KAT6A Antibody (YA6622)(PBS only)
(Synonyms: Histone acetyltransferase KAT6A EC:2.3.1.48 MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3) Monocytic leukemia zinc finger protein Runt-related transcription factor-binding protein 2 Zinc finger protein 220 KAT6A MOZ MYST3 RUNXBP2 Histone acetyltransferase KAT6A EC:2.3.1.48 MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3) Monocytic leukemia zinc finger protein Runt-related transcription factor-binding protein 2 Zinc finger protein 220 KAT6A MOZ MYST3 RUNXBP2 ZNF220 )KAT6A Antibody (YA6622)(PBS only)is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to KAT6A.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, ICC/IF, IHC-P, FC, ChIP
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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FC
FC: Flow Cytometry
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ChIP
ChIP: Chromatin Immunoprecipitation
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|---|---|---|---|---|---|
| Dilution Ratio | 1:2000 | 1:500 | 1:2000-1:20000 | 1:200-1:1000 | Use 5 μg for 25 μg of chromatin. |
Product Details
KAT6A Antibody (YA6622)(PBS only)is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to KAT6A.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Calculated Molecular Weight Predicted band size: 225 kDa
Recombinant protein within human KAT6A aa 785-1,034.
affinity purified.
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
KAT6A is a Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML. May play a role in leukemogenic gene transcription[1][2][3][4][5].
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Subcellular Localization
Nucleus; Nucleus, nucleolus; Nucleus, nucleoplasm; Nucleus, PML body
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Expression
PositiveControl: Huh7, human liver tissue, human placenta tissue, mouse liver tissue, mouse placenta tissue, rat liver tissue. -
Isoforms & Post-Translational Modification
KAT6A has an amino acid length of 2004, molecular weight is 225028 Da.
Autoacetylated; autoacetylation at Lys-604 is required for proper function. Acetylation at Lys-1007 and Lys-1014 is required for the interaction with MLLT1/ENL and MLLT3/AF9. -
Subunit
Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3.
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SwissProt ID
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Synonyms
Histone acetyltransferase KAT6A EC:2.3.1.48 MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3) Monocytic leukemia zinc finger protein Runt-related transcription factor-binding protein 2 Zinc finger protein 220 KAT6A MOZ MYST3 RUNXBP2 Histone acetyltransferase KAT6A EC:2.3.1.48 MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3 (MYST-3) Monocytic leukemia zinc finger protein Runt-related transcription factor-binding protein 2 Zinc finger protein 220 KAT6A MOZ MYST3 RUNXBP2 ZNF220
Documentation
References
[1]. Kitabayashi I, et al. Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein. EMBO J. 2001 Dec 17;20(24):7184-96. [Content Brief]
[2]. Pelletier N, et al. MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2. Oncogene. 2002 Apr 18;21(17):2729-40. [Content Brief]
[3]. Bristow CA, et al. Transcriptional regulation of the human MIP-1alpha promoter by RUNX1 and MOZ. Nucleic Acids Res. 2003 Jun 1;31(11):2735-44. [Content Brief]
[4]. Rokudai S, et al. MOZ increases p53 acetylation and premature senescence through its complex formation with PML. Proc Natl Acad Sci U S A. 2013 Mar 5;110(10):3895-900. [Content Brief]
[5]. Becht DC, et al. A multivalent engagement of ENL with MOZ. Nat Struct Mol Biol. 2025 Apr;32(4):709-718. [Content Brief]