Recombinant IRAK1 Monoclonal Antibody (AN301855L)
For research use only.
| Verified Samples |
Verified Samples in WB: HEK-293, HeLa,K562 Verified Samples in IHC: Mouse pancreas, Rat pancreas |
| Dilution | WB 1:200-1:1000, IHC 1:100-1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human IRAK1 fragment |
| Abbre | IRAK1 |
| Synonyms | IRAK1, IRAK, pelle |
| Swissprot | |
| Calculated MW | 77 kDa |
| Observed MW |
80 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 | Immunology, Signal Transduction, Cardiovascular |
| Clone No. | A567 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | IRAK1 is the first member of the death domain containing protein kinase family that play a key role in initiating innate immune response against foreign pathogens. They are involved in Toll-like receptor (TLR) and interleukin-1 receptor (IL-1R) signaling pathways. Upon ligand binding to TLR/IL-1R, IRAK1 is recruited by MYD88 to the receptor-signaling complex, the association leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Hyper-phosphorylated IRAK1 then disengages from the receptor complex, and forms a cytosolic IRAK1-TRAF6 complex. TRAF6 then interacts with TAK and TAB, resulting in eventual activation of the NF-κB and MAPK pathways. Phosphorylated IRAK1 also undergoes ubiquitin-mediated degradation or sumoylation, which results in nuclear translocation and transcriptional activation of inflammatory target genes. |
Other Clones
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Other Formats
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Unconjugated
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