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MELT Antibody

  • 中文名称：
    MELT兔多克隆抗体
  • 货号：
    CSB-PA355665ZA01DNK
  • 规格：
    ￥440
  • 促销：
    小规格抗体限时一口价
  • 图片：
    • Western Blot
      Positive WB detected in: recombinant protein
      All lanes: MELT Antibody at 1:1000
      Secondary
      Goat polyclonal to rabbit IgG at 1/50000 dilution
      Predicted band size: 17 kDa
      Observed band size: 17 kDa
  • 其他：

产品详情

  • 产品名称：
    Rabbit anti-Apis mellifera (Honeybee) MELT Polyclonal antibody
  • Uniprot No.：
    P01501
  • 基因名：
    MELT
  • 别名：
    Melittin (Allergen Api m 3) (Allergen Api m III) (allergen Api m 4), MELT
  • 宿主：
    Rabbit
  • 反应种属：
    Apis mellifera
  • 免疫原：
    Recombinant Apis mellifera MELT protein (44-69aa)
  • 免疫原种属：
    Apis mellifera (Honeybee)
  • 标记方式：
    Non-conjugated
  • 克隆类型：
    Polyclonal
  • 抗体亚型：
    IgG
  • 纯化方式：
    >95%, Protein G purified
  • 浓度：
    It differs from different batches. Please contact us to confirm it.
  • 保存缓冲液：
    Preservative: 0.03% Proclin 300
    Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
  • 产品提供形式：
    Liquid
  • 应用范围：
    ELISA, WB
  • 推荐稀释比：
    Application Recommended Dilution
    WB 1:500-1:5000
  • Protocols：
  • 储存条件：
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 货期：
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

产品评价

靶点详情

  • 功能：
    Melittin: Main toxin of bee venom with strong hemolytic activity and antimicrobial activity. It has enhancing effects on bee venom phospholipase A2 activity. This amphipathic toxin binds to negatively charged membrane surface and forms pore by inserting into lipid bilayers inducing the leakage of ions and molecules and the enhancement of permeability that ultimately leads to cell lysis. It acts as a voltage-gated pore with higher selectivity for anions over cations. The ion conductance has been shown to be voltage-dependent. Self-association of melittin in membranes is promoted by high ionic strength, but not by the presence of negatively charged lipids. In vivo, intradermal injection into healthy human volunteers produce sharp pain sensation and an inflammatory response. It produces pain by activating primary nociceptor cells directly and indirectly due to its ability to activate plasma membrane phospholipase A2 and its pore-forming activity.; Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.; Melittin-2: Has strong hemolytic activity.
  • 基因功能参考文献：
    1. this study shows that melittin constrains the expression of identified key genes associated with bladder cancer PMID: 29854840
    2. Molecular dynamics simulation was performed to characterize the structure and interaction of melittin with lipid molecules in dimyristoylphosphatidylglycerol bilayers. The simulation results indicate that basic amino acid residues in melittin interact strongly with lipid head groups to generate a pseudo-transmembrane alignment. PMID: 28165239
    3. All-atom/coarse-grained approach simulations demonstrated a clear salt effect and a moderate temperature effect on aggregation and support the molten globule model of melittin aggregates. PMID: 28636825
    4. Taking uPA(1-43) amino acids specifically binding to uPAR as targeted part of fusion protein, and making use of antitumor activity of melittin, the recombinant fusion protein it was able to inhibit growth of ovarian tumors . PMID: 25394558
    5. These findings point to the preservation and, from more aqueous solvent conditions, the formation of an at least partially helical form of melittin in the gas-phase. PMID: 21701716
    6. isolation and biochemical characterization of melittin-S, an isoform of melittin comprising a Ser residue at the 10th position, from the venom of Africanized A. mellifera; seasonal variation in venom content of melittins PMID: 20472009
    7. This paper characterizes the quantitative parameters of the peptide-lipid interactions related to the mechanism of formation of toroidal pores by melittin, compared to the formation of barrel-stave pores by alamethicin. PMID: 15035629
    8. melittin is localized in a motionally restricted region in membranes; increasing unsaturation in membranes causes a considerable change in the secondary structure of membrane-bound melittin PMID: 15471568
    9. from a kinetics point of view, the formation of the alpha-helix is a consequence of the membrane insertion of melittin. The rate of melittin folding was found to be influenced by the lipid composition of the bilayer. PMID: 15533303
    10. Melittin does not block NF-kappa B-p50-DNA interactions; rather, the human cells tested show significantly increased mRNA levels of several inflammatory genes, elevated cyclooxygenase-2 protein levels, and release of large quantities of oxygen radicals. PMID: 17579088
    11. increases in plasma adrenaline, noradrenaline, vasopressin levels and renin activity mediate the pressor responses to melittin in normal and hypotensive conditions in rats PMID: 17897713

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  • 亚细胞定位：
    Secreted. Target cell membrane.
  • 蛋白家族：
    Melittin family
  • 组织特异性：
    Expressed by the venom gland.
  • 数据库链接：

    KEGG: ame:406130

    STRING: 7460.GB10355-PA

    UniGene: Ame.1212