Recombinant Phospho-IκBα (Ser36) Monoclonal Antibody (AN302095L)
For research use only.
| Verified Samples | Verified Samples in WB: HeLa |
| Dilution | WB 1:1000-2000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Phosphorylated human IκBα (Ser36) peptide |
| Abbre | Phospho-IκBα (Ser36) |
| Synonyms | EDAID, MAD, IKBA, MAD-3, NFKBI, IKB alpha, NFKBIA, EDAID2, I kappa B alpha, IkappaBalpha, I-kappa-B-alpha, IKBalpha, IkB-alpha, MAD 3, NF kappa B inhibitor alpha, MAD3, alpha, Major histocompatibility complex enhancer-binding protein MAD3, NF-kappa-B inhibitor alpha, Nuclear factor of kappa light chain gene enhancer in B cells, Nuclear factor of kappa light polypeptide gene enhancer in B cells inhibitor alpha, nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, pIκBα |
| Swissprot | |
| Calculated MW | 36 kDa |
| Observed MW |
39 kDa
The actual band is not consistent with the expectation.
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 | Cytoplasm, Nucleus |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Signal Transduction, Epigenetics and Nuclear Signaling, Cancer, Immunology |
| Clone No. | A819 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins. Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB. IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified. |
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Unconjugated
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