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Antibodies

NFkB P52 Antibody

Product Sizes
100 ul
£600.00
100-4185-100UL
About this Product
SKU:
100-4185
Additional Names:
NFKB2|rabbit Anti-NFKB p52 antibody, Nuclear factor NF-kappa-B p100 subunit, DNA-binding factor KBF2, H2TF1, Lymphocyte translocation chromosome 10 protein, Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2, Oncogene Lyt-10, Lyt10, Nuclear factor NF-kappa-B p52 subunit, NFKB2
Application:
ELISA, Gel Shift/EMSA, Western Blot
Buffer:
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride
CE/IVD:
RUO
Clonality:
Polyclonal
Concentration:
90 mg/ml
Extra Details:
NFkB was originally identified as a factor that binds to the immunoglobulin kappa light chain enhancer in B cells. It was subsequently found in non-B cells in an inactive cytoplasmic form consisting of NFkB bound to IkB. NFkB was originally identified as a heterodimeric DNA binding protein complex consisting of p65 (RelA) and p50 (NFKB1) subunits. Other identified subunits include p52 (NFKB2), c-Rel, and RelB. The p65, cRel, and RelB subunits are responsible for transactivation. The p50 and p52 subunits possess DNA binding activity but limited ability to transactivate. p52 has been reported to form transcriptionally active heterodimers with the NFkB subunit p65, similar to p50/p65 heterodimers. The heterodimers of p52/p65 and p50/p65 are regulated by physical inactivation in the cytoplasm by an inhibitor called IkB-a. IkB-a binds to the p65 subunit, preventing nuclear localization and DNA binding. Low levels of p52 and p50 homodimers can also exist in cells.
Format:
Antiserum
Formulation:
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Host:
Rabbit
Immunogen:
Human NFKB2 p52/p100 peptide corresponding to aa residue 1-19 the human protein conjugated to Keyhole Limpet Hemocyanin (KLH).
Physical State:
Liquid
Reactivities:
Human
Shipping Conditions:
Dry Ice
Specificity:
This product was prepared from monospecific antiserum by delipidation and defibrination. Anti-Human NFKB2 p52 may react non-specifically with other proteins. Control peptide (code #100-4185p) will compete only with the specific reaction of antiserum with Human NFKB2 p52.
Storage Conditions:
-20[o]C aliquoted. Aliquot. Avoid freeze/thaw cycles., 2-8[o]C diluted. Aliquot. Avoid freeze/thaw cycles.
Supplier:
Rockland Inc
Type:
Antibody: Polyclonal Antibody
H1299 cells expressing mutant p53-R175H show increased binding to the NF-K KappaB site. (A) Nuclear extracts of HC-5 and H-R175H were incubated as described in Materials and Methods with a 32P-labeled probe containing the sequence of the NF-K KappaB DNA-binding site. Competition studies were done using a specific competitor (lanes 4 to 7) and a nonspecific competitor (lanes 8 to 11) at both 20x (lanes 4, 5, 8, and 9) and 40x (lanes 6, 7, 10, and 11) molar excess. The single arrows indicate the DNA complexes containing NF-K KappaB complexes. Increased NF-K KappaB activity is observed in the presence of mutant p53 (lanes 2, 3, and 8 to 11). The double arrow indicates the supershifted complex in the presence of antibodies specific for NF-K KappaB1 (p50), NF-K KappaB2 (p52), and p53 (lanes 12 to 15, 20 to 21, and 24 to 29, respectively). Equal amounts of protein were added to each lane. Fig. 7 PMID: 16260623.
EMSA results using Anti-NFKB p52. Comparison of nuclear factor (NF)-K KappaB binding activity among CD30-positive lymphomas with or without stimulation of CD30. (a) Whole-cell lysates of CD30-positive lymphoma cell lines with or without stimulation of CD30 were incubated with the 32P-labeled HIV K KappaB probe, and K KappaB binding was analyzed by electrophoretic mobility shift assay (EMSA). (b) Supershift assay of CD30-stimulated Karpas 299 and SR-786 using the antibodies indicated. Addition of anti-Bcl-3 antibodies produced no apparent supershifted bands (data not shown). The specificity of K KappaB binding was determined by competition with an excess amount of unlabeled HIV K KappaB probe or control unlabeled AP1 probe (5'-CGCTTGATGAGTCAGCCGGAA-3'). (c) NF-K KappaB DNA-binding activities of p52-containing components were compared among CD30-positive lymphoma cell lines upon stimulation of CD30. The whole-cell lysates were incubated with the 32P-labeled H2 K KappaB probe, and the binding was analyzed by EMSA. (d) Supershift assay of CD30-stimulated Karpas 299, KM-H2 and KIS-1. The cell lysates were first incubated with antibodies against p50, p52, p65, RelB and c-Rel, and the components of the NF-K KappaB-binding complexes in each cell line were determined. The specificity of K KappaB binding was determined by competition with an excess amount of unlabeled H2 K KappaB probe or control unlabeled AP1 probe. Fig 5. PMID: 16108830.