Anti-Phospho-RELB-Ser552 antibody (530-579 aa) (STJ91004)
SPECIFICATIONS
ClonalityPolyclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
ImmunogenThe antiserum was produced against synthesized peptide derived from the human RelB around the phosphorylation site of Ser552 at the amino acid range 530-579
General Information
| Short Description | Rabbit polyclonal anti-Phospho-Transcription factor RelB-Ser552 (530-579 aa) for use in WB, IHC, IF and ELISA in Human and Mouse samples. Datasheet included with dilution recommendations, and related reagents. |
| Applications | WB/IHC/IF/ELISA |
| Host | Rabbit |
| Reactivity | Human/Mouse |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Clonality | Polyclonal |
| Isotype | IgG |
| Conjugation | Unconjugated |
| Concentration | 1 mg/mL |
| Purification | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen. |
| Dilution Range | WB 1:500-1:2000IHC 1:100-1:300ELISA 1:20000IF 1:50-200 |
| Formulation | Liquid in PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide. |
| Storage Instruction | Store at-20ยฐC for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
Target Information
| Gene Symbol | RELB |
| Gene ID | 5971 |
| Uniprot ID | RELB_HUMAN |
| Immunogen | The antiserum was produced against synthesized peptide derived from the human RelB around the phosphorylation site of Ser552 at the amino acid range 530-579 |
| Immunogen Region | 530-579 aa |
| Specificity | Phospho-RelB (S552) Polyclonal Antibody detects endogenous levels of RelB protein only when phosphorylated at S552. |
Additional Info
| Function | NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed 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. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a CRY1/CRY2 independent manner. Increased repression of the heterodimer is seen in the presence of NFKB2/p52. Is required for both T and B lymphocyte maturation and function. |
| Protein Name | Transcription Factor RelbI-Rel |
| Database Links | Reactome: R-HSA-5607761Reactome: R-HSA-5621575Reactome: R-HSA-5676590 |
| Cellular Localisation | NucleusCytoplasmCytoskeletonMicrotubule Organizing CenterCentrosomeColocalizes With Nek6 In The Centrosome |
| Alternative Antibody Names | Anti-Transcription Factor Relb antibodyAnti-I-Rel antibodyAnti-RELB antibody |
Information sourced from Uniprot.org