Recombinant Rat ING3 Protein, His (Fc)-Avi-tagged

• Cat.No.: ING3-2719R
• Product Overview: Recombinant Rat ING3 with His (Fc)-Avi tag was expressed and purified

Specification

• Source: HEK293
• Species: Rat
• Tag: His (Fc)-Avi
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Purity: ≥85% by SDS-PAGE
• Stability: Stable for at least 6 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
• Storage: For long term storage, aliquot and store at -20 to -80 centigrade. Avoid repeated freezing and thawing cycles.
• Storage Buffer: PBS buffer

Gene Information

• Gene Name: Ing3 inhibitor of growth family, member 3 [ Rattus norvegicus ]
• Official Symbol: ING3
• Gene ID: 312154
• mRNA Refseq: NM_001034107.1
• Protein Refseq: NP_001029279.1
• UniProt ID: Q498T3

Reviews

05/15/2022

 The product’s unique attributes propelled our research to innovative heights.

09/08/2020

Dependable protein-protein interaction outcomes were achieved due to the product's pure composition.

09/16/2018

 The product consistently met our expectations, reinforcing the credibility of our findings.

Q&As

What specific modification does ING3 recognize on histones, and where is this recognition mediated?

ING3 recognizes histone H3 trimethylated at Lysine 4 (H3K4me3) through the Plant HomeoDomain (PHD) present at its C-terminal region.

What structural similarity was observed between ING3’s PHD and that of its homologs?

The crystal structure of ING3’s PHD showed similarity to the PHD domains of its four homologs, suggesting a common structural motif among them.

What enzymatic activity does ING3 facilitate regarding histones H2A and H4?

ING3 facilitates acetylation of histones H2A and H4 by interacting with the NuA4-Tip60 MYST histone acetyltransferase complex.

How does the PHD of ING3 interact with histone H3K4me3?

The PHD of ING3 binds histone H3K4me3 with low-micromolar affinity, while its affinity for non-methylated histone is reduced by 54-fold.

What insights do these structural features provide regarding ING3 mutations in tumors?

The structural features explain the possible deleterious effects of ING3 mutations detected in tumors, which may disrupt its histone recognition and functional roles.

How has ING3 been characterized in relation to cancer?

ING3 has been proposed to be an oncoprotein, suggesting its potential involvement in tumorigenesis.

What structural features were observed in the crystal structure of ING3’s N-terminal domain?

The crystal structure of the N-terminal domain of ING3 revealed that it forms homodimers with an antiparallel coiled-coil fold.