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 il 18 Human |产品详情|进口橙子视频旧款采购网




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    il 18 Human
    品牌:Prospec
    货号:
    规格:5µg
    货期:

    il 18 Human

    商品详情 参考文献 相关资料

    Catalogue number

    CYT-269

    Synonyms

    IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.

    Introduction

    IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.

    Description

    Interleukin-18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 18.2 kDa. The IL-18 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Physical Appearance

    Sterile Filtered White lyophilized (freeze-dried) powder.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in PBS and DTT.

    Solubility

    It is recommended to reconstitute the lyophilized Interleukin 18 in sterile 18MΩ-cm H2O not less than 200µg/ml, which can then be further diluted to other aqueous solutions.

    Stability

    Lyophilized Interleukin 18 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL18 should be stored at 4°C between 2-7 days and for future use below -18°C.
    For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
    Please prevent freeze-thaw cycles.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 is 1.5-9 ng/mL and is measured by Interleukin 18 ability to induce IFN-γ secretion by KG‑1 human acute myelogenous leukemia cells in the presence of TNF-alpha.

    References

    1.Title:Discovery of IL-18 As a Novel Secreted Protein Contributing to Resistance by Comparative Secretome Analysis of MCF-7 and MCF-7/Dox.
    Publication:Yao L, Zhang Y, Chen K, Hu X, Xu LX (2011) Discovery of IL-18 As a Novel Secreted Protein Contributing to Resistance by Comparative Secretome Analysis of MCF-7 and MCF-7/Dox. PLoS ONE 6(9): e24684. doi:10.1371/journal.pone.0024684
    Link:http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0024684

     
    2.Title: Influence of Interleukin IL-2 and IL-12 + IL-18 on Surface Expression of Immunoglobulin-Like Receptors KIR2DL1, KIR2DL2, and KIR3DL2 in Natural Killer Cells
    Publications:  Mediators of inflammation 2006 (2006).
    Link: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1618942/

    Usage

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Safety Data Sheet

    SDS

    Background

    Also known as interferon-gamma inducing factor, Interleukin-18 or IL18 is a protein. In humans this protein is encoded by the IL18 gene. The protein is a proinflammatory cytokine.

     

    Mechanism
    The levels of IL-18 in the human body are increased at sites of inflammation. This includes cases of rheumatoid arthritis as well as other similar conditions. Osteoblastic cells express the protein and it is capable of inhibiting osteoclast formation. It is able to do this through a variety of mechanisms.
    For instance, it is able to stimulate GM-CSF. This is created by T cells and is a response to treatment using IL-18. As well as this, the cytokine does stimulate INF-y production through vivo in bone. Furthermore, the impact on bone resorption and osteoclastogenesis is increased when used in conjunction with IL-12 treatment. Studies have shown that IL-18 provides an indirect stimulus on osteoclastogenesis due to the effect it has on T lymphocytes.
    Furthermore, evidence has shown that IL-18 does increase the production of OPG. This was studied in research on transgenic mice that overexpressed IL-18. In these cases osteoclasts decreased as did bone mass. This suggested that IL-18 also has an impact on bone growth.

    Interactions
    Research has also explored the different interactions of IL-18 on other proteins. This includes the interaction between IL-18 and IL-18R. This has been shown to decrease the power of protective immunity and increase pathogenic responses during an infection involving intracellular bacteria. This interaction suggests that the presence or absence of IL-18R signal does impact the pathogenic compared to protective immunity.
    Another interaction between interleukin 19 and Astrocyte has shown that it can improve neuropathic pain processing following nerve injury. It is proposed this is due to the fact that the nociceptive signals in the spinal cord are augmented due to this reaction.

    Function
    Belonging to the IL-1 superfamily, this cytokine is produced by macrophages as well as various other cells. It operates after binding with the interleukin-18 receptor. Working with IL-12, the protein is then able to induce-cell mediated immunity after an infection from lipopolysaccharide and other microbial products.
    Once stimulated by IL-18 other cells including natural killer and T cells then release interferon-y. This type II interferon plays a crucial part in activating the macrophages of various other cells.
    Together IL12 and IL-18 are able to successfully inhibit IgE and IG1 production that is dependent on IL-4. As well as this, the protein is also able to increase IgG2a production through B cells. IL-18 will interact specifically with this type of cytokine and has a negative impact on regulation of biological activity.

    Structure
    Many researchers have suggested that the structure of IL-18 is a key way to understand it’s receptor activation mechanism. The structure of IL-18 closely resembles of IL-1 and has various similarities. It is folded into a beta-trefoil structure and three sites have been shown to be important for receptor activation. These were revealed through extensive mutagenesis. Two of the sites provide s for the IL-18 receptor and are located in positions similar to IL-1. The third structure seems to be used for IL-18 receptor beta binding.

     

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