This Rela Sandwich ELISA is an in-vitro enzyme-linked immunosorbent assay for the measurement of samples in mouse serum, plasma and other biological fluids.
Applications
ELISA
Reactivity
Mouse
Sensitivity
0.19ng/mL
Detection Limit
0.31~20ng/mL
Note
FOR SCIENTIFIC EDUCATIONAL RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR OTHER MEDICAL APPLICATIONS.
Product Properties
Storage Instruction
If unopened the kit may be stored at 2-8°C for up to 1 month. If the kit will not be used within 1 month, store the components separately, according to the component table in the manual.
This kit recognizes Mouse NFKB-p65 in samples. No significant cross-reactivity or interference between Mouse NFKB-p65 and analogues was observed.
Sample Type
Serum, plasma and other biological fluids
Additional Info
Post Translational Modifications
Ubiquitinated by MKRN2, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response. Polyubiquitinated via 'Lys-29'-linked ubiquitin.leading to lysosomal degradation. Monomethylated at Lys-310 by SETD6. Monomethylation at Lys-310 is recognized by the ANK repeats of EHMT1 and promotes the formation of repressed chromatin at target genes, leading to down-regulation of NF-kappa-B transcription factor activity. Phosphorylation at Ser-311 disrupts the interaction with EHMT1 without preventing monomethylation at Lys-310 and relieves the repression of target genes. Phosphorylation on Ser-534 stimulates acetylation on Lys-310 and interaction with CBP.the phosphorylated and acetylated forms show enhanced transcriptional activity. Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities. Reversibly acetylated.the acetylation seems to be mediated by CBP, the deacetylation by HDAC3 and SIRT2. Acetylation at Lys-122 enhances DNA binding and impairs association with NFKBIA. Acetylation at Lys-310 is required for full transcriptional activity in the absence of effects on DNA binding and NFKBIA association. Acetylation at Lys-310 promotes interaction with BRD4. Acetylation can also lower DNA-binding and results in nuclear export. Interaction with BRMS1 promotes deacetylation of Lys-310. Lys-310 is deacetylated by SIRT2. S-nitrosylation of Cys-38 inactivates the enzyme activity. Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity. Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B. Proteolytically cleaved within a conserved N-terminus region required for base-specific contact with DNA in a CPEN1-mediated manner, and hence inhibits NF-kappa-B transcriptional activity.
Function
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 heterodimeric RELA-NFKB1 complex appears to be most abundant one. 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. Different dimer combinations act as transcriptional activators or repressors, respectively. The NF-kappa-B heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function as transcriptional activators. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The inhibitory effect of I-kappa-B on NF-kappa-B through retention in the cytoplasm is exerted primarily through the interaction with RELA. RELA shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Besides its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells. The NF-kappa-B homodimeric RELA-RELA complex appears to be involved in invasin-mediated activation of IL-8 expression.
Protein Name
Transcription Factor P65Nuclear Factor Nf-Kappa-B P65 SubunitNuclear Factor Of Kappa Light Polypeptide Gene Enhancer In B-Cells 3
NucleusCytoplasmNuclearBut Also Found In The Cytoplasm In An Inactive Form Complexed To An Inhibitor (I-Kappa-B)Colocalized With Ddx1 In The Nucleus Upon Tnf-Alpha InductionColocalizes With Gfi1 In The Nucleus After Lipopolysaccharide (Lps) Stimulation
