein 40 (HSP40). (uscnk.com)
  • After TMB substrate solution is added, only those wells that contain Heat Shock Protein 40 (HSP40), biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. (uscnk.com)
  • The concentration of Heat Shock Protein 40 (HSP40) in the samples is then determined by comparing the O.D. of the samples to the standard curve. (uscnk.com)
  • Human heat shock 40 protein (Hsp40) was identified as an interacting partner of Influenza A virus nucleoprotein (IAV NP) using a yeast two-hybrid screen. (nih.gov)
  • Another protein chaperone, Hsp104, acts with Hsp70 and Hsp40 to break up and reactivate proteins that have become aggregated. (nih.gov)
  • Hsp70 and Hsp40 Functionally Interact with Soluble Mutant Huntingtin O" by Gregor P. Lotz, Justin Legleiter et al. (marquette.edu)
  • The molecular chaperones Hsp70 and Hsp40 colocalize to inclusion bodies and are neuroprotective in HD animal models. (marquette.edu)
  • Thus, Hsp70 and Hsp40 (DNAJB1) dynamically target specific subsets of soluble oligomers in a classic ATP-dependent reaction cycle, supporting a pathogenic role for these structures in HD. (marquette.edu)
  • 30. Specification of Hsp70 function by Type I and Type II Hsp40. (nih.gov)
  • PKR activity is regulated by a 58 kilo Dalton cellular inhibitor (P58(IPK)), which is present in inactive state as a complex with Hsp40 under normal conditions. (nih.gov)
  • Hsp70 associated with A11-reactive oligomers in an Hsp40- and ATP-dependent manner and inhibited their formation coincident with suppression of caspase 3 activity in PC12 cells. (marquette.edu)
  • Hsp70 activity is regulated by co-chaperones, such as Hsp40. (nih.gov)
  • Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. (enzolifesciences.com)
  • Cellular localization studies showed that NP and Hsp40 co-localize primarily in the nucleus. (nih.gov)