Amplite® Fluorimetric Lysyl Oxidase Assay Kit Red Fluorescence

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Spectral properties

Excitation (nm)	571
Emission (nm)	584

Storage, safety and handling

H-phrase	H303, H313, H333
Hazard symbol	XN
Intended use	Research Use Only (RUO)
R-phrase	R20, R21, R22
UNSPSC	12352200

Overview SDS Protocol

Excitation (nm)

571

Emission (nm)

584

Lysyl oxidase (LOX) is an extracellular enzyme that catalyzes formation of aldehydes from lysine residues in collagen and elastin precursors. These aldehydes are highly reactive, and undergo spontaneous chemical reactions with other lysyl oxidase-derived aldehyde residues, or with unmodified lysine residues. This results in cross-linking collagen and elastin which is essential for stabilization of collagen fibrils and for the integrity and elasticity of mature elastin. Lysyl oxidase has been identified as a possible tumor suppressor. Lysyl oxidase activity in biological samples is traditionally and most reliably assessed by tritium release end-point assays using radiolabeled collagen or elastin substrates involving laborious vacuum distillation of the released tritiated water. This kit offers a sensitive fluorescent assay to measure LOX activity using our proprietary LOX substrate that releases hydrogen peroxide upon LOX oxidation. The amount of hydrogen peroxide released by the LOX oxidation is detected using our Amplite® HRP substrate in the HRP-coupled reactions. This method allows the detection of sub ng/mL lysyl oxidase and is much more sensitive than the currently available fluorimetric assay for this enzyme activity. This method eliminates the interference that occurs in some biological samples and can be readily used to detect lysyl oxidase activity in cell culture experiments. Please note that the kit does not include the lysyl oxidase enzyme.

Platform

Fluorescence microplate reader

Excitation	540 nm
Emission	590 nm
Cutoff	570 nm
Recommended plate	Solid black

Components

Example protocol

AT A GLANCE

Protocol Summary

Prepare lysyl oxidase standards or test samples (50 µL)
Add lysyl oxidase working solution (50 µL)
Incubate at 37°C for 10 - 30 minutes
Monitor fluorescence intensity at Ex/Em = 540/590 nm

Important Thaw all the kit components at room temperature before starting the experiment.

CELL PREPARATION

For guidelines on cell sample preparation, please visit https://www.aatbio.com/resources/guides/cell-sample-preparation.html

PREPARATION OF STOCK SOLUTIONS

Unless otherwise noted, all unused stock solutions should be divided into single-use aliquots and stored at -20 °C after preparation. Avoid repeated freeze-thaw cycles.

1. Amplite™ HRP Substrate stock solution (250X)

Add 100 µL of DMSO (Component D) into the vial of Amplite™ HRP Substrate (Component A).
Note Amplite™ HRP Substrate is unstable in the presence of thiols such as DTT, glutathione (reduced form: GSH) and β-mercaptoethanol. The presence of thiols at concentration higher than 10 µM will significantly decrease the assay dynamic range. Some detergents (such as Brij-35, Tween-20 and NP40), NADH, and NADPH can also interfere with this assay.

2. Horseradish Peroxidase stock solution (50 U/mL)

Add 1 mL of Assay Buffer (Component B) into the vial of Horseradish Peroxidase (Component C).

PREPARATION OF STANDARD SOLUTION

For convenience, use the Serial Dilution Planner:
https://www.aatbio.com/tools/serial-dilution/15255

Lysyl Oxidase standard

Prepare lysyl oxidase standards by serial dilution to obtain standards from 0.04 to 4 µg/mL (LS1 - LS7).Note: Lysyl oxidase standard is not provided in this kit. It can be purchased from R&D Sytems (2639-AO-010 or 6069-AO-010).

PREPARATION OF WORKING SOLUTION

Amplite™ HRP Substrate working solution

Add 20 μL of Amplite™ HRP Substrate stock solution (250X) and 20 μL of Horseradish Peroxidase (50 U/mL) into 5 mL of Assay Buffer (Component B) to make a total volume of 5.04 mL.
Note The working solution is not stable, use it promptly and avoid direct exposure to light.

SAMPLE EXPERIMENTAL PROTOCOL

Table 1. Layout of lysyl oxidase standards and test samples in a solid black 96-well microplate. LS = lysyl oxidase standard (LS1-LS7, 0.04 to 4 µg/mL); BL = blank control; TS = test sample.

BL	BL	TS	TS
LS1	LS1	...	...
LS2	LS2	...	...
LS3	LS3
LS4	LS4
LS5	LS5
LS6	LS6
LS7	LS7

Table 2. Reagent composition for each well. Note that high concentration of Lysyl Oxidase may cause reduced fluorescence signal due to the over oxidation of Amplite™ HRP Substrate (to a non-fluorescent product). Lysyl Oxidase standards are for positive control only, and should not be relied on as a quantitation standard for enzyme activity.

Well	Volume	Reagent
LS1-LS7	50 µL	Serial Dilution (0.04 to 4 µg/mL)
BL	50 µL	Assay Buffer (Component B)
TS	50 µL	Test Sample

Lysyl Oxidase assay in supernatants

Prepare lysyl oxidase standards (LS), blank controls (BL) and test samples (TS) according to the layout provided in Table 1 and Table 2. For a 384-well plate, use 25 µL of each corresponding reagent instead of 50 µL.
Add 50 µL of lysyl oxidase working solution into each well of lysyl oxidase standard, blank control, and test samples to make the total lysyl oxidase assay volume of 100 µL/well. For a 384-well plate, add 25 µL of working solution into each well for a total volume of 50 µL.
Incubate the reaction at 37°C for 10 to 30 minutes, protected from light.
Monitor the fluorescence increase with a fluorescence plate reader at Ex/Em = 540/590 nm.
Note The contents of the plate can also be transferred to a white clear bottom plate and read by an absorbance microplate reader at the wavelength of 576 ± 5 nm. Note though that the absorption detection has lower sensitivity compared to fluorescence reading.

Lysyl Oxidase assay for cells

Prepare cells in a 96-well plate (50 - 100 µL/well), and activate the cells as desired. For a 384-well plate, use 25 µL/well instead. Harvest the cell media.
Note The negative controls (media alone and non-activated cells) are included for measuring background fluorescence.
Add 50 µL of lysyl oxidase working solution into each well of the cell media (from previous step) and well of lysyl oxidase standards (see Table 1). For a 384-well plate, add 25 µL of working solution into each well instead.
Incubate the reaction at 37°C for 10 to 30 minutes, protected from light.
Monitor the fluorescence increase with a fluorescence plate reader at Ex/Em = 530 to 570/590 to 600 nm (maximum Ex/Em = 540/590 nm, cut off 570 nm).

Spectrum

Open in Advanced Spectrum Viewer

Spectral properties

Excitation (nm)	571
Emission (nm)	584

Product Family

Name	Excitation (nm)	Emission (nm)
Amplite® Fluorimetric Glucose Oxidase Assay Kit Red Fluorescence	571	584
Amplite® Fluorimetric Glutamate Oxidase Assay Kit Red Fluorescence	571	584
Amplite® Fluorimetric Monoamine Oxidase Assay Kit Red Fluorescence	571	584
Amplite® Fluorimetric Xanthine Oxidase Assay Kit Red Fluorescence	571	584

Images

Figure 1. Lysyl oxidase dose response was measured with Amplite® Fluorimetric Lysyl Oxidase Assay Kit on a solid black 96-well plate using a Gemini fluorescence microplate reader (Molecular Devices).

Figure 2. Effect of LOX inhibition on LPS-induced EC inflammatory activation. Human pulmonary EC grown on 2.8(300 µM), and then stimulated with LPS (200 ng/ml) for 48 hrs with or without BAPN. A – IL-8 production by EC stimulated with or without BAPN was evaluated in conditioned medium by ELISA assay; *P<0.05. B – Expression of ICAM-1 and VCAM-1 was determined by western blot analysis with specific antibodies. C – ICAM-1 expression was examined by immunofluorescence staining of stimulated EC using ICAM-1 antibody (green). Counterstaining with DAPI (blue) was used to visualize cell nuclei. D – HPAEC were transfected with non-specific (nsRNA) or LOX-specific siRNA (si-LOX). ICAM-1 expression was determined by western blot. Equal protein loading was confirmed by membrane re-probing with β-actin antibody. LOX activity and interleukin-8 (IL-8) production in conditioned medium was measured using LOX activity assay (AAT Bioquest, Sunnyvale, CA) and IL-8 ELISA kit (R&D Systems, Minneapolis, MN), respectively, according to the manufacturers' instructions. Source: Graph from Stiffness-Activated GEF-H1 Expression Exacerbates LPS-Induced Lung Inflammation by Isa Mambetsariev et al., PLOS, Apr. 2014.

Figure 3. Effects of IL1β and TGFβ1 on the expression and activity level of lysyl oxidase in dermal and lung fibroblasts. (A–B) HDFa and HLFa were treated with IL1β, TGFβ1, or a combination of both, for 24 and 48 h. The mRNA levels of LOX were measured with qRT-PCR and expressed as fold change compared to untreated control. (C–D) Quantification of lysyl oxidase activity as secreted in the culture medium by HDFa and HLFa treated with IL1β, TGFβ1, or a combination of both for 24 and 48 h. LOX activity was determined with the Amplite Fluorimetric Lysyl Oxidase Assay Kit (AAT Bioquest Inc, USA) in accordance to the manufacturer's protocol. Source: Graph from Interleukin-1β Attenuates Myofibroblast Formation and Extracellular Matrix Production in Dermal and Lung Fibroblasts Exposed to Transforming Growth Factor-β1 by Masum M et al., PLOS, Mar. 2014.

Figure 4. Activity of lysyl oxidase (LOX) is increased in whole-lung tissues of chronically hypoxic mice and in culture media from human PASMC exposed to hypoxia or treated with CoCl2. Enzymatic activity of LOX was determined using Fluorimetric Lysyl Oxidase Assay Kit by monitoring LOX-catalyzed H2O2 release from the fluorescent substrate in HRP-coupled reaction. A: LOX activity in lung tissue homogenates from normoxic (Nor, room air for 5 weeks, nâ€Š=â€Š5) and hypoxic (Hyp, 10% O2 for 5 weeks, nâ€Š=â€Š5) mice. **P<0.01 vs. Nor. B: LOX activity in culture media collected from human PASMC after 24, 48 and 72 hrs of exposure to normoxia (Nor, 21% O2) or hypoxia (Hyp, 3% O2). *P<0.05, **P<0.01 vs. Nor. C: LOX activity in culture media collected from PASMC treated with vehicle (Cont) or CoCl2 (100 µM for 48 hrs). **P<0.01 vs. Cont. Each bar graph displays the Cu-dependent activity of LOX determined by subtracting values obtained in the presence of BCS (a Cu chelator) from values in the absence of BCS. LOX activity is expressed in nanomoles of H2O2 released from the cells and normalized to the amount of total protein in each sample. Data are shown as mean±SE. Activity in the conditioned media and the cell extracts was measured using the Fluorimetric Lysyl Oxidase Assay Kit (AAT Bioquest, Inc., prod. no. 15255). Source: Graph from Upregulated Copper Transporters in Hypoxia-Induced Pulmonary Hypertension by Adriana M. Zimnicka et al., PLOS, Mar. 2014.

Figure 5. Atox1 is required for ECM maturation and Cu enzyme LOX activation. (A,B) Masson’s Trichrome staining, scale bars = 500 μm (A) and LOX activity (B) in wound tissues at day 7 after wounding in WT and Atox1^−/− mice. In (A) boxed regions are shown at higher magnification to the right, scale bars = 100 μm. Blue color indicates the collagen deposition; light red or pink for keratin, muscle or cytoplasm; and dark brown or black for cell nuclei. W: wound area; WE: wound edge In (B) a graph represents mean ± SE for LOX activity and a western blot represents Pro-LOX protein expression in wound tissues at days 0 and 7 (n = 3. **p < 0.01 vs. WT). (C) Schematic diagram showing the essential role of Cu-dependent transcription factor and Cu chaperone function of Atox1 in Cu-dependent wound healing. Source: Endothelial Antioxidant-1: a Key Mediator of Copper-dependent Wound Healing in vivo by Das et al., Scientific Reports, Sept. 2016.

Atox1 promotes angiogenesis via activating Cu enzyme lysyl oxidase in ECs in an ATP7A-dependent manner. (A) Sponge implant assay was performed by implanting polyvinyl alcohol sponge containing VEGF subcutaneously into WT and Atox1 KO mice. Representative images for H&E staining and isolectin immunostaining for blood vessel formation in sponges harvested on day 21. Right panels show quantitative analysis of the number of red blood cells (RBC) and isolection+ ECs. Scale bars = 50μm. (B) HUVECs were transfected with control, Atox1 or ATP7A siRNAs or treated with Cu chelator TTM (20 nM, 24 hrs) and seeded on Matrigel-coated plates in culture media containing VEGF for 6 h. Four random fields per well were imaged, and representative pictures are shown (left). Averaged numbers of capillary tube branches, branching points, and tube length per field are shown (Right). (C) HUVECs were treated with LOX inhibitor β-aminopropionitrile (BAPN, 100 μM) for 24 hrs and capillary tube formation was measured (n = 3). (D) Activity of LOX was measured in ischemic gastrocnemius muscle of WT and Atox1 KO mice (left)(n = 4) or in culture medium from VEGF (20ng/ml)-stimulated HUVECs transfected with siControl or siAtox1 (right)(n = 4). *p < 0.05.  Source:  <strong>Copper Transport Protein Antioxidant-1 Promotes Inflammatory Neovascularization via Chaperone and Transcription Factor Function</strong> by Chen et al., <em>Scientific Reports</em>, Oct. 2015.

Figure 6. Atox1 promotes angiogenesis via activating Cu enzyme lysyl oxidase in ECs in an ATP7A-dependent manner. (A) Sponge implant assay was performed by implanting polyvinyl alcohol sponge containing VEGF subcutaneously into WT and Atox1 KO mice. Representative images for H&E staining and isolectin immunostaining for blood vessel formation in sponges harvested on day 21. Right panels show quantitative analysis of the number of red blood cells (RBC) and isolection+ ECs. Scale bars = 50μm. (B) HUVECs were transfected with control, Atox1 or ATP7A siRNAs or treated with Cu chelator TTM (20 nM, 24 hrs) and seeded on Matrigel-coated plates in culture media containing VEGF for 6 h. Four random fields per well were imaged, and representative pictures are shown (left). Averaged numbers of capillary tube branches, branching points, and tube length per field are shown (Right). (C) HUVECs were treated with LOX inhibitor β-aminopropionitrile (BAPN, 100 μM) for 24 hrs and capillary tube formation was measured (n = 3). (D) Activity of LOX was measured in ischemic gastrocnemius muscle of WT and Atox1 KO mice (left)(n = 4) or in culture medium from VEGF (20ng/ml)-stimulated HUVECs transfected with siControl or siAtox1 (right)(n = 4). *p < 0.05. Source: Copper Transport Protein Antioxidant-1 Promotes Inflammatory Neovascularization via Chaperone and Transcription Factor Function by Chen et al., Scientific Reports, Oct. 2015.

$Processing by FXa does not influence the activity of soluble LOXL2. a Schematic of LOXL2 mutants used with predicted molecular weights in parenthesis and b representative Western blotting image of HEK293 cells overexpressing WT-LOXL2, LOXL2-DM, and ΔN-LOXL2 by transfection in the cytosol, conditioned media, and ECM. Equal amounts of protein were loaded for the cytosol, and a normalized volume of ECM and conditioned media proteins based on the cytosolic protein concentration were loaded on gels. c LOX activity in conditioned media measured by Amplite Fluorimetric LOX assay kit under indicated conditions. LOX activity was normalized to the average of AdLOXL2 condition. Data are shown as mean ± SEM (n ≥ 6, ****P < 0.0001 by one-way ANOVA). d Representative Western blot of LOXL2 expression in the cell-culture media used for the Amplex Red activity assay. e LOX activity in the cytosolic fraction measured by Amplite Fluorimetric LOX assay kit under indicated conditions. LOX activity was normalized to the average of AdLOXL2 condition. Data are shown as mean ± SEM (n = 3 **p < 0.01, ***p < 0.001 by one-way ANOVA). Source: <b>Lysyl oxidase-like 2 processing by factor Xa modulates its activity and substrate preference</b> by Huilei Wang, Alan Poe, Marta Martinez Yus, Lydia Pak, Kavitha Nandakumar & Lakshmi Santhanam. <em>Communications Biology</em>. April 2023.$

Figure 7. Processing by FXa does not influence the activity of soluble LOXL2. a Schematic of LOXL2 mutants used with predicted molecular weights in parenthesis and b representative Western blotting image of HEK293 cells overexpressing WT-LOXL2, LOXL2-DM, and ΔN-LOXL2 by transfection in the cytosol, conditioned media, and ECM. Equal amounts of protein were loaded for the cytosol, and a normalized volume of ECM and conditioned media proteins based on the cytosolic protein concentration were loaded on gels. c LOX activity in conditioned media measured by Amplite Fluorimetric LOX assay kit under indicated conditions. LOX activity was normalized to the average of AdLOXL2 condition. Data are shown as mean ± SEM (n ≥ 6, ****P < 0.0001 by one-way ANOVA). d Representative Western blot of LOXL2 expression in the cell-culture media used for the Amplex Red activity assay. e LOX activity in the cytosolic fraction measured by Amplite Fluorimetric LOX assay kit under indicated conditions. LOX activity was normalized to the average of AdLOXL2 condition. Data are shown as mean ± SEM (n = 3 **p < 0.01, ***p < 0.001 by one-way ANOVA). Source: Lysyl oxidase-like 2 processing by factor Xa modulates its activity and substrate preference by Huilei Wang, Alan Poe, Marta Martinez Yus, Lydia Pak, Kavitha Nandakumar & Lakshmi Santhanam. Communications Biology. April 2023.

LOXL2 processing by FXa reduces total LOX activity in the cell-derived ECM. Representative confocal microscopy images of in situ LOXs activity (green), LOXL2 (red), and nuclei (DAPI, blue) for the following conditions: (1) control A7r5s cells, (2) ΔN-LOXL2 overexpression, (3) wild-type LOXL2 overexpression (4) LOXL2 overexpression with FXa incubation (1 μg/ml), (5) LOXL2 overexpression with FXa (1 μg/ml) and rivaroxaban (50 nM) incubation, (6) catalytically inactive LOXL2-DM overexpression, (7) LOXL2 overexpression + LOXL2-specific inhibitor PAT-1251 (10 µM), (8) LOXL2 overexpression + inhibitors BAPN (10 µM) + PAT-1251 (10 µM). (Scale bar = 50 μm). Source: <b>Lysyl oxidase-like 2 processing by factor Xa modulates its activity and substrate preference</b> by Huilei Wang, Alan Poe, Marta Martinez Yus, Lydia Pak, Kavitha Nandakumar & Lakshmi Santhanam. <em>Communications Biology</em>. April 2023.

Figure 8. LOXL2 processing by FXa reduces total LOX activity in the cell-derived ECM. Representative confocal microscopy images of in situ LOXs activity (green), LOXL2 (red), and nuclei (DAPI, blue) for the following conditions: (1) control A7r5s cells, (2) ΔN-LOXL2 overexpression, (3) wild-type LOXL2 overexpression (4) LOXL2 overexpression with FXa incubation (1 μg/ml), (5) LOXL2 overexpression with FXa (1 μg/ml) and rivaroxaban (50 nM) incubation, (6) catalytically inactive LOXL2-DM overexpression, (7) LOXL2 overexpression + LOXL2-specific inhibitor PAT-1251 (10 µM), (8) LOXL2 overexpression + inhibitors BAPN (10 µM) + PAT-1251 (10 µM). (Scale bar = 50 μm). Source: Lysyl oxidase-like 2 processing by factor Xa modulates its activity and substrate preference by Huilei Wang, Alan Poe, Marta Martinez Yus, Lydia Pak, Kavitha Nandakumar & Lakshmi Santhanam. Communications Biology. April 2023.

Citations

View all 54 citations: Citation Explorer

HCG supplement did not accelerate tunica albuginea remodeling to facilitate penile growth
Authors: Li, Tao and Tian, Yuan and Zhong, Quliang and Chen, Peng and Zhang, Junhao and Du, Guangshi and Li, Lei and Jiang, Yiting and Jiang, Kehua
Journal: Scientific Reports (2023): 16519

Triptolide attenuates pulmonary fibrosis by inhibiting fibrotic extracellular matrix remodeling mediated by MMPs/LOX/integrin
Authors: Lin, Weiji and Song, Yaqin and Li, Tingting and Yan, Jiahui and Zhang, Ruiyuan and Han, Liang and Ba, Xin and Huang, Yao and Qin, Kai and Chen, Zhe and others,
Journal: Biomedicine \& Pharmacotherapy (2023): 115394

Lysyl oxidase-like 2 processing by factor Xa modulates its activity and substrate preference
Authors: Wang, Huilei and Poe, Alan and Martinez Yus, Marta and Pak, Lydia and Nandakumar, Kavitha and Santhanam, Lakshmi
Journal: Communications Biology (2023): 375

Cysteine oxidation of copper transporter CTR1 drives VEGFR2 signalling and angiogenesis
Authors: Das, Archita and Ash, Dipankar and Fouda, Abdelrahman Y and Sudhahar, Varadarajan and Kim, Young-Mee and Hou, Yali and Hudson, Farlyn Z and Stansfield, Brian K and Caldwell, Ruth B and McMenamin, Malgorzata and others,
Journal: Nature Cell Biology (2022): 1--16

Exposure to oxLDL impairs TGF-$\beta$ activity in human tendon cells
Authors: Mousavizadeh, Rouhollah and Waugh, Charlie M and DeBruin, Erin and McCormack, Robert G and Duronio, Vincent and Scott, Alex
Journal: (2022)

Androgen supplement did not accelerate tunica albuginea remodeling to facilitate penile growth
Authors: Sun, Fa and Li, Tao and Jiang, Yiting and Jiang, Kehua and Tian, Ye and Wang, Zhen and Ban, Yong and Gu, Jiang
Journal: (2022)

Lysyl oxidase directly contributes to extracellular matrix production and fibrosis in systemic sclerosis
Authors: Nguyen, Xinh-Xinh and Nishimoto, Tetsuya and Takihara, Takahisa and Mlakar, Logan and Bradshaw, Amy D and Feghali-Bostwick, Carol
Journal: American Journal of Physiology-Lung Cellular and Molecular Physiology (2021): L29--L40

The P-type ATPase transporter ATP7A promotes angiogenesis by limiting autophagic degradation of VEGFR2
Authors: Ash, Dipankar and Sudhahar, Varadarajan and Youn, Seock-Won and Okur, Mustafa Nazir and Das, Archita and O’Bryan, John P and McMenamin, Maggie and Hou, Yali and Kaplan, Jack H and Fukai, Tohru and others,
Journal: Nature communications (2021): 1--16

An in situ activity assay for lysyl oxidases
Authors: Huilei, Wang and Poe, Alan and Pak, Lydia and Kavitha, Nandakumar and Sandeep, Jandu and Jochen, Steppan and Reik, L{\"o}ser and Lakshmi, Santhanam
Journal: Communications Biology (2021)

An In Situ Activity Assay For Lysyl Oxidases
Authors: Wang, Huilei and Poe, Alan and Pak, Lydia and Nandakumar, Kavitha and Jandu, Sandeep and Steppan, Jochen and L{\"o}ser, Reik and Santhanam, Lakshmi
Journal: Communications biology (2021): 1--10

References

View all 21 references: Citation Explorer

Overexpression of lysyl oxidase to increase matrix crosslinking and improve tissue strength in dermal wound healing
Authors: Lau YK, Gobin AM, West JL.
Journal: Ann Biomed Eng (2006): 1239

Cellular fibronectin binds to lysyl oxidase with high affinity and is critical for its proteolytic activation
Authors: Fogelgren B, Polgar N, Szauter KM, Ujfaludi Z, Laczko R, Fong KS, Csiszar K.
Journal: J Biol Chem (2005): 24690

The Pro-regions of lysyl oxidase and lysyl oxidase-like 1 are required for deposition onto elastic fibers
Authors: Thomassin L, Werneck CC, Broekelmann TJ, Gleyzal C, Hornstra IK, Mecham RP, Sommer P.
Journal: J Biol Chem (2005): 42848

A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and tumor progression
Authors: Peinado H, Del Carmen Iglesias-de la Cruz M, Olmeda D, Csiszar K, Fong KS, Vega S, Nieto MA, Cano A, Portillo F.
Journal: Embo J (2005): 3446

Lysyl oxidase is essential for normal development and function of the respiratory system and for the integrity of elastic and collagen fibers in various tissues
Authors: Maki JM, Sormunen R, Lippo S, Kaarteenaho-Wiik R, Soininen R, Myllyharju J.
Journal: Am J Pathol (2005): 927

Inhibition of lysyl oxidase activity can delay phenotypic modulation of chondrocytes in two-dimensional culture
Authors: Farjanel J, Seve S, Borel A, Sommer P, Hulmes DJ.
Journal: Osteoarthritis Cartilage (2005): 120

A peptide model of the copper-binding region of lysyl oxidase
Authors: Ryvkin F, Greenaway FT.
Journal: J Inorg Biochem (2004): 1427

The propeptide domain of lysyl oxidase induces phenotypic reversion of ras-transformed cells
Authors: Palamakumbura AH, Jeay S, Guo Y, Pischon N, Sommer P, Sonenshein GE, Trackman PC.
Journal: J Biol Chem (2004): 40593

Elastic fiber homeostasis requires lysyl oxidase-like 1 protein
Authors: Liu X, Zhao Y, Gao J, Pawlyk B, Starcher B, Spencer JA, Yanagisawa H, Zuo J, Li T.
Journal: Nat Genet (2004): 178

Enhancing mechanical properties of tissue-engineered constructs via lysyl oxidase crosslinking activity
Authors: Elbjeirami WM, Yonter EO, Starcher BC, West JL.
Journal: J Biomed Mater Res A (2003): 513

Documents

Safety data sheet
Product protocol
Certificate of analysis

Application notes

Endothelial Antioxidant-1: a Key Mediator of Copper-dependent Wound Healing in vivo
Stiffness-Activated GEF-H1 Expression Exacerbates LPS-Induced Lung Inflammation
The role of lysyl oxidase family members in the stabilization of abdominal aortic aneurysms
LOX Fails to Substitute for RANKL in Osteoclastogenesis
Copper Transport Protein Antioxidant-1 Promotes Inflammatory Neovascularization via Chaperone and Transcription Factor Function

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BL	BL	TS	TS
LS1	LS1	...	...
LS2	LS2	...	...
LS3	LS3
LS4	LS4
LS5	LS5
LS6	LS6
LS7	LS7

BL	BL	TS	TS
LS1	LS1	...	...
LS2	LS2	...	...
LS3	LS3
LS4	LS4
LS5	LS5
LS6	LS6
LS7	LS7

Amplite® Fluorimetric Lysyl Oxidase Assay Kit *Red Fluorescence*

OverviewSDSProtocol

Platform

Fluorescence microplate reader

Components

Example protocol

AT A GLANCE

CELL PREPARATION

PREPARATION OF STOCK SOLUTIONS

PREPARATION OF STANDARD SOLUTION

PREPARATION OF WORKING SOLUTION

SAMPLE EXPERIMENTAL PROTOCOL

Spectrum

Spectral properties

Product Family

Images

Citations

References

Documents

Application notes

FAQ

AssayWise

Amplite® Fluorimetric Lysyl Oxidase Assay Kit Red Fluorescence

Overview SDS Protocol

BL	BL	TS	TS
LS1	LS1	...	...
LS2	LS2	...	...
LS3	LS3
LS4	LS4
LS5	LS5
LS6	LS6
LS7	LS7