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Results for "

Tip60

" in MedChemExpress (MCE) Product Catalog:

4

Inhibitors & Agonists

3

Recombinant Proteins

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Cat. No. Compare Product Name Species Source
  • HY-P71707
    KAT5 Protein, Human (His)

    60kDa Tat interactive protein; cPLA2 interacting protein; ESA1; Histone acetyltransferase HTATip; HTATip1; K(lysine) acetyltransferase 5; PLIP; Tat interacting protein, 60kDa; Tip; Tip60

    		 Human E. coli
    The KAT5 protein is the catalytic subunit of the NuA4 histone acetyltransferase complex and activates gene transcription through histone acetylation. KAT5 Protein, Human (His) is the recombinant human-derived KAT5 protein, expressed by E. coli , with N-6*His labeled tag. The total length of KAT5 Protein, Human (His) is 511 a.a., with molecular weight of ~62.4 kDa.
  • HY-P71661
    RUVBL2 Protein, Human (His-SUMO)

    48kDa TATA box-binding protein-interacting protein; CGI-46; TIH2; Tip48; Tip49b; Tip60-associated protein 54-beta; wu:fi25f01; zreptin

    		 Human E. coli
    The RUVBL2 protein has DNA-stimulated ATPase and DNA helicase activities and can hexamerize for ATP hydrolysis. As a member of the NuA4 complex, RUVBL2 contributes to histone acetylation, altering nucleosome-DNA interactions to activate genes. RUVBL2 Protein, Human (His-SUMO) is the recombinant human-derived RUVBL2 protein, expressed by E. coli , with N-SUMO, N-6*His labeled tag. The total length of RUVBL2 Protein, Human (His-SUMO) is 462 a.a., with molecular weight of ~67.0 kDa.
  • HY-P701625
    MYST1 Protein, Human

    KAT8; Histone acetyltransferase KAT8; Lysine acetyltransferase 8; MOZ; YBF2/SAS3; SAS2 and Tip60 protein 1; MYST-1; hMOF

    		 Human E. coli
    The MYST1 protein is a histone acetyltransferase associated with transcriptional activation and potential regulation of gene expression. In addition to transcription, MYST1 may also affect ATM function. MYST1 Protein, Human is the recombinant human-derived MYST1 protein, expressed by E. coli , with tag free. The total length of MYST1 Protein, Human is 458 a.a., .

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