IL-33 Monoclonal Antibody (AN200101P)
For research use only.
| Verified Samples |
Verified Samples in WB: Hela, K562, Jurkat Verified Samples in IP: HeLa, K562, jurkat |
| Dilution | WB 1:500-1:2000, IP 0.5-2 μL/mg of lysate |
| Isotype | IgG2a |
| Host | Mouse |
| Reactivity | Human |
| Applications | WB, IP |
| Clonality | Monoclonal |
| Immunogen | Recombinant Human IL-33 Protein |
| Abbre | IL33 |
| Synonyms | DVS, IL1F, Interleukin, C9orf, IL-1F, IL33, C9orf26, DVS27, IL1F11, NF-HEV, NFEHEV, DVS27 related protein, IL-1F11, IL-33, Interleukin-1 family member 11, Interleukin-33, Nuclear factor from high endothelial venules, NFHEV, CHROMOSOME 9 OPEN READING FRAME 26, DKFZp586H0523, IL 1F11, IL 33, Interleukin 1 family member 11, Interleukin 33, INTERLEUKIN 33 NFHEV, Interleukin 33 precursor, Interleukin33, Interleukin-33 (109-270), NF HEV, Nuclear factor for high endothelial venules, OTTHUMP00000021041, RP11 575C20.2 |
| Swissprot | |
| Calculated MW | 31 kDa |
| Observed MW |
25 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. |
| Concentration | 1 mg/mL |
| Buffer | 0.2 μm filtered solution in PBS |
| Purification Method | Protein A |
| Research Areas | Cardiovascular, Immunology |
| Clone No. | 4D9 |
| Conjugation | Unconjugated |
| Storage | This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles. |
| Shipping | Ice bag |
| background | IL-33, also known as NF-HEV and DVS 27, is a 30 kDa proinflammatory protein that may also regulate gene transcription. DVS 27 was identifed as a gene that is upregulated in vasospastic cerebral arteries. NF-HEV was described as a nuclear factor that is preferentially expressed in the endothelial cells of high endothelial venules relative to endothelial cells from other tissues. IL-33 was identified based on sequence and structural homology with IL-1 family cytokines. DVS 27, NF-HEV, and IL-33 share 100% amino acid sequence identity. IL-33 is constitutively expressed in smooth muscle and airway epithelia. It is upregulated in arterial smooth muscle, dermal fibroblasts, and keratinocytes following IL-1 alpha or IL-1 beta stimulation. Similar to IL-1, IL-33 can be cleaved in vitro by caspase-1, generating an N-terminal fragment that is slightly shorter than the C-terminal fragment. The N-terminal portion of full length IL-33 contains a predicted bipartite nuclear localization sequence and a homeodomain-like helix-turn-helix DNA binding domain. By immunofluorescence, full length IL-33 localizes to the nucleus in HUVECs and transfectants. The C-terminal fragment, corresponding to mature IL-33, binds and triggers signaling through mast cell IL-1 R4/ST2L, a longtime orphan receptor involved in the augmentation of Th2 cell responses. A ternary signaling complex is formed by the subsequent association of IL-33 and ST2L with IL-1R AcP. Stimulation of Th2 polarized lymphocytes with mature IL-33 in vitro induces IL-5 and IL-13 secretion. In vivo administration of mature IL-33 promotes increased production of IL-5, IL-13, IgE, and IgA, as well as splenomegaly and inflammatory infiltration of mucosal tissues. Full length and mature human IL-33 share 52 ‑ 58% aa sequence identity with mouse and rat IL-33. Human IL-33 shares less than 20% aa sequence identity with other IL-1 family proteins. |
Other Clones
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Unconjugated
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