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The protein encoded by TCP1 is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). Zusätzlich bieten wir Ihnen T-Complex 1 Proteine (10) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 252 products:
Human Monoclonal TCP1 Primary Antibody für IF, IHC (p) - ABIN563128
Seo, Baye, Schulz, Beck, Zhang, Slusarski, Sheffield: BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly. in Proceedings of the National Academy of Sciences of the United States of America 2010
Human Polyclonal TCP1 Primary Antibody für IHC (p), IHC - ABIN250182
Yaffe, Farr, Miklos, Horwich, Sternlicht, Sternlicht: TCP1 complex is a molecular chaperone in tubulin biogenesis. in Nature 1992
treating BACHD cortical neurons with ApiCCT1 prevented BACHD striatal neuronal atrophy by enhancing release of BDNF (zeige BDNF Antikörper) that subsequently acts through tyrosine receptor kinase B (TrkB (zeige NTRK2 Antikörper)) receptor on striatal neurons. Our findings are evidence that TRiC (zeige MARVELD2 Antikörper) reagent-mediated reductions in mHTT enhanced BDNF (zeige BDNF Antikörper) delivery to restore the trophic status of BACHD striatal neurons.
this study shows that CCTalpha (zeige PCYT1A Antikörper) is required for antigen-specific, germinal center-derived memory B cells
Data show that T-complex protein 1 (TCP-1) may be a crucial downstream mo (zeige P2RX7 Antikörper)lecule (zeige P2RX7 Antikörper)of purinergic receptor P2X 7 (P2X7R) and plays a role in lymphoid neoplasm metastasis.
The data presented here reveal an additional level of interplay between CCT (zeige FLVCR2 Antikörper) and actin mediated via gelsolin (zeige GSN Antikörper), suggesting that CCT (zeige FLVCR2 Antikörper) may influence processes depending on gelsolin (zeige GSN Antikörper) activity, such as cell motility.
Host CCTalpha (zeige PCYT1A Antikörper) is required for efficient transcription and replication of rabies virus.
Our data provide new evidence indicating the essential role of the chaperonin CCT in the biogenesis of vertebrate photoreceptor sensory cilia
Results suggest that chaperonin containing t-complex protein 1 (CCT) is required for efficient delivery of enzymatically active toxin to the cytosol and are consistent with a direct role for CCT in translocation of LF through the protective antigen pore.
Normal CCT function is ultimately required for the morphogenesis and survival of sensory neurons of the retina.
TRiC (zeige MARVELD2 Antikörper)-peptide complexes of the heat shock protein 60 (zeige HSPD1 Antikörper) family are efficient vehicles of cross-presentation in assays in vitro and in mice in vivo; immunization with TRiC (zeige MARVELD2 Antikörper) purified from a tumor elicits specific protection against a challenge with that tumor.
downregulated expression in T cells following treatment with bis (zeige BAG3 Antikörper)(tri (zeige VANGL2 Antikörper)-n-butylin)oxide (TBTO), an immunotoxic organotin
Result suggest the positive correlation between purinergic receptor P2X 7 (zeige P2RX7 Antikörper) (P2X7R (zeige P2RX7 Antikörper)) and T-complex protein 1 (TCP-1) in lymphoma patients.
Data suggest that biosynthesis and folding of leukemogenic fusion oncoprotein AML1 (zeige RUNX1 Antikörper)-ETO (zeige RUNX1T1 Antikörper)/RUNX1 (zeige RUNX1 Antikörper)-RUNX1T1 (zeige RUNX1T1 Antikörper) is facilitated by interaction with the chaperonin (zeige HSPD1 Antikörper) TRiC/CCT1/TCP1 and HSP70 (heat shock protein 70 (zeige HSP70 Antikörper)).
Changes for CRMP2 (zeige DPYSL2 Antikörper), TCP1epsilon, TPM2 (zeige TPM2 Antikörper) and 14-3-3gamma (zeige YWHAG Antikörper) were confirmed in experimental tumors and in a series of 28 human SI-NETs.
A role for the TRiC (zeige MARVELD2 Antikörper) subunits TCP1 and CCT2 (zeige CCT2 Antikörper), and potentially the entire TRiC (zeige MARVELD2 Antikörper) complex, in breast cancer.
CCT8 (zeige CCT8 Antikörper) might be an oncogene (zeige RAB1A Antikörper) and participate in HCC (zeige FAM126A Antikörper) cell proliferation.
identified 6 of the 8 components of the chaperonin-containing TCP-1 (zeige CCT6A Antikörper) (CCT) complex bound to LOX-1 (zeige OLR1 Antikörper) cytoplasmic domain
Data suggest that specific molecular mediators involved in glucocerebrosidase (zeige GBA Antikörper) maturation and degradation, and abnormal interaction with TCP1 and c-Cbl (zeige CBL Antikörper), could be responsible for phenotypic variation among patients with the same genotypes.
Expression patterns of chaperone proteins in cerebral cortex of the fetus with Down syndrome: dysregulation of T-complex protein 1 (zeige CCT3 Antikörper).
TRiC (zeige MARVELD2 Antikörper) chaperonin (zeige HSPD1 Antikörper) binds to HIF prolyl hydroxylase PHD3 (zeige EGLN3 Antikörper)
the strong inhibitory action of PhLP (zeige PDCL Antikörper)(S) on Gbetagamma signaling is the result of a previously unrecognized mechanism of Gbetagamma-regulation, inhibition of Gbetagamma-folding by interference with TCP-1alpha
The mammalian TRiC structure was determined at 4.7-A resolution.
Results indicate that the kinetic mechanism of the allosteric transitions of chaperonin (zeige HSPD1 Antikörper) containing t-complex polypeptide 1 (TCP-1) differs considerably from that of GroEL (zeige GroEL Antikörper)
unlike GroEL (zeige GroEL Antikörper), TRiC does not close its lid upon nucleotide binding, but instead responds to the trigonal-bipyramidal transition state of ATP hydrolysis.
Data show that chaperonin (zeige HSPD1 Antikörper) TRiC binding is specified by two short hydrophobic beta strands in the von Hippel-Lindau protein (zeige VHLL Antikörper) that, upon folding, become buried within the native structure [TRiC].
antagonistic actions of PhLP3 and prefoldin serve to modulate CCT activity and play a key role in establishing a functional cytoskeleton in vivo
one of the cytosolic chaperonin containing t-complex polypeptide 1 (CCT)/TRiC-specific targets is hydrophobic beta-strands, which are highly prone to aggregation
Domain movements in TRiC are coordinated through unique interdomain contacts within each subunit and, further, these contacts are absent in prokaryotic chaperonins.
analysis of the formation of a stable complex between chaperonin-containing TCP-1 (zeige CCT6A Antikörper) (CCT) and Hsc70 (zeige HSPA8 Antikörper)
The protein encoded by this gene is a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized. In addition, three pseudogenes that appear to be derived from this gene have been found.
T-complex protein 1 subunit alpha
, T-complex protein 1, alpha subunit
, tailless complex polypeptide 1
, T-complex protein 1 subunit alpha A
, T-complex protein 1 subunit alpha B
, t-complex polypeptide 1
, tailless complex polypeptide 1A
, tailless complex polypeptide 1B
, cytosolic chaperonin containing t-complex polypeptide 1
, T-complex 1
, 65 kDa antigen
, t-complex 1
, t-complex 1 S homeolog
, T-complex protein 1 subunit alpha-like protein
, chaperonin-containing T-complex polypeptide alpha subunit
, T-complex protein 1 alpha subunit-like protein