|Sample Size:||30ug for $99, contact us for details|
Data & Images
|Product Name||Anti-NFkB p105/P50 Picoband™ Antibody|
|Description||Rabbit IgG polyclonal antibody for Nuclear factor NF-kappa-B p105 subunit(NFKB1) detection. Tested with WB, IHC-P in Human;Rat.|
|Cite This Product||Anti-NFkB p105/P50 Picoband™ Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PB9149)|
|Replacement Item||This antibody may replace the following items: sc-23639|sc-134427|sc-20228|sc-20230 from Santa Cruz Biotechnology.|
|Validated Species||Human, Rat|
*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, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P).
*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 2017!
|Immunogen||E.coli-derived human NFkB p105/P50 recombinant protein (Position: M1-Q360). Human NFkB p105/P50 shares 93% amino acid (aa) sequence identity with mouse NFkB p105/P50.|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
*carrier free antibody available upon request.
|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||Nuclear factor NF-kappa-B p105 subunit|
|Molecular Weight||105356 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 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. .|
|Sequence Similarities||Contains 7 ANK repeats.|
|Subcellular Localization||Nucleus. Cytoplasm. Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).|
|Alternative Names||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;Nuclear factor NF-kappa-B p50 subunit;NFKB1;|
Background for Nuclear factor NF-kappa-B p105 subunit
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-NFkB p105/P50 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:|
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, By Heat|
Western blot, 0.1-0.5μg/ml, Human, Rat
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-NFkB p105/P50 Picoband™ Antibody Images
Click the images to enlarge.
All lanes: Anti NFKBP105 (PB9149) at 0.5ug/ml
WB: Recombinant Human NFKBP105 Protein 0.5ng
Predicted bind size: 40KD
Observed bind size: 40KD
All lanes: Anti NFKBP105 (PB9149) at 0.5ug/ml
Lane 1: Rat Spleen Tissue Lysate at 50ug
Lane 2: PC-12 Whole Cell Lysate at 40ug
Lane 3: HELA Whole Cell Lysate at 40ug
Lane 4: A431 Whole Cell Lysate at 40ug
Lane 5: JURKAT Whole Cell Lysate at 40ug
Lane 6: MCF-7 Whole Cell Lysate at 40ug
Predicted bind size: 50KD
Observed bind size: 50KD
IHC(P): Human Lung Cancer Tissue
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.,