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Heated citrate buffer

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Heated citrate buffer is a laboratory solution used to maintain a specific pH range for various biological and chemical applications. It provides a controlled environment to facilitate chemical reactions, sample preparation, or preservation of biological materials.

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Lab products found in correlation

Rabbit anti phospho cmet, by R&D Systems (2 mentions) Non immune mouse igg, by Merck Group (2 mentions) Mouse anti matriptase, by R&D Systems (2 mentions) Rabbit anti phospho cmet, by Abcam (2 mentions) Goat anti c met, by R&D Systems (2 mentions) Rabbit anti c met, by Leica (2 mentions)

2 protocols using heated citrate buffer

1

Immunohistochemical Analysis of Breast Cancer

Check if the same lab product or an alternative is used in the 5 most similar protocols
The use of human tissue paraffin embedded samples was approved according to the Institutional Review Board Administration. The “BC20812 and “BRC711” breast cancer tissue arrays with pathology grading were obtained from US Biomax, Inc. (Rockville, MD). Grade II and III tumors were analyzed in this study. Tissue arrays were deparaffinized with xylene and hydrated with graded ethanol solutions. Antigen retrieval was performed using heated citrate buffer, reduced pH (Bethyl Laboratories, Montgomery, TX). The arrays were blocked with 2 % bovine serum albumin in PBS, and immunostained overnight at 4°C5 (link). Primary antibodies were mouse anti-matriptase (1:200), goat anti-c-Met (1:200) and rabbit anti-phospho-cMet (1:200) (R&D Systems, Minneapolis, MN), rabbit anti-matriptase (1:100) (Calbiochem/EMD Millipore, San Diego, CA), rabbit anti c-Met (1:30)(Leica Microsystems Inc., Buffalo Grove, IL) and rabbit anti-phospho-cMet (1:200) (Abcam, Cambridge, MA). As negative controls, non-immune mouse IgG, rabbit IgG or goat IgG were used (Sigma, St. Louis, MO) (adjusted to same final concentration as specific primary antibodies).
Zoratti G.L., Tanabe L.M., Varela F.A., Murray A.S., Bergum C., Colombo E., Lang J., Molinolo A.A., Leduc R., Marsault E., Boerner J, & List K. (2015). Targeting matriptase in breast cancer abrogates tumor progression via impairment of stromal-epithelial growth factor signaling. Nature communications, 6, 6776.
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2

Immunohistochemical Analysis of Breast Cancer

Check if the same lab product or an alternative is used in the 5 most similar protocols
The use of human tissue paraffin embedded samples was approved according to the Institutional Review Board Administration. The “BC20812 and “BRC711” breast cancer tissue arrays with pathology grading were obtained from US Biomax, Inc. (Rockville, MD). Grade II and III tumors were analyzed in this study. Tissue arrays were deparaffinized with xylene and hydrated with graded ethanol solutions. Antigen retrieval was performed using heated citrate buffer, reduced pH (Bethyl Laboratories, Montgomery, TX). The arrays were blocked with 2 % bovine serum albumin in PBS, and immunostained overnight at 4°C5 (link). Primary antibodies were mouse anti-matriptase (1:200), goat anti-c-Met (1:200) and rabbit anti-phospho-cMet (1:200) (R&D Systems, Minneapolis, MN), rabbit anti-matriptase (1:100) (Calbiochem/EMD Millipore, San Diego, CA), rabbit anti c-Met (1:30)(Leica Microsystems Inc., Buffalo Grove, IL) and rabbit anti-phospho-cMet (1:200) (Abcam, Cambridge, MA). As negative controls, non-immune mouse IgG, rabbit IgG or goat IgG were used (Sigma, St. Louis, MO) (adjusted to same final concentration as specific primary antibodies).
Zoratti G.L., Tanabe L.M., Varela F.A., Murray A.S., Bergum C., Colombo E., Lang J., Molinolo A.A., Leduc R., Marsault E., Boerner J, & List K. (2015). Targeting matriptase in breast cancer abrogates tumor progression via impairment of stromal-epithelial growth factor signaling. Nature communications, 6, 6776.
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