Recombinant Human ZNHIT3 protein (denatured) (His tag N-Terminus)
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Recombinant Human ZNHIT3 protein (denatured) (His tag N-Terminus) is a Human Full Length protein, in the 1 to 155 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
View Alternative Names
TRIP3, ZNHIT3, Zinc finger HIT domain-containing protein 3, HNF-4a coactivator, Thyroid hormone receptor interactor 3, Thyroid receptor-interacting protein 3, TR-interacting protein 3, TRIP-3
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human ZNHIT3 protein (denatured) (His tag N-Terminus) (AB171718)
15% SDS-PAGE analysis of ab171718 (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
ZNHIT3 functions as a critical component of several cellular complexes including the chromatin remodeling complexes. These complexes modulate the structure of chromatin thereby regulating gene expression. ZNHIT3 contributes to the maintenance of chromatin state impacting transcriptional activity. Its interaction with other proteins in these complexes highlights its role in gene regulatory mechanisms. Due to its involvement in chromatin dynamics ZNHIT3 is essential in managing both normal cellular proliferation and differentiation.
Pathways
ZNHIT3 participates in pathways related to chromosomal architecture and gene expression regulation including the chromatin modification and transcription regulation pathways. It associates with notable proteins such as BRG1 and SMARCA4 within these pathways. These interactions facilitate remodeling of nucleosome structures influencing accessibility to transcription factors and transcription machinery ensuring proper expression of genetic information.
Specifications
Form
Liquid
Additional notes
ab171718 was purified by anion-exchange and gel-filtration chromatography techniques.
General info
Subcellular localisation
Nucleus
Target data
Product promise
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