Bovine lactoperoxidase (LPO) ELISA kit

Code CSB-EL013066BO
Size 96T,5×96T,10×96T
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Product Details

Target Name
lactoperoxidase
Alternative Names
LPO ELISA Kit; Lactoperoxidase ELISA Kit; LPO ELISA Kit; EC 1.11.1.7 ELISA Kit
Abbreviation
LPO
Uniprot No.
Species
Bos taurus (Bovine)
Sample Types
breast milk
Detection Range
1.56 mU/mL-100 mU/mL
Sensitivity
1.56 mU/mL
Assay Time
1-5h
Sample Volume
50-100ul
Detection Wavelength
450 nm
Research Area
Cancer
Assay Principle
quantitative
Measurement
Competitive
Precision
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.
Typical Data
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
Troubleshooting
and FAQs
Storage
Store at 2-8°C. Please refer to protocol.
Lead Time
3-5 working days after you place the order, and it takes another 3-5 days for delivery via DHL or FedEx
Description

This Bovine LPO ELISA Kit was designed for the quantitative measurement of Bovine LPO protein in breast milk. It is a Competitive ELISA kit, its detection range is 1.56 mU/mL-100 mU/mL and the sensitivity is 1.56 mU/mL.

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Target Background

Function
(From Uniprot)
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.
Gene References into Functions
  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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Subcellular Location
Secreted.
Protein Families
Peroxidase family, XPO subfamily
Tissue Specificity
Mammary gland; milk.
Database Links
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