T-Complex 1 Proteins (TCP1)

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 Antibodies (232) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
TCP1 21455  
TCP1 6950 P17987
TCP1 24818 P28480
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Top T-Complex 1 Proteins at antibodies-online.com

Showing 10 out of 12 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
Insect Cells Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 60 Days
Insect Cells Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 60 Days
HOST_Escherichia coli (E. coli) Human His tag 50 μg Log in to see 15 to 19 Days
HOST_Wheat germ Human GST tag 10 μg Log in to see 11 to 12 Days
HOST_HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Log in to see 10 to 12 Days
Yeast Mesocricetus auratus His tag   1 mg Log in to see 60 to 71 Days
Yeast Rat His tag   1 mg Log in to see 60 to 71 Days
HOST_Escherichia coli (E. coli) Human Un-conjugated   50 μg Log in to see 2 to 3 Days
HOST_Escherichia coli (E. coli) Human His tag   1 mg Log in to see 2 to 3 Days
Human Un-conjugated   2 μg Log in to see 6 Days

TCP1 Proteins by Origin and Source

Origin Expressed in Conjugate
Mouse (Murine)

Human , , ,
, ,
Rat (Rattus)

Top referenced T-Complex 1 Proteins

  1. Human TCP1 Protein expressed in Escherichia coli (E. coli) - ABIN667253 : Yokota, Yanagi, Yura, Kubota: Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle. in European journal of biochemistry / FEBS 2001 (PubMed)
    Show all 2 references for 667253

  2. Human TCP1 Protein expressed in Wheat germ - ABIN1322407 : Hirai, Maeda, Omori, Yamamoto, Kokeguchi, Takashiba: Serum antibody response to group II chaperonin from Methanobrevibacter oralis and human chaperonin CCT. in Pathogens and disease 2013 (PubMed)

More Proteins for T-Complex 1 (TCP1) Interaction Partners

Mouse (Murine) T-Complex 1 (TCP1) interaction partners

  1. this study shows that CCTalpha (show PCYT1A Proteins) is required for antigen-specific, germinal center-derived memory B cells

  2. Data show that T-complex protein 1 (TCP-1) may be a crucial downstream mo (show P2RX7 Proteins)lecule (show P2RX7 Proteins)of purinergic receptor P2X 7 (P2X7R) and plays a role in lymphoid neoplasm metastasis.

  3. The data presented here reveal an additional level of interplay between CCT (show FLVCR2 Proteins) and actin mediated via gelsolin (show GSN Proteins), suggesting that CCT (show FLVCR2 Proteins) may influence processes depending on gelsolin (show GSN Proteins) activity, such as cell motility.

  4. Host CCTalpha (show PCYT1A Proteins) is required for efficient transcription and replication of rabies virus.

  5. Our data provide new evidence indicating the essential role of the chaperonin CCT in the biogenesis of vertebrate photoreceptor sensory cilia

  6. 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.

  7. Normal CCT function is ultimately required for the morphogenesis and survival of sensory neurons of the retina.

  8. TRiC (show MARVELD2 Proteins)-peptide complexes of the heat shock protein 60 (show HSPD1 Proteins) family are efficient vehicles of cross-presentation in assays in vitro and in mice in vivo; immunization with TRiC (show MARVELD2 Proteins) purified from a tumor elicits specific protection against a challenge with that tumor.

  9. downregulated expression in T cells following treatment with bis (show BAG3 Proteins)(tri (show VANGL2 Proteins)-n-butylin)oxide (TBTO), an immunotoxic organotin

  10. 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

Human T-Complex 1 (TCP1) interaction partners

  1. Result suggest the positive correlation between purinergic receptor P2X 7 (show P2RX7 Proteins) (P2X7R (show P2RX7 Proteins)) and T-complex protein 1 (TCP-1) in lymphoma patients.

  2. Data suggest that biosynthesis and folding of leukemogenic fusion oncoprotein AML1 (show RUNX1 Proteins)-ETO (show RUNX1T1 Proteins)/RUNX1 (show RUNX1 Proteins)-RUNX1T1 (show RUNX1T1 Proteins) is facilitated by interaction with the chaperonin (show HSPD1 Proteins) TRiC/CCT1/TCP1 and HSP70 (heat shock protein 70 (show HSP70 Proteins)).

  3. Changes for CRMP2 (show DPYSL2 Proteins), TCP1epsilon, TPM2 (show TPM2 Proteins) and 14-3-3gamma (show YWHAG Proteins) were confirmed in experimental tumors and in a series of 28 human SI-NETs.

  4. A role for the TRiC (show MARVELD2 Proteins) subunits TCP1 and CCT2 (show CCT2 Proteins), and potentially the entire TRiC (show MARVELD2 Proteins) complex, in breast cancer.

  5. CCT8 (show CCT8 Proteins) might be an oncogene (show RAB1A Proteins) and participate in HCC (show FAM126A Proteins) cell proliferation.

  6. identified 6 of the 8 components of the chaperonin-containing TCP-1 (show CCT6A Proteins) (CCT) complex bound to LOX-1 (show OLR1 Proteins) cytoplasmic domain

  7. Data suggest that specific molecular mediators involved in glucocerebrosidase (show GBA Proteins) maturation and degradation, and abnormal interaction with TCP1 and c-Cbl (show CBL Proteins), could be responsible for phenotypic variation among patients with the same genotypes.

  8. Expression patterns of chaperone proteins in cerebral cortex of the fetus with Down syndrome: dysregulation of T-complex protein 1 (show CCT3 Proteins).

  9. TRiC (show MARVELD2 Proteins) chaperonin (show HSPD1 Proteins) binds to HIF prolyl hydroxylase PHD3 (show EGLN3 Proteins)

  10. the strong inhibitory action of PhLP (show PDCL Proteins)(S) on Gbetagamma signaling is the result of a previously unrecognized mechanism of Gbetagamma-regulation, inhibition of Gbetagamma-folding by interference with TCP-1alpha

Cow (Bovine) T-Complex 1 (TCP1) interaction partners

  1. The mammalian TRiC structure was determined at 4.7-A resolution.

  2. Results indicate that the kinetic mechanism of the allosteric transitions of chaperonin (show HSPD1 Proteins) containing t-complex polypeptide 1 (TCP-1) differs considerably from that of GroEL (show GroEL Proteins)

  3. unlike GroEL (show GroEL Proteins), TRiC does not close its lid upon nucleotide binding, but instead responds to the trigonal-bipyramidal transition state of ATP hydrolysis.

  4. Data show that chaperonin (show HSPD1 Proteins) TRiC binding is specified by two short hydrophobic beta strands in the von Hippel-Lindau protein (show VHLL Proteins) that, upon folding, become buried within the native structure [TRiC].

  5. antagonistic actions of PhLP3 and prefoldin serve to modulate CCT activity and play a key role in establishing a functional cytoskeleton in vivo

  6. one of the cytosolic chaperonin containing t-complex polypeptide 1 (CCT)/TRiC-specific targets is hydrophobic beta-strands, which are highly prone to aggregation

  7. Domain movements in TRiC are coordinated through unique interdomain contacts within each subunit and, further, these contacts are absent in prokaryotic chaperonins.

  8. analysis of the formation of a stable complex between chaperonin-containing TCP-1 (show CCT6A Proteins) (CCT) and Hsc70 (show HSPA8 Proteins)

T-Complex 1 (TCP1) Protein Profile

Protein Summary

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.

Gene names and symbols associated with T-Complex 1 Proteins (TCP1)

  • Tcp1-like (T-cp1)
  • t-complex protein 1, pseudogene 1 (Tcp1-ps1)
  • Protein CCT-1 (cct-1)
  • t-complex 1 (TCP1)
  • t-complex 1 (Tcp1)
  • t-complex protein 1 (Tcp1)
  • AI528772 protein
  • BEST:GH05123 protein
  • c-cpn protein
  • CCT protein
  • CCT-alpha protein
  • Cct1 protein
  • Cct1-1P protein
  • Ccta protein
  • CCTalpha protein
  • CG5374 protein
  • D6S230E protein
  • Dmel\\CG5374 protein
  • gh05123 protein
  • p63 protein
  • T-cpl protein
  • Tcp-1 protein
  • TCP-1-alpha protein
  • TCP-1alpha protein
  • Tcp1 protein
  • Tcp1-alpha protein
  • TCPA_DROME protein
  • Tp63 protein
  • TRic protein

Protein level used designations for T-Complex 1 Proteins (TCP1)

CG5374-PA , CG5374-PB , T-complex 1 , T-cp1-PA , T-cp1-PB , T-complex protein 1 subunit alpha , T-complex protein 1, alpha subunit , tailless complex polypeptide 1 , CCT-alpha , TCP-1-alpha , cytosolic chaperonin containing t-complex polypeptide 1 , T-complex protein 1 subunit alpha A , T-complex protein 1 subunit alpha B , TCP-1-A , TCP-1-B , t-complex polypeptide 1 , tailless complex polypeptide 1A , tailless complex polypeptide 1B , 65 kDa antigen , t-complex 1

42649 Drosophila melanogaster
21455 Mus musculus
174318 Caenorhabditis elegans
6950 Homo sapiens
512043 Bos taurus
24818 Rattus norvegicus
21454 Mus musculus
100689476 Cricetulus griseus
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