NFκB-p65 Polyclonal Antibody (E-AB-32233)
For research use only.
| Verified Samples |
Verified Samples in WB: KB, Hela, 293T, 3T3 Verified Samples in IHC: Human stomach cancer, Mouse kidney |
| Dilution | WB 1:500-1:2000, IHC 1:100-1:300 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB, IHC-p |
| Clonality | Polyclonal |
| Immunogen | Synthesized peptide derived from human NFκB-p65 around the non-phosphorylation site of Ser281. |
| Abbre | NFκB-p65 |
| Synonyms | Avian reticuloendotheliosis viral (v rel) oncogene homolog A, MGC131774, NF kappa B p65delta3, NFKB3, Nuclear Factor NF Kappa B p65 Subunit, Nuclear fact, Nuclear factor NF-kappa-B p65 subunit, Nuclear factor of kappa light polypeptide gene enhancer in B cells 3 |
| Swissprot | |
| Calculated MW | 60 kDa |
| Observed MW |
60 kDa
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Nucleus. Cytoplasm. Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). Colocalized with RELA in the nucleus upon TNF-alpha induction. |
| Concentration | 1 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer, 0.5% protein protectant and 50% glycerol. |
| Purification Method | Affinity purification |
| Research Areas | Cancer, Cell Biology, Cardiovascular, Epigenetics and Nuclear Signaling, Metabolism, Microbiology, Neuroscience, Signal Transduction |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
| background | Proteins encoded by the v-Rel viral oncogene and its cellular homolog, c-Rel,are members of a family of transcription factors that include the two subunits of the transcription factor NFκB (p50 and p65) and the Drosophila maternal morphogen, dorsal. Both proteins specifically bind to DNA sequences that are the same or slight variations of the 10 bp κB sequence in the immunoglobulin κ light chain enhancer. This same sequence is also present in a number of other cellular and viral enhancers. The DNA binding activity of NFκB is activated and NFκB is subsequently transported from the cytoplasm to the nucleus in cells exposed to mitogens or growth factors. cDNAs encoding precursors for two distinct proteins of the same size have been described, designated p105 and p100. The p105 precursor contains p50 at its N-terminus and a C-terminal region that when expressed as a separate molecule, designated pdI, binds to p50 and regulates its activity. |
Other Clones
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Unconjugated
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