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Rabbit anti gfp ab6556

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Rabbit anti-GFP (ab6556) is a primary antibody that specifically recognizes green fluorescent protein (GFP). It is produced in rabbits and can be used for the detection and localization of GFP in various applications.

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Lab products found in correlation

Rat anti mouse cd45, by BD (1 mentions) Alexa fluor 488 donkey anti rabbit igg, by Thermo Fisher Scientific (1 mentions) Alexa fluor 488 phalloidin, by Thermo Fisher Scientific (1 mentions) Alexa fluor 594 donkey anti rat igg, by Thermo Fisher Scientific (1 mentions) Mouse anti flag m2, by Merck Group (1 mentions)

2 protocols using rabbit anti gfp ab6556

1

Immunofluorescence Staining of Mouse Cells

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Rat anti-mouse CD54 (intracellular adhesion molecule 1 (ICAM-1)) antibody (clone #: YN1/1.7.4, rat IgG2b, κ) was purchased from BioLegend (San Diego, CA, U.S.A.). Rat anti-mouse CD45 (clone #: 30-F11) was obtained from BD Biosciences Pharmingen (San Diego, CA, U.S.A.). Rabbit anti-GFP (ab6556) was purchased from Abcam (Cambridge, MA, U.K.). Alexa Fluor® 594 Donkey anti-Rat IgG, Alexa Fluor®488 Donkey anti-Rabbit IgG and Alexa Fluor®488 phalloidin were sourced from Molecular Probes (Invitrogen, U.S.A.). Recombinant mouse IL-1β and MCP-1 were purchased from PROSPEC (East Brunswick, NJ, U.S.A.). Recombinant human fibroblast growth factor 2 (rhFGF-2) was obtained from Miltenyi Biotec (Bergisch-Gladbach, Germany).
Ibi M., Horie S., Kyakumoto S., Chosa N., Yoshida M., Kamo M., Ohtsuka M, & Ishisaki A. (2018). Cell–cell interactions between monocytes/macrophages and synoviocyte-like cells promote inflammatory cell infiltration mediated by augmentation of MCP-1 production in temporomandibular joint. Bioscience Reports, 38(2), BSR20171217.
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2

Western Blot Antibody Protocol

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Primary antibodies for western blotting were mouse anti-FLAG M2 (Sigma) and rabbit anti-GFP ab6556 (Abcam). Secondary antibodies were horseradish peroxidase conjugated anti-mouse or anti-rabbit IgGs (GE Healthcare).
Richards M.W., O'Regan L., Roth D., Montgomery J.M., Straube A., Fry A.M, & Bayliss R. (2015). Microtubule association of EML proteins and the EML4-ALK variant 3 oncoprotein require an N-terminal trimerization domain. The Biochemical journal, 467(3).
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