Anti-CCT4 monoclonal antibody, clone FQS9505(C)

Name: Anti-CCT4 monoclonal antibody, clone FQS9505(C)
SKU: DCABH-2163
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Rabbit anti-Human CCT4 monoclonal antibody for WB

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COA

SDS

Datasheet

Summary

Specifications

Antibody Isotype

IgG

Clone

FQS9505(C)

Species Reactivity

Rat; Human

Immunogen

Synthetic peptide corresponding to N-terminal amino acids of Human TCP1 delta.

Conjugate

Unconjugated

Applications

Application Notes

WB: 1/1000 - 1/10000.

Target

Alternative Names

CCT4; chaperonin containing TCP1, subunit 4 (delta); T-complex protein 1 subunit delta; Cctd; TCP-1-delta; stimulator of TAR RNA-binding; chaperonin containing t-complex polypeptide 1, delta subunit; SRB; CCT-DELTA; MGC126164; MGC126165;

Entrez Gene ID

10575

UniProt ID

P50991

Product Background

Antigen Description

The chaperonin containing TCP1 complex (CCT), also called the TCP1 ring complex, consists of 2 back to back rings, each containing 8 unique but homologous subunits (e.g. CCT3). CCT assists the folding of newly translated polypeptide substrates through multiple rounds of ATP driven release and rebinding of partially folded intermediate forms. Substrates of CCT include the cytoskeletal proteins actin and tubulin, as well as alpha transducin. TCP1 delta belongs to the TCP1 chaperonin family, and is a molecular chaperone; assisting the folding of proteins upon ATP hydrolysis. It is known to play a role, in vitro, in the folding of actin and tubulin.

Pathway

Association of TriC/CCT with target proteins during biosynthesis, organism-specific biosystem; Chaperonin-mediated protein folding, organism-specific biosystem; Cooperation of Prefoldin and TriC/CCTin actin and tubulin folding, organism-specific biosystem; Folding of actin by CCT/TriC, organism-specific biosystem; Formation of tubulin folding intermediates by CCT/TriC, organism-specific biosystem; Metabolism of proteins, organism-specific biosystem; Prefoldin mediated transfer of substrateto CCT/TriC, organism-specific biosystem;

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Serum antibody response to group II chaperonin from Methanobrevibacter oralis and human chaperonin CCT

PATHOGENS AND DISEASE

Authors: Hirai, Kimito; Maeda, Hiroshi; Omori, Kazuhiro; Yamamoto, Tadashi; Kokeguchi, Susumu; Takashiba, Shogo

Abstract

Both group I (HSP60) and group II (CCT) chaperonins are targets of autoantibodies. Autoimmune reactions to HSP60 have been well characterized, while immune reactions to group II chaperonin have not been clarified. Methanobrevibacter oralis is a suspected periodontal pathogen with group II chaperonin. In this study, serum responses to M.oralis chaperonin, human HSP60, and CCT subunits were examined using sera from patients with periodontitis and autoimmune diseases. In comparison with healthy controls, periodontitis patients showed significantly higher responses to CCT4 and CCT8 on dot blot analysis. Signals for CCT3 and CCT8 in autoimmune disease patients were significantly higher than in controls. Significant differences were also demonstrated by Western blotting in anti-CCT4 response in both patient groups. All subjects showed strong reactivity to M.oralis chaperonin and faint signals to human HSP60. Autoantibodies were raised against CCT rather than HSP60; and CCT3, CCT4, and CCT8 were shown to be the main targets. Host immune systems may be frequently exposed to chaperonins of Archaea in various habitats. Although further studies of the cross-reactivity between M.oralis chaperonin and human CCT are required, anti-CCT autoantibodies may be involved in the pathogenesis of periodontitis and autoimmune diseases.

ATP-induced allostery in the eukaryotic chaperonin CCT is abolished by the mutation G345D in CCT4 that renders yeast temperature-sensitive for growth

JOURNAL OF MOLECULAR BIOLOGY

Authors: Shimon, Liat; Hynes, Gillian M.; McCormack, Elizabeth A.; Willison, Keith R.; Horovitz, Amnon

Abstract

Saccharomyces cerevisiae yeast cells containing the chaperonin CCT (chaperonin-containing t-complex polypeptide 1 (TCP-1)) with the G345D mutation in subunit CCT4 (anc2-1) are temperature-sensitive for growth and display defects in organization of actin structure, budding and cell shape. In this first structure-function analysis of CCT, we show that this mutation abolishes both intra- and inter-ring cooperativity in ATP binding by CCT. The finding that a single mutation in only one subunit in each CCT ring has such drastic effects highlights the importance of allostery for its in vivo function. These results, together with other kinetic data for wild-type CCT reported in this study, provide support for the sequential model for ATP-dependent allosteric transitions in CCT. (C) 2008 Elsevier Ltd. All rights reserved.