Nuclear Factor Of Kappa Light Polypeptide Gene Enhancer In B-Cells 2 Peptide 1

CPTC-NFKB2-1

AB_2617299

Nuclear Factor Of Kappa Light Polypeptide Gene Enhancer In B-Cells 2 Peptide 1

IgG

Rabbit Monoclonal Antibody

03/20/2024

Peptide, Endogenous

Immuno-Oncology (IO)

00034

Nuclear Factor Of Kappa Light Polypeptide Gene Enhancer In B-Cells 2 Peptide 1

CPTC-NFKB2 Peptide 1

NFKB2; H2TF1; LYT-10; LYT10; P105; P52; Lymphocyte Translocation Chromosome 10 Protein; DNA-Binding Factor KBF2; Nuclear Factor NF-Kappa-B P100 Subunit; Nuclear Factor Of Kappa Light Chain Gene Enhancer In B-Cells 2; Oncogene Lyt-10; Nuclear Factor Of Kappa Light Polypeptide Gene Enhancer In B-Cells 2

This gene encodes one of the subunits of the transcription factor complex nuclear factor-kappa-B (NFkB). The NFkB transcription factor complex is expressed in numerous cell types and functions as a central activator of genes involved in inflammation and immune function. The NFkB complex can consist of different subunits that form both homo- or heterodimers which bind specific kappa-B elements in target genes. This gene encodes the p100 subunit that is processed into the active p52 subunit. This protein can function as both a transcriptional activator and repressor, depending on its dimer partner. Alternate splicing results in both coding and non-coding variants.

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. Different dimer combinations act as transcriptional activators or repressors, respectively. 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. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65.

NF-kappaB (nuclear factor-kappa B) is a rapidly acting primary transcription factor found in all cell types. It is involved in cellular responses to stimuli such as cytokines and stress and plays a key role in regulating the immune response to infection. In unstimulated cells NF-kappaB dimers are sequestered inactively in the cytoplasm by a protein complex called inhibitor of kappa B (IkappaB). IkappaB inactivates NF-kappaB by masking the nuclear localization signals (NLS). Activation of NF-kappaB occurs via degradation of IkappaB, a process that is initiated by its phosphorylation by IkappaB kinase (IKK). Phosphorylated IvB becomes dissociated from NF-kappaB, unmasking the NLS. Phosphorylation also results in IkappaB ubiquitination and targeting to the proteasome. NF-kappaB can now enter the nucleus and regulate gene expression. NF-kappaB turns on expression of IkappaB forming a negative feedback loop.

10q24

NP_002493.2

Q00653

N/A

Synthetic Peptide

N/A

0

1430

06/11/2013