• Immunohistochemical analysis of paraffin-embedded human liver cancer. 1, Antibody was diluted at 1:200 (4°C overnight). 2, Tris-EDTA, pH9.0 was used for antigen retrieval. 3, Secondary antibody was diluted at 1:200 (room temperature, 45min).

Anti-Cleaved-NFKB1-Gly433 antibody (433-434) (STJA0005901)

SKU:
STJA0005901

Current Stock:
Host: Rabbit
Applications: WB/ELISA/IHC
Reactivity: Human/Mouse
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-Cleaved-Nuclear factor NF-kappa-B p105 subunit-Gly433 (433-434) is suitable for use in Western Blot, ELISA and Immunohistochemistry research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: Liquid in PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide.
Purification: The antibody was affinity-purified from rabbit serum by affinity-chromatography using specific immunogen.
Concentration: 1 mg/mL
Dilution Range: WB 1:500-2000
IHC-p 1:50-300
ELISA 2000-20000
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: NFKB1
Gene ID: 4790
Uniprot ID: NFKB1_HUMAN
Immunogen Region: 433-434
Specificity: This antibody detects endogenous levels of Human, Mouse NF-Kappa B p50 (Cleaved-Gly433, protein was cleaved amino acid sequence between 433-434 )
Immunogen: Synthesized peptide derived from human NF-Kappa B p105 (Cleaved-Gly433)
Post Translational Modifications Generation of the NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit) transcription factor takes place both cotranslationally and post-translationally via non-mutually exclusive mechanisms. A cotranslational processing allows the production of both p50 and p105 (Nuclear factor NF-kappa-B p105 subunit) from a single NFKB1 mRNA. While translation occurs, the particular unfolded structure after the GRR repeat region acts as a substrate for the proteasome, promoting degradation of the C-terminus. The GRR acts as a proteasomal 'stop signal', protecting the region upstream of the GRR from degradation and promoting generation of p50. It is unclear if limited proteasome degradation during cotranslational processing depends on ubiquitination. NF-kappa-B p50 is also generated post-translationally following ubiquitination by the KPC complex, leading to limited processing by the proteasome downstream of the GRR region, thereby generating p50. Nuclear factor NF-kappa-B p105 subunit: Phosphorylation at the C-terminus by IKBKB/IKKB acts as a signal for ubiquitination and promotes either complete degradation or processing to generate the NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit). Phosphorylation at Ser-903 and Ser-907 primes p105 for proteolytic processing in response to TNF-alpha stimulation. Phosphorylation at Ser-923, Ser-927 and Ser-932 are required for BTRC/BTRCP-mediated ubiquitination and proteolysis. Phosphorylation at Ser-927 is also required for ubiquitination by the KPC complex and limited processing to generate NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit). Nuclear factor NF-kappa-B p105 subunit: Polyubiquitinated at multiple Lys residues in the C-terminus. Polyubiquitinated by the SCF(FBXW11) and SCF(BTRC) complexes following phosphorylation at Ser-923, Ser-927 and Ser-932, leading to its complete degradation. In contrast, polyubiquitination by the KPC complex following phosphorylation at Ser-927 leads to limited proteosomal processing and generation of the active NF-kappa-B p50 (Nuclear factor NF-kappa-B p50 subunit). S-nitrosylation of Cys-61 affects DNA binding. The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation.
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 and the heterodimeric p65-p50 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. 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. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 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. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling.active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105. Nuclear factor NF-kappa-B p105 subunit: P105 is the precursor of the active p50 subunit (Nuclear factor NF-kappa-B p50 subunit) of the nuclear factor NF-kappa-B. Acts as a cytoplasmic retention of attached NF-kappa-B proteins by p105. Nuclear factor NF-kappa-B p50 subunit: Constitutes the active form, which associates with RELA/p65 to form the NF-kappa-B p65-p50 complex to form a transcription factor. Together with RELA/p65, 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.
Protein Name Nuclear Factor Nf-Kappa-B P105 Subunit
Dna-Binding Factor Kbf1
Ebp-1
Nuclear Factor Of Kappa Light Polypeptide Gene Enhancer In B-Cells 1 Cleaved Into - Nuclear Factor Nf-Kappa-B P50 Subunit
Database Links Reactome: R-HSA-1169091
Reactome: R-HSA-1810476
Reactome: R-HSA-193692
Reactome: R-HSA-202424
Reactome: R-HSA-209560
Reactome: R-HSA-2559582
Reactome: R-HSA-2871837
Reactome: R-HSA-3134963
Reactome: R-HSA-3214841
Reactome: R-HSA-381340
Reactome: R-HSA-445989
Reactome: R-HSA-448706
Reactome: R-HSA-5603029
Reactome: R-HSA-5607764
Reactome: R-HSA-5621575
Reactome: R-HSA-5660668
Reactome: R-HSA-5684264
Reactome: R-HSA-6798695
Reactome: R-HSA-844456
Reactome: R-HSA-8853884
Reactome: R-HSA-9020702
Reactome: R-HSA-933542
Reactome: R-HSA-9609690
Reactome: R-HSA-9660826
Reactome: R-HSA-9692916
Cellular Localisation Nuclear Factor Nf-Kappa-B P105 Subunit: Cytoplasm
Nuclear Factor Nf-Kappa-B P50 Subunit: Nucleus
Cytoplasm
Association With Nfkbia Inhibitor (I-Kappa-B)
Promotes Its Retention In The Cytoplasm In An Inactive Form
Translocates Into The Nucleus Following Nfkbia Degradation
Alternative Antibody Names Anti-Nuclear Factor Nf-Kappa-B P105 Subunit antibody
Anti-Dna-Binding Factor Kbf1 antibody
Anti-Ebp-1 antibody
Anti-Nuclear Factor Of Kappa Light Polypeptide Gene Enhancer In B-Cells 1 Cleaved Into - Nuclear Factor Nf-Kappa-B P50 Subunit antibody
Anti-NFKB1 antibody

Information sourced from Uniprot.org

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