biological source
rabbit
conjugate
unconjugated
antibody form
whole antiserum
antibody product type
primary antibodies
clone
polyclonal
mol wt
antigen, JNK1 46 kDa, antigen, JNK2 55 kDa
contains
15 mM sodium azide
species reactivity
rat, human, mouse
technique(s)
microarray: suitable, western blot: 1:16,000 using rat brain extract and mouse NIH-3T3 fibroblast extract, respectively, western blot: 1:2,000 using mouse NIH 3T3 fibroblast cell lysate
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... MAPK8(5599)
mouse ... Mapk8(26419)
rat ... Mapk8(116554)
General description
Anti-c-Jun N-Terminal Kinase (JNK1, JNK2) is developed in rabbit using a synthetic peptide, corresponding to amino acids of human c-Jun N-terminal kinase 1 (JNK1), coupled to KLH as the immunogen.
JNK (c-Jun N terminal protein kinase, also known as stress activated protein kinase, SAPK1) is a protein that belongs to serine/threonine-protein kinase family. It has a critical role in inhibiting WOX1 (WW domain-containing oxidoreductase) mediated apoptosis. It also mediates starvation-induced BCL2 phosphorylation and activates autophagy. Anti-c-Jun N-terminal kinase antibody can be used in microarray. Rabbit anti-c-Jun N-terminal kinase antibody reacts specifically with JNK1 (46 kD) and JNK2 (55 kD) of cell culture lysates and rat brain tissue extracts. The product has also shown weak cross reactivity for JNK2β (50 kD) isoform in mouse NIH-3T3 fibroblast cell lysate.
Immunogen
Synthetic peptide corresponding to amino acids 339-354 of human JNK1 (c-Jun N-terminal kinase 1), conjugated to KLH. The sequence is highly conserved in JNK1, JNK2 α, β, γ (p54 SAPK α, β, γ) and identical in human, rat, and mouse JNK1.
Application
Anti-c-Jun N-Terminal Kinase antibody produced in rabbit has been used in western blotting.
Biochem/physiol Actions
Mitogen-activated protein kinases (MAPKs) are serine/threonine kinases which play a central role in mitogenic signaling. The MAPKs function to transduce extracellular signals to intracellular targets, including transcription factors controlling the expression of genes essential to many cellular processes including proliferation, development and differentiation. JNK1 is essential for tumor necrosis factor alpha (TNF-α)-induced c-Jun kinase activation, c-Jun expression, and apoptosis. JNK1 and JNK2 participates in the survival of neuronal cells.
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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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
动植物来源生物产品
常规特殊物品
此项目有
c-Jun N-terminal protein kinase 1 (JNK1), but not JNK2, is essential for tumor necrosis factor alpha-induced c-Jun kinase activation and apoptosis
Liu J, et al.
Molecular and Cellular Biology, 24(24), 10844-10856 (2004)
Induction of COX-2 enzyme and down-regulation of COX-1 expression by lipopolysaccharide (LPS) control prostaglandin E2 production in astrocytes
Font-Nieves M, et al.
The Journal of Biological Chemistry, 287(9), 6454-6468 (2012)
MEK7-dependent activation of p38 MAP kinase in keratinocytes
Dashti SR, et al.
The Journal of Biological Chemistry, 276(11), 8059-8063 (2001)
Nan-Shan Chang et al.
The Journal of biological chemistry, 278(11), 9195-9202 (2003-01-07)
Transient activation of c-Jun N-terminal kinase (JNK) promotes cell survival, whereas persistent JNK activation induces apoptosis. Bovine testicular hyaluronidase PH-20 activates JNK1 and protects L929 fibroblasts from staurosporine-mediated cell death. PH-20 also induces the expression of a p53-interacting WW domain-containing
Ilan Feine et al.
PloS one, 7(7), e41633-e41633 (2012-08-23)
Major circulation pathologies are initiated by oxidative insult expansion from a few injured endothelial cells to distal sites; this possibly involves mechanisms that are important to understanding circulation physiology and designing therapeutic management of myocardial pathologies. We tested the hypothesis
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