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Rat anti gfp clone 3h9

Manufactured by Proteintech
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The Rat anti-GFP (clone 3H9) is a primary antibody that recognizes the green fluorescent protein (GFP). It can be used to detect and visualize GFP-tagged proteins in various applications.

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Lab products found in correlation

Rat anti myc clone 9e1, by Proteintech (2 mentions) Anti tbc1d5, by Proteintech (1 mentions) Mouse anti gapdh, by Proteintech (1 mentions) Gfp trap, by Proteintech (1 mentions) Rfp trap, by Proteintech (1 mentions) Camptothecin, by Bio-Techne (1 mentions) Rabbit anti gapdh antibody, by Santa Cruz Biotechnology (1 mentions) Actinomycin d, by Merck Group (1 mentions) Ab15309, by Abcam (1 mentions) Ab97545, by Abcam (1 mentions) Ab98929, by Abcam (1 mentions) Ab77799, by Abcam (1 mentions) Ab181352, by Abcam (1 mentions) Ab131238, by Abcam (1 mentions) Ab24170, by Abcam (1 mentions) Mouse anti gapdh 10494 1 ap, by Proteintech (1 mentions) Rabbit anti igf1rβ, by Cell Signaling Technology (1 mentions)

4 protocols using rat anti gfp clone 3h9

1

Western Blot Analysis of Vpu Expression

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TZM-bl cells were transfected with 3 μg Vpu expression plasmid using polyethylenimine (PEI), harvested 24 h post-transfection and lysed in SDS-sample buffer. Proteins were separated on 12.5% SDS-PAGE and blotted onto nitrocellulose membranes. Blocked membranes were probed with the following primary antibodies: rabbit polyclonal anti-Vpu (Vpu-101AP, Fab Gennix), rat anti-GFP (clone 3H9, Chromotek), monoclonal mouse anti-transferrin receptor (Tfr) (clone H68.4, Zymed Laboratories). Secondary antibodies were conjugated to horseradish peroxidase for ECL-based detection.
Chen J., Tibroni N., Sauter D., Galaski J., Miura T., Alter G., Mueller B., Haller C., Walker B.D., Kirchhoff F., Brumme Z.L., Ueno T, & Fackler O.T. (2015). Modest Attenuation of HIV-1 Vpu Alleles Derived from Elite Controller Plasma. PLoS ONE, 10(3), e0120434.
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2

Antibody Characterization for Autophagy Research

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Antibodies used in this study were as follows rabbit LC3b (3868), rabbit ATG16L1 (8089), and rabbit EEA1 (3288) from Cell Signaling Technologies; rabbit anti‐RAB7a (EPR7589), rabbit anti‐CI‐MPR (ab124767), rabbit LAMP1 (ab24170), rabbit GLUT1 (ab15309), rabbit VPS35 (ab97545), rabbit VPS26 (ab181352), rabbit VPS29 (ab98929), rabbit SNX5 (EPR14358), rabbit ULK1 (EPR4885), and rabbit ATG9a (ab108338) from Abcam; mouse TOM20 (612278), mouse EEA1 (610457), mouse SNX1 (611482), and mouse SNX2 (611308) from BD Biosciences; and sheep anti‐TGN46 (AHP500) and mouse anti‐CI‐MPR (anti‐CD222, clone MEM‐238) from AbD Serotec/Bio‐Rad. Further antibodies used were as follows: mouse anti‐GAPDH (10494‐1‐AP), anti‐VARP (24034‐1‐AP), and anti‐TBC1D5 (17078‐1‐AP) from Proteintech; SNX6 from Sigma‐Aldrich (S6324); rat anti‐myc (clone 9E1) and rat anti‐GFP (clone 3H9) from Chromotek; and mouse anti‐LAMP1 (clone H4A3) and mouse anti‐LAMP2 (clone H4B4) from the DSHB. For Western blotting, all antibodies were used at a dilution of 1:1,000. For immunofluorescence, all antibodies were used at 1:100 dilution.
Jimenez‐Orgaz A., Kvainickas A., Nägele H., Denner J., Eimer S., Dengjel J, & Steinberg F. (2017). Control of RAB7 activity and localization through the retromer‐TBC1D5 complex enables RAB7‐dependent mitophagy. The EMBO Journal, 37(2), 235-254.
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3

Multimodal Protein Interaction Detection

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The following primary antibodies were used: rat anti-GFP clone 3H9 (ChromoTek), mouse anti-RFP clone 3F5 (ChromoTek), rabbit anti-TagRFP (Evrogen, AB233), mouse anti-PARP1 clone CII-10 (BD-Biosciences), mouse anti-pADPr clone 10H (Santa Cruz) and rabbit anti-GAPDH antibody (Santa Cruz, sc 25778). The following secondary antibodies were used for detecting the primaries: anti-rat/mouse/rabbit-Alexa Fluor 647/568/488 (Cell Signaling). The following small molecule compounds were administered: camptothecin (Tocris), actinomycin D (Sigma), 4-NQO (Sigma) and H2O2 (Sigma). The following affinity resins were used for immunoprecipitation: GFP-Trap®, RFP-Trap® and PARP1 nanotrap (ChromoTek).
Buchfellner A., Yurlova L., Nüske S., Scholz A.M., Bogner J., Ruf B., Zolghadr K., Drexler S.E., Drexler G.A., Girst S., Greubel C., Reindl J., Siebenwirth C., Romer T., Friedl A.A, & Rothbauer U. (2016). A New Nanobody-Based Biosensor to Study Endogenous PARP1 In Vitro and in Live Human Cells. PLoS ONE, 11(3), e0151041.
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4

Antibody Inventory for Organelle Studies

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Antibodies used in this study were: From Abcam: rabbit anti–CI-MPR (ab124767), rabbit anti-LAMP1 (ab24170), rabbit anti-GLUT1 (ab15309), rabbit anti-VPS35 (ab97545), rabbit anti-VPS26 (ab181352), rabbit anti-VPS29 (ab98929), mouse anti-SNX27 (ab77799), rabbit anti-SNX5 (ab18520), and rabbit anti-INSR (ab131238). From BD: mouse anti-EEA1 (610457), mouse anti-SNX1 (611482), and mouse anti-SNX2 (611308). From AbD Serotec/Bio-Rad Laboratories: sheep anti-TGN46 (AHP500) and mouse anti–CI-MPR (anti-CD222; clone MEM-238). Further antibodies used were: rabbit anti–IGF1R β (9750; Cell Signaling Technology), mouse anti-GAPDH (10494-1-AP; Proteintech), rabbit anti-GGA2 (10356-1-AP; Proteintech), rabbit anti-AP1B1 (16932-1-AP; Proteintech), mouse anti-SNX6 (S6324; Sigma-Aldrich), rat anti-myc (clone 9E1; ChromoTek), and rat anti-GFP (clone 3H9; ChromoTek).
Kvainickas A., Jimenez-Orgaz A., Nägele H., Hu Z., Dengjel J, & Steinberg F. (2017). Cargo-selective SNX-BAR proteins mediate retromer trimer independent retrograde transport. The Journal of Cell Biology, 216(11), 3677-3693.
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