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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). Additionally we are shipping T-Complex 1 Proteins (10) and many more products for this protein.
Showing 10 out of 250 products:
Human Polyclonal TCP1 Primary Antibody for IHC (p), IHC - ABIN250182
Yaffe, Farr, Miklos, Horwich, Sternlicht, Sternlicht: TCP1 complex is a molecular chaperone in tubulin biogenesis. in Nature 1992
Human Monoclonal TCP1 Primary Antibody for 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
this study shows that CCTalpha (show PCYT1A Antibodies) 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 (show P2RX7 Antibodies)lecule (show P2RX7 Antibodies)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 (show FLVCR2 Antibodies) and actin mediated via gelsolin (show GSN Antibodies), suggesting that CCT (show FLVCR2 Antibodies) may influence processes depending on gelsolin (show GSN Antibodies) activity, such as cell motility.
Host CCTalpha (show PCYT1A Antibodies) 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 (show MARVELD2 Antibodies)-peptide complexes of the heat shock protein 60 (show HSPD1 Antibodies) family are efficient vehicles of cross-presentation in assays in vitro and in mice in vivo; immunization with TRiC (show MARVELD2 Antibodies) purified from a tumor elicits specific protection against a challenge with that tumor.
downregulated expression in T cells following treatment with bis (show BAG3 Antibodies)(tri (show VANGL2 Antibodies)-n-butylin)oxide (TBTO), an immunotoxic organotin
cellular distribution of CCT during spermatogenesis; in the cytoplasm,it associates to the microtubule organizing center and the manchette; in the nucleus, it concentrates at highly condensed chromatin regions
Result suggest the positive correlation between purinergic receptor P2X 7 (show P2RX7 Antibodies) (P2X7R (show P2RX7 Antibodies)) and T-complex protein 1 (TCP-1) in lymphoma patients.
Data suggest that biosynthesis and folding of leukemogenic fusion oncoprotein AML1 (show RUNX1 Antibodies)-ETO (show RUNX1T1 Antibodies)/RUNX1 (show RUNX1 Antibodies)-RUNX1T1 (show RUNX1T1 Antibodies) is facilitated by interaction with the chaperonin (show HSPD1 Antibodies) TRiC/CCT1/TCP1 and HSP70 (heat shock protein 70 (show HSP70 Antibodies)).
Changes for CRMP2 (show DPYSL2 Antibodies), TCP1epsilon, TPM2 (show TPM2 Antibodies) and 14-3-3gamma (show YWHAG Antibodies) were confirmed in experimental tumors and in a series of 28 human SI-NETs.
A role for the TRiC (show MARVELD2 Antibodies) subunits TCP1 and CCT2 (show CCT2 Antibodies), and potentially the entire TRiC (show MARVELD2 Antibodies) complex, in breast cancer.
CCT8 (show CCT8 Antibodies) might be an oncogene (show RAB1A Antibodies) and participate in HCC (show FAM126A Antibodies) cell proliferation.
identified 6 of the 8 components of the chaperonin-containing TCP-1 (show CCT6A Antibodies) (CCT) complex bound to LOX-1 (show OLR1 Antibodies) cytoplasmic domain
Data suggest that specific molecular mediators involved in glucocerebrosidase (show GBA Antibodies) maturation and degradation, and abnormal interaction with TCP1 and c-Cbl (show CBL Antibodies), 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 (show CCT3 Antibodies).
TRiC (show MARVELD2 Antibodies) chaperonin (show HSPD1 Antibodies) binds to HIF prolyl hydroxylase PHD3 (show EGLN3 Antibodies)
the strong inhibitory action of PhLP (show PDCL Antibodies)(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 (show HSPD1 Antibodies) containing t-complex polypeptide 1 (TCP-1) differs considerably from that of GroEL (show GroEL Antibodies)
unlike GroEL (show GroEL Antibodies), 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 (show HSPD1 Antibodies) TRiC binding is specified by two short hydrophobic beta strands in the von Hippel-Lindau protein (show VHLL Antibodies) 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 (show CCT6A Antibodies) (CCT) and Hsc70 (show HSPA8 Antibodies)
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 1
, T-complex protein 1 subunit alpha
, T-complex protein 1, alpha subunit
, tailless complex polypeptide 1
, cytosolic chaperonin containing t-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
, 65 kDa antigen
, t-complex 1