Recombinant Phospho-IRF3 (Ser396) Monoclonal Antibody (AN301389L)
For research use only.
| Verified Samples | Verified Samples in WB: Hela |
| Dilution | WB 1:500-1:2000, |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | A synthetic peptide corresponding to residues around (Ser396) of Human Phospho-IRF3 |
| Abbre | IRF3 |
| Synonyms | IRF, IRF3, entrez:3661, IIAE7, IRF-3, IRF-3 |
| Swissprot | |
| Calculated MW | 47 kDa |
| Observed MW |
60 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, Mitochondrion, Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect (PubMed:10805757). When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm (PubMed:10805757). Recruited to mitochondria via TOMM70:HSP90AA1 upon Sendai virus infection (PubMed:25609812). |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Immunology, Epigenetics and Nuclear Signaling |
| Clone No. | 10A12 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | This gene encodes a member of the interferon regulatory transcription factor (IRF) family. The encoded protein is found in an inactive cytoplasmic form that upon serine/threonine phosphorylation forms a complex with CREBBP. This complex translocates to the nucleus and activates the transcription of interferons alpha and beta, as well as other interferon-induced genes. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. |
Other Clones
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Unconjugated
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