Recombinant Human ING3, GST-tagged
Cat.No. : | ING3-112H |
Product Overview : | Recombinant Human ING3 protein, fused to GST-tag, was expressed in E.coli and purified by GSH-sepharose. |
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Source : | E.coli |
Species : | Human |
Tag : | GST |
Protein length : | N-term-92aa |
Storage : | The protein is stored in PBS buffer at -20℃. Avoid repeated freezing and thawing cycles. |
Storage Buffer : | 1M PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH8. ) added with 100mM GSH and 1% Triton X-100,15%glycerol. |
Gene Name : | ING3 inhibitor of growth family, member 3 [ Homo sapiens ] |
Official Symbol : | ING3 |
Synonyms : | ING3; inhibitor of growth family, member 3; inhibitor of growth protein 3; Eaf4; FLJ20089; MEAF4; p47ING3; ING2; |
Gene ID : | 54556 |
mRNA Refseq : | NM_019071 |
Protein Refseq : | NP_061944 |
MIM : | 607493 |
UniProt ID : | Q9NXR8 |
Chromosome Location : | 7q31 |
Function : | contributes_to histone acetyltransferase activity; metal ion binding; methylated histone residue binding; zinc ion binding; |
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◆ Lysates | ||
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (7)
Ask a questionING3 recognizes histone H3 trimethylated at Lysine 4 (H3K4me3) through the Plant HomeoDomain (PHD) present at its C-terminal region.
The crystal structure of ING3’s PHD showed similarity to the PHD domains of its four homologs, suggesting a common structural motif among them.
ING3 facilitates acetylation of histones H2A and H4 by interacting with the NuA4-Tip60 MYST histone acetyltransferase complex.
The PHD of ING3 binds histone H3K4me3 with low-micromolar affinity, while its affinity for non-methylated histone is reduced by 54-fold.
The structural features explain the possible deleterious effects of ING3 mutations detected in tumors, which may disrupt its histone recognition and functional roles.
ING3 has been proposed to be an oncoprotein, suggesting its potential involvement in tumorigenesis.
The crystal structure of the N-terminal domain of ING3 revealed that it forms homodimers with an antiparallel coiled-coil fold.
Customer Reviews (3)
Write a reviewThe product’s unique attributes propelled our research to innovative heights.
Dependable protein-protein interaction outcomes were achieved due to the product's pure composition.
The product consistently met our expectations, reinforcing the credibility of our findings.
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