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CCT7 encodes a molecular chaperone that is a member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC).
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Human Polyclonal CCT7 Primary Antibody für WB - ABIN1881183
Mukherjee, Conway de Macario, Macario, Brocchieri: Chaperonin genes on the rise: new divergent classes and intense duplication in human and other vertebrate genomes. in BMC evolutionary biology 2010
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Cow (Bovine) Monoclonal CCT7 Primary Antibody für IHC (p), WB - ABIN2477954
Hynes, Celis, Lewis, Carne, U, Lauridsen, Willison: Analysis of chaperonin-containing TCP-1 subunits in the human keratinocyte two-dimensional protein database: further characterisation of antibodies to individual subunits. in Electrophoresis 1997
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Human Polyclonal CCT7 Primary Antibody für ICC, IF - ABIN4358161
Erdmann, Stark, Esslinger, Rumpf, Koesling, de Wit, Kaiser, Braunholz, Medack, Fischer, Zimmermann, Tennstedt, Graf, Eck, Aherrahrou, Nahrstaedt, Willenborg, Bruse, Brænne, Nöthen, Hofmann, Braund et al.: Dysfunctional nitric oxide signalling increases risk of myocardial infarction. ... in Nature 2013
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Human Monoclonal CCT7 Primary Antibody für ELISA, WB - ABIN564614
Freund, Zhong, Venteicher, Meng, Veenstra, Frydman, Artandi: Proteostatic control of telomerase function through TRiC-mediated folding of TCAB1. in Cell 2014
Human Monoclonal CCT7 Primary Antibody für ELISA, WB - ABIN524002
Machida, Masutani, Kobayashi, Mikami, Nishino, Miyazawa, Imataka: Reconstitution of the human chaperonin CCT by co-expression of the eight distinct subunits in mammalian cells. in Protein expression and purification 2012
the increased expression of CCT-eta appears to be a marker for latent and active Dupuytren's contracture and to be essential for the increased contractility exhibited by these fibroblasts
Functional characterization of the CCT complex and its subunits in mouse.
A protein in mouse, that is highly similar to the one described in this record, was found to interact with a protein involved in the Nitric oxide (NO) signal transduction pathway, soluble guanylyl cyclase (sGC).
CCTeta is a novel soluble guanylyl cyclase-interacting protein [CCTeta]
CCT-eta is a specific regulator of fibroblast motility and contractility and may be a key determinant of the scarless wound healing phenotype by means of its specific regulation of alpha-SMA (zeige SMN1 Antikörper) expression
CCT-eta mRNA remains persistently elevated in healing adult wounds for 28 days following injury.
This gene encodes 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. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 5 and 6.
chaperonin containing TCP1, subunit 7
, chaperonin subunit 7 (eta)
, chaperonin containing TCP1, subunit 7 (eta)
, chaperonin containing TCP1, subunit 7-like
, T-complex protein 1 subunit eta-like
, HIV-1 Nef interacting protein
, HIV-1 Nef-interacting protein
, T-complex protein 1 subunit eta
, chaperonin containing t-complex polypeptide 1, eta subunit
, chaperonin containing t-complex subunit eta
, subunit 7
, chaperonin-containing TCP-1 subunit eta