Product: TIP60 Antibody
Catalog: BF0454
Description: Mouse monoclonal antibody to TIP60
Application: WB IHC ELISA
Reactivity: Human
Mol.Wt.: 60kDa; 59kD(Calculated).
Uniprot: Q92993
RRID: AB_2833604

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Product Info

Source:
Mouse
Application:
ELISA 1:10000, WB 1:500-1:2000, IHC 1:200-1:1000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human
Clonality:
Monoclonal [AFB1579]
Specificity:
TIP60 antibody detects endogenous levels of total TIP60.
RRID:
AB_2833604
Cite Format: Affinity Biosciences Cat# BF0454, RRID:AB_2833604.
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

60 kDa Tat interactive protein; 60 kDa Tat-interactive protein; cPLA(2) interacting protein; cPLA(2)-interacting protein; cPLA2; cPLA2 interacting protein; ESA1; Histone acetyltransferase HTATIP; Histone acetyltransferase KAT5; HIV 1 Tat interactive protein; HIV 1 Tat interactive protein, 60kDa; HIV-1 Tat interactive protein; HTATIP; HTATIP1; K(lysine) acetyltransferase 5; K-acetyltransferase 5; KAT5; KAT5_HUMAN; Lysine acetyltransferase 5; PLIP; Tat interacting protein, 60kDa; TIP; Tip60;

Immunogens

Immunogen:

Purified recombinant fragment of human TIP60 expressed in E. Coli.

Uniprot:
Gene(ID):
Description:
HTATIP (HIV-1 Tat interacting protein TIP60, about 60kDa) belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein. HATs play important roles in regulating chromatin remodeling, transcription and other nuclear processes by acetylating histone and nonhistone proteins. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure. There are five major variants of histone H2A: canonical H2A (most abundant), H2A.X, MacroH2A, H2ABbd and H2A.Z. Histone H2A.Z, the most conserved variant across species, functions as both a positive and negative regulator of transcription and is important for chromosome stability. Several homologous protein complexes, such as SWR-C, TIP60 and SRCAP (mammals), have been shown to catalyze the ATP-dependent exchange of H2A.Z for H2A in the nucleosome. This protein is a histone acetylase that has a role in DNA repair and apoptosis and is thought to play an important role in signal transduction.
Sequence:
MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVPASAQASGKTLPIPVQITLRFNLPKEREAIPGGEPDQPLSSSSCLQPNHRSTKRKVEVVSPATPVPSETAPASVFPQNGAARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMGLKSESGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDIVDGHERAMLKRLLRIDSKCLHFTPKDWSKRGKW

PTMs - Q92993 As Substrate

Site PTM Type Enzyme
K35 Ubiquitination
Y44 Phosphorylation
K52 Acetylation
S86 Phosphorylation P49841 (GSK3B) , P06493 (CDK1)
S90 Phosphorylation P06493 (CDK1) , P49841 (GSK3B)
K104 Acetylation
K120 Acetylation
K148 Acetylation
K150 Acetylation
S155 Phosphorylation
T158 Phosphorylation Q16539 (MAPK14)
K187 Acetylation
K189 Acetylation
S190 Phosphorylation
T195 Phosphorylation
S199 Phosphorylation
S202 Phosphorylation
S203 Phosphorylation
T227 Phosphorylation
K230 Ubiquitination
K274 Ubiquitination
T281 Phosphorylation
K282 Ubiquitination
Y294 Phosphorylation P00519 (ABL1)
K296 Ubiquitination
T298 Phosphorylation Q02156 (PRKCE)
S300 Phosphorylation Q02156 (PRKCE)
K310 Ubiquitination
K327 Acetylation
Y376 Phosphorylation
K404 Ubiquitination
K430 Sumoylation
S431 Phosphorylation
K451 Sumoylation
K451 Ubiquitination
Y472 Phosphorylation
K498 Ubiquitination
K505 Ubiquitination

Research Backgrounds

Function:

Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome. Also acetylates non-histone proteins, such as ATM, NR1D2, RAN, FOXP3, ULK1 and RUBCNL/Pacer. Directly acetylates and activates ATM. Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2. Promotes FOXP3 acetylation and positively regulates its transcriptional repressor activity. Acetylates RAN at 'Lys-134'. Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer.

PTMs:

(Microbial infection) In case of HIV-1 infection, interaction with the viral Tat protein leads to KAT5 polyubiquitination and targets it to degradation.

Sumoylated by UBE2I at Lys-430 and Lys-451, leading to increase of its histone acetyltransferase activity in UV-induced DNA damage response, as well as its translocation to nuclear bodies.

Ubiquitinated by MDM2, leading to its proteasome-dependent degradation.

Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase. The phosphorylated form has a higher histone acetyltransferase activity. Phosphorylation at Ser-86 by GSK3 (GSK3A or GSK3B) activates acetyltransferase activity. Phosphorylation at Ser-90 is a prerequisite for phosphorylation at Ser-86 by GSK3.

Autoacetylation at Lys-327 is required for proper function.

Subcellular Location:

Nucleus. Nucleus>Nucleolus. Cytoplasm>Perinuclear region.
Note: Upon stimulation with EDN1, it is exported from the nucleus to the perinuclear region and UV irradiation induces translocation into punctuate subnuclear structures named nuclear bodies.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT complex termed Piccolo NuA4. The NuA4 complex interacts with MYC. Interacts with ATM. Interacts with JADE1. Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7. Interacts with the cytoplasmic tail of APP and APBB1/FE65 (By similarity). Interacts with TRIM24 and TRIM68. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Identified in a complex with HINT1. Interacts with ATF2 and CUL3. Interacts with NR1D2 (via N-terminus). Component of a SWR1-like complex. Interacts with FOXP3. Interacts with ZBTB49.

(Microbial infection) Interacts with HIV-1 TAT.

Family&Domains:

Belongs to the MYST (SAS/MOZ) family.

Research Fields

· Human Diseases > Infectious diseases: Viral > HTLV-I infection.

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