Anti lox antibody

Manufactured by Abcam

Sourced in United Kingdom, United States

The Anti-LOX antibody is a laboratory research tool that specifically binds to and detects the Lysyl Oxidase (LOX) protein. LOX is an enzyme involved in the cross-linking of collagen and elastin, which are important structural components of the extracellular matrix. This antibody can be used in various experimental techniques, such as Western blotting and immunohistochemistry, to study the expression and localization of the LOX protein.

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Lab products found in correlation

Imagescope software, by Leica (2 mentions) Dako envision system hrp, by Agilent Technologies (1 mentions) Scanscope xt digital slide scanner, by Leica (1 mentions) Anti snai2, by Abcam (1 mentions) Horseradish peroxidase conjugated goat anti rabbit igg antibody, by ZSGB-BIO (1 mentions) Anti collagen type 1 antibody, by Abcam (1 mentions) Bovine serum albumin (bsa), by Merck Group (1 mentions) Nb100 417, by Novus Biologicals (1 mentions)

4 protocols using anti lox antibody

Immunohistochemical Analysis of LOX in Thyroid Carcinoma

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Sections were deparaffinized and rehydrated, and antigen retrieval was performed with citrate buffer in a water bath at 120°C. The sections were incubated with the anti-LOX antibody (1:100, Abcam) overnight at 4°C, followed by incubation with a biotinylated secondary antibody for 1 hour at room temperature. The slides were developed with DAB [Dako EnVision+ system HRP (DAB), Dako] and counterstained with hematoxylin. The slides were scanned at ×20 magnification using a ScanScope XT digital slide scanner (Aperio Technologies, Inc.) to create whole-slide image data files at 0.5 μm/pixel resolution and viewed using ImageScope software (Aperio Technologies).
Tissue microarrays were purchased from US Biomax (#TH641). This array included duplicates of six follicular adenomas, six follicular thyroid carcinomas, six papillary thyroid carcinomas, six anaplastic thyroid carcinomas, and 16 normal tissues from lungs, thyroid, and testis.

Boufraqech M., Nilubol N., Zhang L., Gara S.K., Sadowski S.M., Mehta A., He M., Davis S., Dreiling J., Copland J.A., Smallridge R.C., Quezado M.M, & Kebebew E. (2014). miR30a Inhibits LOX Expression and Anaplastic Thyroid Cancer Progression. Cancer research, 75(2), 367-377.

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Immunohistochemical Analysis of Thyroid Cancer Markers

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Sections were deparaffinized and rehydrated, and antigen retrieval was performed with citrate buffer in a water bath at 120°C. The sections were incubated with the anti-LOX antibody (1:100; Abcam), anti-SNAI2 or anti-TIMP4 (1:100, Abcam) overnight at 4°C, followed by incubation with a biotinylated secondary antibody for 1 hour at room temperature. The slides were developed with diaminobenzidine [DAB; EnVision+ Kit system HRP (DAB), Dako] and counterstained with hematoxylin. The slides were scanned at a 20× magnification using a ScanScope XT digital slide scanner (Aperio Technologies, Leica) to create whole-slide image data files at a resolution of 0.5 μm/pixel, and they were viewed using ImageScope software (Aperio Technologies).
Tissue microarrays were purchased from US Biomax (#TH641). These arrays included duplicates of six follicular adenomas, six follicular thyroid carcinomas, six papillary thyroid carcinomas, six anaplastic thyroid carcinomas, and 16 normal tissues from lung, thyroid, and testis.

Boufraqech M., Zhang L., Nilubol N., Sadowski S.M., Kotian S., Quezado M, & Kebebew E. (2016). Lysyl Oxidase (LOX) Transcriptionally Regulates SNAI2 Expression and TIMP4 Secretion in Human Cancers. Clinical cancer research : an official journal of the American Association for Cancer Research, 22(17), 4491-4504.

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Immunohistochemistry of Colorectal Cancer

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For immunohistochemical staining, 4-μm sections of the human colorectal cancer tissue arrays were used. Briefly, the slides were subsequently dewaxed, rehydrated, and incubated in 3% peroxide-methanol at 37 °C for 30 minutes to quench endogenous peroxidase. Next, the sections were treated with 10% bovine serum albumin (Sigma-Aldrich, St Louis, MO, USA) to block the non-specific binding and incubated with anti-collagen type I antibody (1:100 dilution, Abcam, Cambridge, CB, UK) or anti-LOX antibody (1:100 dilution, Abcam) overnight at 4 °C. The slides were then incubated with a horseradish peroxidase-conjugated goat anti-rabbit IgG antibody (ZSGB-BIO, Beijing, China) at 37 °C for 50 minutes. All the sections were stained with diaminobenzidine solution (DAB, Dako Cytomation, Hamburg, Germany) and counterstained with hematoxylin. The images were analyzed to quantify the LOX expression using IPP (version 6.0) under a 400× objective field. The images were evaluated by two experimenters.

Wei B., Zhou X., Liang C., Zheng X., Lei P., Fang J., Han X., Wang L., Qi C, & Wei H. (2017). Human colorectal cancer progression correlates with LOX-induced ECM stiffening. International Journal of Biological Sciences, 13(11), 1450-1457.

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Immunohistochemical Evaluation of LOX and CA9

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An anti-LOX antibody (Abcam, Cambridge, MA, USA) and an anti-carbonic anhydrase 9 (CA9) antibody (1: 1000; NB 100-417, Novus Biologicals, Littleton, CO, USA) were used. The methods used for the immunohistochemical determination are described in the kit manufacturer's instructions, as previously reported [14] . LOX expression was evaluated by the intensity of staining and the percentage of stained cancer cells at the invading tumor front: intensity was given a score ranging from 0 to 2 (0 = no intensity, 1 = weak to moderate intensity, 2 = intense intensity), and the percentage of immunopositive cells was given a score ranging from 0 to 4 (0 = 0 %, 1 = 1-30 %, 2 = 31-60 %, 3 = 61-80 %, 4 = 81-100 %). The two scores were multiplied to obtain the final result, ranging from 0 to 8. Expression was considered positive when the scores was 5 or more and was considered negative when the score was 4 or less. CA9 expression was evaluated as previously reported [41] . Evaluation was done by two double-blinded independent observers who were unaware of the clinical data and outcome. When there was a discrepant evaluation between the two independent observers, the evaluation was rechecked and discussed.

Kasashima H., Yashiro M., Kinoshita H., Fukuoka T., Morisaki T., Masuda G., Sakurai K., Kubo N., Ohira M, & Hirakawa K. (2016). Lysyl oxidase is associated with the epithelial-mesenchymal transition of gastric cancer cells in hypoxia. Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association, 19(2).

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