T5452
Anti-TTP (C-terminal) antibody produced in rabbit
~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution
别名:
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
产品名称
Anti-TTP (C-terminal) antibody produced in rabbit, ~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution
biological source
rabbit
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
Quality Level
Gene Information
human ... ZFP36(7538)
mouse ... Zfp36(22695)
rat ... Zfp36(79426)
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.
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.
General 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.
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.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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存储类别
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
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)
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
Tristetraprolin mediates radiation-induced TNF-α production in lung macrophages
Ray D, et al.
PLoS ONE, 8(2), e57290-e57290 (2013)
Posttranslational regulation of tristetraprolin subcellular localization and protein stability by p38 mitogen-activated protein kinase and extracellular signal-regulated kinase pathways
Brook M, et al.
Molecular and Cellular Biology, 26(6), 2408-2418 (2006)
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)
相关内容
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