IL-17C Polyclonal Antibody (AN006890L)
For research use only.
| Verified Samples | Verified Samples in WB: HT-29, Rat small intestine |
| Dilution | WB 1:500-1:1000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Rat |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Recombinant Mouse IL-17C protein expressed by E.coli |
| Abbre | IL-17C |
| Synonyms | IL17C, CX2, IL-17C, Cytokine CX2, IL 17C, IL 21, Interleukin 17C, Interleukin-17C |
| Swissprot | |
| Calculated MW | 22 kDa |
| Observed MW |
50 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 | Secreted |
| Tissue Specificity | Expressed by epithelial cells after bacterial challenge. Low expression, if any, in lymphocytes. |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Antigen Affinity Purification |
| 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 | The Interleukin 17 (IL-17) family proteins, comprising six members (IL-17, IL-17B through IL-17F), are secreted, structurally related proteins that share a conserved cysteine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus. With the exception of IL-17B, which exists as a non‑covalently linked dimer, all IL-17 family members are disulfide-linked dimers. IL-17 family proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions. Two receptors (IL-17 R, and IL-17B R), which are activated by IL-17 family members have been identified. In addition, at least three additional orphan type I transmembrane receptors with homology to IL-17 R, including IL-17 RL (IL-17 RC), IL-17 RD, and IL‑17 RE, have also been reported. Mouse IL-17C cDNA encodes a 194 amino acid (aa) protein with a putative 14 aa signal peptide. Although there are no potential N-linked glycosylation sites, it is reportedly glycosylated. IL-17C shares from 15%‑30% aa sequence identity with other IL-17 family members. Mouse and human IL-17C share 83% aa sequence identity. IL-17C has a very restricted expression pattern and was detected as a rare expressed sequence tag (EST) in an adult prostate and fetal kidney libraries. IL-17C has been shown to stimulate the release of TNF-alpha and IL-1 beta from the monocytic cell line THP-1, a property it shares with IL-17B. Human IL‑17C is active on mouse cells. |
Other Clones
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Unconjugated
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