MAP3K8 (Phospho-Ser400) Antibody

Description

Product Name MAP3K8 (Phospho-Ser400) 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 IHC
Species Reactivity Hu
Specificity The antibody detects endogenous levels of MAP3K8 only when phosphorylated at serine 400.
Immunogen Type Peptide-KLH
Immunogen Description Peptide sequence around phosphorylation site of Serine 400(C-Q-S(p)-L-D) derived from HumanMAP3K8.
Target Name MAP3K8
Modification Phospho-Ser400
Alternative Names C-COT;; M3K8; MAP3K8; TPL2;
Accession No. Swiss-Prot#: P41279;
NCBI Gene#: 1326;
NCBI Protein#: NP_001231063.1.
SDS-PAGE MW 52kd
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

Immunohistochemistry: 1:50~1:100

Images

Immunohistochemical analysis of paraffin-embedded human brain tissue using MAP3K8 (Phospho-Ser400) antibody #AB11739 (left)or the same antibody preincubated with blocking peptide (right).

Background

This gene was identified by its oncogenic transforming activity in cells. The encoded protein is a member of the serine/threonine protein kinase family. This kinase can activate both the MAP kinase and JNK kinase pathways. This kinase was shown to activate IkappaB kinases, and thus induce the nuclear production of NF-kappaB. This kinase was also found to promote the production of TNF-alpha and IL-2 during T lymphocyte activation. Studies of a similar gene in rat suggested the direct involvement of this kinase in the proteolysis of NF-kappaB1,p105 (NFKB1).

Miyoshi J., Mol. Cell. Biol. 11:4088-4096(1991).
Aoki M., J. Biol. Chem. 268:22723-22732(1993).
Chan A.M.,Oncogene 8:1329-1333(1993).

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