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  4. Bovine lactoperoxidase (LPO) ELISA kit

Bovine lactoperoxidase (LPO) ELISA kit

  • 中文名稱：
    牛乳過氧化物酶(LPO)酶聯(lián)免疫試劑盒
  • 貨號：
    CSB-EL013066BO
  • 規(guī)格：
    96T/48T
  • 價格：
    ￥4200/￥3000
  • 其他：

產(chǎn)品詳情

  • 產(chǎn)品描述：
    牛乳過氧化物酶(LPO)酶聯(lián)免疫試劑盒（CSB-EL013066BO）為競爭法ELISA試劑盒，定量檢測breast牛奶樣本中的LPO含量。試劑盒檢測范圍為1.56 mU/mL-100 mU/mL，適用于母乳中LPO活性動態(tài)監(jiān)測、乳源酶類功能研究以及乳制品加工過程中天然防腐成分評估等科研用途本品僅用于科研，不用于臨床診斷，產(chǎn)品具體參數(shù)及操作步驟詳見產(chǎn)品說明書。
  • 別名：
    LPO ELISA Kit; Lactoperoxidase ELISA Kit; LPO ELISA Kit; EC 1.11.1.7 ELISA Kit
  • 縮寫：
    LPO
  • Uniprot No.：
  • 種屬：
    Bos taurus (Bovine)
  • 樣本類型：
    breast milk
  • 檢測范圍：
    1.56 mU/mL-100 mU/mL
  • 靈敏度：
    1.56 mU/mL
  • 反應(yīng)時間：
    1-5h
  • 樣本體積：
    50-100ul
  • 檢測波長：
    450 nm
  • 研究領(lǐng)域：
    Cancer
  • 測定原理：
    quantitative
  • 測定方法：
    Competitive
  • 精密度：
    Intra-assay Precision (Precision within an assay): CV%<8%
    Three samples of known concentration were tested twenty times on one plate to assess.
    Inter-assay Precision (Precision between assays): CV%<10%
    Three samples of known concentration were tested in twenty assays to assess.
  • 標(biāo)準(zhǔn)曲線：
    These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
    mU/ml OD1 OD2 Average
    100 0.142 0.136 0.139
    50 0.215 0.219 0.217
    25 0.356 0.342 0.349
    12.5 0.679 0.669 0.674
    6.25 1.191 1.182 1.187
    3.12 1.769 1.781 1.775
    1.56 1.912 1.885 1.899
    0 2.123 2.154 2.139
  • 數(shù)據(jù)處理：
  • 貨期：
    3-5 working days

產(chǎn)品評價

靶點(diǎn)詳情

  • 功能：
    Antimicrobial agent which utilizes hydrogen peroxide and thiocyanate (SCN) to generate the antimicrobial substance hypothiocyanous acid (HOSCN). May protect the udder from infection and promote growth in newborn calves. Inhibits growth of the following bacterial species: E.coli, K.pneumoniae, P.aeruginosa, S.sonnei, S.saphrophyticus, S.epidermidis, and S.dysenteriae.
  • 基因功能參考文獻(xiàn)：
    1. Bovine LPO enzyme was effectively inhibited by phenolic molecules. Ki values of these natural products were found as 0.20 +/- 0.09, 0.22 +/- 0.17, 0.49 +/- 0.11, 0.49 +/- 0.27, and 1.20 +/- 0.25 muM, respectively. Tetrakis and digoxin exhibited noncompetitive inhibition, and other molecules showed competitive inhibition. PMID: 28594102
    2. establish urate as a likely physiological substrate for LPO that will influence host defense and give rise to reactive electrophilic metabolites PMID: 24928513
    3. Studied the 3-dimensional structure of CO-LPO at 2.0A resolution and infrared (IR) spectra of the iron-bound CO stretch from pH 3 to 8.8 at 1 cm(-1) resolution. PMID: 22886082
    4. LPO serve as a catalytic sink for HOCl (hypochlorous acid), while HOCl serves to modulate LPO catalytic activity, bioavailability, and function. PMID: 22132121
    5. Results describe the crystal structure of the complex of lactoperoxidase and 3-amino-1,2,4-triazole (amitrole), which revealed the presence of two ligand molecules, one in the substrate binding site and the second in the hydrophobic channel. PMID: 20461536
    6. LPO can be used for INH activation. It also indicates that the conversion of INH into isonicotinoyl radical by LPO may be the cause of INH toxicity. PMID: 19907057
    7. at higher temperature, the protein hydrophobic core, rich in alpha-helices, unfolds with concomitant disruption of the catalytic heme pocket & activity loss. the stabilizing role of the disulfide bridges and the covalently bound heme cofactor are shown. PMID: 17698426
    8. Comparative spectroscopic analysis of the ferrous forms of LPO, wild-type MPO and the variants demonstrate that a single, stable ferrous form of MPO is present only in those proteins which retain an intact sulfonium linkage. PMID: 18359301
    9. lactoperoxidase containing thiocyanate (SCN(-)) and hypothiocyanate (OSCN(-)) ions were purified and crystallized; the structure was determined at 2.3-A resolution and refined to R(cryst) and R(free) factors of 0.184 and 0.221, respectively PMID: 19167310
    10. The crystal structure of the complex of lactoperoxidase (LPO) with its physiological substrate thiocyanate (SCN(-)) has been determined at 2.4A resolution. PMID: 19339248
    11. The structures of three complexes of LPO with aromatic substrate, acetylsalicylic acid, and two aromatic inhibitors salicylhydroxamic acid and benzylhydroxamic acid indicate the distinctiveness in their modes of binding as a substrate and as an inhibitor. PMID: 19465478

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  • 亞細(xì)胞定位：
    Secreted.
  • 蛋白家族：
    Peroxidase family, XPO subfamily
  • 組織特異性：
    Mammary gland; milk.
  • 數(shù)據(jù)庫鏈接：

    KEGG: bta:280844

    STRING: 9913.ENSBTAP00000016986

    UniGene: Bt.4784