NF-κB p100 (Phospho-Ser872) Antibody

Description

Product Name NF-κB p100 (Phospho-Ser872) Antibody
Host Species Rabbit
Clonality Polyclonal
Purification Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
Applications WB
Species Reactivity Hu Ms Rt
Specificity The antibody detects endogenous level of NF-κB p100 only when phosphorylated at serine 872.
Immunogen Type Peptide-KLH
Immunogen Description Peptide sequence around phosphorylation site of serine872(S-Q-S(p)-V-E) derived from Human NF-κB p100 .
Target Name NF-κB p100
Modification Phospho-Ser872
Alternative Names DNA-binding factor KBF2; Lymphocyte translocation chromosome 10; Lyt10; Nuclear factor NF-kappa-B p100 subunit; Oncogene Lyt-10
Accession No. Swiss-Prot#: Q00653;
NCBI Gene#: 4791;
NCBI Protein#: NP_001070962.1
SDS-PAGE MW 100kd
Concentration 1.0mg/ml
Formulation Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Storage Store at -20˚C/1 year

Application Details

Western blotting: 1:500~1:1000

Images

Western blot analysis of extracts from RAW264.7 cells treated with EGF using Phospho-NF-κB p100 (Ser872) antibody #AB11919.The lane on the right is treated with the antigen-specific peptide.

Background

NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity.

Qu Z, Qing G, Rabson A, Xiao G (2004) J Biol Chem 279, 44563-72 . Xiao G, Fong A, Sun SC (2004) J Biol Chem 279, 30099-105 .

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