Data & Images
|Product Name||Anti-NF-kB p65 Picoband™ Antibody|
|Description||Rabbit IgG polyclonal antibody for Transcription factor p65(RELA) detection. Tested with WB in Human.|
|Cite This Product||Anti-NF-kB p65 Picoband™ Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PB9087)|
|Replacement Item||This antibody may replace the following items: sc-81622 from Santa Cruz Biotechnology.|
*Our Boster Guarantee covers the use of this product in the above tested applications.
**For positive and negative control design, consult "Tissue specificity" under Protein Target Info.
|Recommended Detection Systems||Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
*Blocking peptide can be purchased at $50. Contact us for more information
**Boster also offers various secondary antibodies for Immunoflourescecne and IHC. Take advantage of the buy 1 primary antibody get 1 secondary antibody for free promotion for the entire year 2018!
|Immunogen||E.coli-derived human NF-kB p65 recombinant protein (Position: F99-S551). Human NF-kB p65 shares 86% amino acid (aa) sequence identity with mouse NF-kB p65.|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.|
|Concentration||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Storage||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Purification||Immunogen affinity purified.|
Protein Target Info (Source: Uniprot.org)
You can check the tissue specificity below for information on selecting positive and negative control.
|Protein Name||Transcription factor p65|
|Molecular Weight||60219 MW|
|Protein 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 p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681). .|
|Sequence Similarities||Contains 1 RHD (Rel-like) domain.|
|Subcellular Localization||Nucleus. Cytoplasm. Colocalized with DDX1 in the nucleus upon TNF-alpha induction (By similarity). Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). Colocalizes with GFI1 in the nucleus after LPS stimulation. .|
|Alternative Names||Transcription factor p65;Nuclear factor NF-kappa-B p65 subunit;Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3;RELA;NFKB3;|
|Research Areas|||epigenetics and nuclear signaling|transcription|domain families|zinc finger| signal transduction|signaling pathway|nuclear hormone receptors|estrogen| epigenetics and nuclear signaling|nuclear signaling pathways|nuclear receptors| cancer| metabolism|pathways and processes|mitochondrial metabolism|mitochondrial biogenesis|metabolic signaling pathways|nucleotide metabolism|molecular processes|mitochondrial transcription||
Background for Transcription factor p65
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-NF-kB p65 Picoband™ Antibody by testing all applications on non-spiked tissues and cell lines to ensure that the affinity of the antibody is enough to react to the endogenouse level of the target protein. Read more about our QC panel here.
|Recommended dilution ratios are listed below:|
Western blot, 0.1-0.5μg/ml, Human|
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-NF-kB p65 Picoband™ Antibody Images
Click the images to enlarge.
All lanes: Anti- NF-kB p65 (PB9087) at 0.5ug/ml
Lane 1: Jurkat Whole Cell Lysate at 40ug
Lane 2: Colo320 Whole Cell Lysate at 40ug
Lane 3: Hela Whole Cell Lysate at 40ug
Predicted bind size: 64 KD
Observed bind size: 64KD
1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,