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T5452

Sigma-Aldrich

Anti-TTP (C-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-G0/G1 switch regulatory protein 24, Anti-GOS24, Anti-Growth factor-inducible nuclear protein NUP475, Anti-NUP475, Anti-RNF162A, Anti-TIS11, Anti-Tristetraprolin, Anti-Zfp36, Zinc finger protein 36 homolog Protein

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~50 kDa

species reactivity

human

concentration

~1.0 mg/mL

technique(s)

western blot: 0.5-1.0 μg/mL using lysates of HEK-293 cells overexpressing human TTP

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ZFP36(7538)
mouse ... Zfp36(22695)
rat ... Zfp36(79426)

General description

TTP is also known as Tristetraproline, Zfp-36, TIS11A, and Growth factor-inducible nuclear protein NUP475. TTP belongs to a family of human ARE (AU-rich element found in 3′ UTR mRNA) binding protein that contains tandem CCCH zinc finger RNA-binding domains required for interaction with ARE. TTP is a phosphoprotein. Anti-TTP (C-terminal) is produced in rabbit using as immunogen a synthetic peptide corresponding to human TTP conjugated to KLH.

Immunogen

synthetic peptide corresponding to amino acids 270-284 of human TTP conjugated to KLH. The corresponding sequence differs by one amino acid in mouse and rat.

Application

Anti-TTP (C-terminal) antibody has been used in immunoprecipitationand may be used for immunoblotting.

Biochem/physiol Actions

Tristetraprolin (TTP) is an RNA-binding protein that suppresses inflammation by accelerating the degradation of cytokine mRNA. TTP plays a role in both mRNA deadenylation and 3′ to 5′ degradation of the mRNA and helps in recruiting several factors involved in these processes. TTP acts as a substrate for multiple kinases like ERK (extracellular signal-regulated kinases), JNK (Jun N-terminal kinase) , p38, and MAPKAPK2.

Target description

TTP (C-terminal) (also known as Tristetraproline, Zfp-36, TIS11A, and Growth factor-inducible nuclear protein NUP475) is an RNA-binding protein that suppresses inflammation by accelerating the degradation of cytokine mRNA.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Tristetraprolin mediates radiation-induced TNF-α production in lung macrophages
Ray D, et al.
PLoS ONE, 8(2), e57290-e57290 (2013)
Dipankar Ray et al.
PloS one, 8(2), e57290-e57290 (2013-03-08)
The efficacy of radiation therapy for lung cancer is limited by radiation-induced lung toxicity (RILT). Although tumor necrosis factor-alpha (TNF-α) signaling plays a critical role in RILT, the molecular regulators of radiation-induced TNF-α production remain unknown. We investigated the role
Interactions of CCCH zinc finger proteins with mRNA non-binding tristetraprolin mutants exert an inhibitory effect on degradation of AU-rich element-containing mRNAs
Lai W S, et al.
The Journal of biological chemistry, 277(11), 9606-9613 (2002)
Roles of Tristetraprolin in tumorigenesis
Park J M, et al.
International Journal of Molecular Sciences, 19(11), 3384-3384 (2018)
Structure/function analysis of tristetraprolin (TTP): p38 stress-activated protein kinase and lipopolysaccharide stimulation do not alter TTP function
Rigby W F, et al.
Journal of immunology (Baltimore, Md. : 1950), 174(12), 7883-7893 (2005)

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