Rabbit anti shp 1

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Rabbit anti-SHP-1 is a primary antibody that recognizes the SHP-1 protein. SHP-1 is a protein tyrosine phosphatase that plays a key role in the negative regulation of cell signaling pathways. This antibody can be used for the detection and analysis of SHP-1 expression in various experimental systems.

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Lab products found in correlation

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2 protocols using rabbit anti shp 1

Protein Expression Analysis in Stem Cells

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Unless otherwise indicated, reagents were purchased from Sigma Chemical Co. (St. Louis, MO, USA). Rabbit anti-SHP-1 was obtained from Santa Cruz Biotechnology (Santa Cruz, CA, USA), and a mouse anti-Nanog polyclonal antibody was obtained from Bethyl Laboratories (Montgomery, TX, USA). Rabbit anti-STAT3 antibody was purchased from Merck Millipore (Millipore Chemicals, MA, USA) and a rabbit anti-phospho-STAT3 antibody was purchased from Cell Signaling Technology (Beverly, MA, USA). Mouse anti-GAPDH polyclonal antibody was purchased from beyotime (Beyotime, Shanghai, China). Secondary antibodies for ICC were alexa fluor 488-labeled goat anti-Rabbit IgG and cy3-labeled goat anti-mouse IgG purchased from beyotime (Beyotime, Shanghai, China). Secondary antibodies for Western were goat anti-rabbit IgG-HRP and goat anti-mouse IgG-HRP purchased from beyotime (Beyotime, Shanghai, China).

Yin S., Wu H., Lv J., Wu X., Zhang Y., Du J, & Zhang Y. (2014). SHP-1 Arrests Mouse Early Embryo Development through Downregulation of Nanog by Dephosphorylation of STAT3. PLoS ONE, 9(1), e86330.

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Siglec-9 Interaction with SHP-1 in Neutrophils

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Human neutrophils were seeded into 6-well plates at 1.2 × 10⁷ cells and pretreated in the presence/absence HMW-HA and ± 25 nM of phorbol −12myristate 13-acetate (PMA). Protein concentration was normalized to 1 mg and immunoprecipitation performed using goat anti-Siglec-9, (R&D Systems #BAF1139) at 2 µg/ml in the presence of 5x protease inhibitor cocktail, phosphatase inhibitors (50 mM Na₃O₄V,10 mM NaF, 20 mM imidazole, 5 mM Na Molybdate) and 5 mU micrococcal nuclease for 12 h at 4°C. The next day, protein-G Sepharose beads were added for 3 h at 4°C. Proteins were separed by reducing SDS-PAGE, transferred to PVDF and probed with anti-Siglec-9 (R&D Systems #BAF1139) and rabbit anti-SHP-1 (Santa Cruz Biotechnology #sc-287) an appropriate HRP-conjugated secondary antibody and quimioluminicence substrate (Thermo Scientific).

Secundino I., Lizcano A., Roupé K.M., Wang X., Cole J.N., Olson J., Ali S.R., Dahesh S., Amayreh L.K., Henningham A., Varki A, & Nizet V. (2015). Host and Pathogen Hyaluronan Signal Through Human Siglec-9 to Suppress Neutrophil Activation. Journal of molecular medicine (Berlin, Germany), 94(2), 219-233.

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