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Merck

DR1041

Anti-TIP60 Rabbit pAb

liquid, Calbiochem®

Synonym(s):

Anti-HIV-1 Tat interactive protein, Anti-cPLA2-interaction protein

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About This Item

NACRES:
NA.43
UNSPSC Code:
12352203

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Product Name

Anti-TIP60 Rabbit pAb, liquid, Calbiochem®

biological source

rabbit

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

form

liquid

contains

≤0.1% sodium azide as preservative

species reactivity

human

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

dilution

(Immunoblotting (1:3000)
Immunoprecipitation (1:100))

isotype

IgG

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

100

Gene Information

human ... KAT5(10524)

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Anti-TIP60 Rabbit pAb liquid, Calbiochem®

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antibody form

serum

antibody form

purified antibody

antibody form

purified antibody

antibody form

serum

biological source

rabbit

biological source

rabbit

biological source

rabbit

biological source

rabbit

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

100

form

liquid

form

liquid

form

liquid

form

liquid

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

shipped in

wet ice

Gene Information

human ... KAT5(10524)

Gene Information

human ... TWIST1(7291)
mouse ... Twist1(22160)

Gene Information

human ... SPINK1(6690)

Gene Information

human ... UCHL1(7345)

Analysis Note

Positive Control
Saos-2 cells

Application


Immunoblotting (1:3000)
Immunoprecipitation (1:100)

Disclaimer

Toxicity: Standard Handling (A)

General description

Rabbit polyclonal antibody supplied as undiluted serum. Recognizes the ~60 kDa TIP60 protein.
Recognizes the ~60 kDa TIP60 protein in Saos-2 cells.
This Anti-TIP60 Rabbit pAb is validated for use in Immunoblotting, Immunoprecipitation for the detection of TIP60.

Immunogen

recombinant, human TIP60 protein

Other Notes

Murr, R., et al. 2006. Nat. Cell Biol.8, 91.
Sykes, S.M., et al. 2006. Mol. Cell24, 841.
Tang, Y., et al. 2006. Mol. Cell24, 827.
Frank, S.R., et al. 2003. EMBO Rep.6, 575.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class

10 - Combustible liquids

wgk

WGK 1

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Sokhna M S Yakhine-Diop et al.
Molecular neurobiology, 56(4), 2466-2481 (2018-07-23)
Parkinson's disease (PD) is a chronic and progressive neurodegenerative disorder. While most PD cases are idiopathic, the known genetic causes of PD are useful to understand common disease mechanisms. Recent data suggests that autophagy is regulated by protein acetylation mediated
Cheng Wang et al.
Communications biology, 3(1), 268-268 (2020-05-29)
Cisplatin and other platinum-based compounds are frequently used to treat breast cancer, but their utility is severely compromised by drug resistance. Many genes dictating drug responsiveness are subject to pre-mRNA alternative splicing which is regulated by key kinases such as
Ling-Jun Zhao et al.
Virology, 499, 178-184 (2016-09-25)
The adenovirus E1A 243R oncoprotein targets TRRAP, a scaffold protein that assembles histone acetyltransferase (HAT) complexes, such as the NuA4/Tip60 complex which mediates transcriptional activity of the proto-oncogene MYC and helps determine the cancer cell phenotype. How E1A transforms cells
Kristin A Krukenberg et al.
Cell reports, 8(6), 1808-1818 (2014-09-10)
Poly(ADP-ribose) polymerases (PARPs) catalyze poly(ADP-ribose) addition onto proteins, an important posttranslational modification involved in transcription, DNA damage repair, and stem cell identity. Previous studies established the activation of PARP1 in response to DNA damage, but little is known about PARP1
Yixin Dong et al.
Molecular and cellular biology, 37(19) (2017-07-12)
Global histone hyperacetylation is suggested to play a critical role for replacement of histones by transition proteins and protamines to compact the genome during spermiogenesis. However, the underlying mechanisms for hyperacetylation-mediated histone replacement remains poorly understood. Here, we report that
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