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Anti mouse 800cw

Manufactured by LI COR
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Sourced in United States, Japan

The Anti-mouse 800CW is a near-infrared fluorescent secondary antibody designed for use with LI-COR imaging systems. It is used to detect and quantify mouse primary antibodies in western blotting, immunohistochemistry, and other applications.

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Lab products found in correlation

Anti rabbit 680lt, by LI COR (5 mentions) Anti β actin, by Cell Signaling Technology (3 mentions) Ab251652, by Cell Signaling Technology (2 mentions) Ab6721, by Abcam (2 mentions) Anti hdac1, by Cell Signaling Technology (2 mentions) Anti egfp, by Cell Signaling Technology (2 mentions) Anti bcl6, by Santa Cruz Biotechnology (2 mentions) Anti v5 tag, by Thermo Fisher Scientific (2 mentions) Anti streptavidin, by Merck Group (2 mentions) Anti mouse alexa fluor 633, by Thermo Fisher Scientific (2 mentions) Alexa anti mouse 488, by BioLegend (2 mentions) Anti beta tubulin, by Cell Signaling Technology (2 mentions) Anti histone h3, by Cell Signaling Technology (2 mentions) Anti hsp90, by Cell Signaling Technology (2 mentions) Odyssey blocking buffer, by LI COR (2 mentions) Phospho stat3 tyr705 9145, by Cell Signaling Technology (1 mentions) Anti rabbit 800cw, by LI COR (1 mentions) Odyssey secondary antibodies, by LI COR (1 mentions) Trans blot, by Bio-Rad (1 mentions) Anti brd4, by Fortis Life Sciences (1 mentions)

12 protocols using anti mouse 800cw

1

Antibodies for Cyclin K and CRBN

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The following antibodies were used in this study: anti-cycK (Bethyl Laboratories, A301–939A for full length cycK), anti-cycK (abcam, ab251652, for cycK1−267), anti-beta-actin (Cell Signaling, #3700), anti-CRBN (Sigma prestige, HPA045910), anti-mouse 800CW (LI-COR Biosciences, 926–32211), anti-rabbit 680LT (LI-COR Biosciences, 925–68021), anti-rabbit IgG antibodies (abcam, ab6721).
Słabicki M., Kozicka Z., Petzold G., Li Y.D., Manojkumar M., Bunker R., Donovan K.A., Sievers Q.L., Koeppel J., Suchyta D., Sperling A.S., Fink E.C., Gasser J.A., Wang L.R., Corsello S.M., Sellar R.S., Jan M., Gillingham D., Scholl C., Fröhling S., Golub T.R., Fischer E.S., Thomä N.H, & Ebert B.L. (2020). The CDK inhibitor CR8 acts as a molecular glue degrader that depletes cyclin K. Nature, 585(7824), 293-297.
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2

Antibodies for Cyclin K and CRBN

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The following antibodies were used in this study: anti-cycK (Bethyl Laboratories, A301–939A for full length cycK), anti-cycK (abcam, ab251652, for cycK1−267), anti-beta-actin (Cell Signaling, #3700), anti-CRBN (Sigma prestige, HPA045910), anti-mouse 800CW (LI-COR Biosciences, 926–32211), anti-rabbit 680LT (LI-COR Biosciences, 925–68021), anti-rabbit IgG antibodies (abcam, ab6721).
Słabicki M., Kozicka Z., Petzold G., Li Y.D., Manojkumar M., Bunker R., Donovan K.A., Sievers Q.L., Koeppel J., Suchyta D., Sperling A.S., Fink E.C., Gasser J.A., Wang L.R., Corsello S.M., Sellar R.S., Jan M., Gillingham D., Scholl C., Fröhling S., Golub T.R., Fischer E.S., Thomä N.H, & Ebert B.L. (2020). The CDK inhibitor CR8 acts as a molecular glue degrader that depletes cyclin K. Nature, 585(7824), 293-297.
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3

Comprehensive Antibody Panel for Protein Analysis

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The following antibodies were used in this study: anti-BCL6 (Santa Cruz Biotechnology, sc-7388), anti-beta-tubulin (Cell Signaling, 2146S), anti-Hsp90 (Cell Signaling, 4874S), anti-HDAC1 (Cell Signaling, 2062S), anti-Histone H3 (Cell Signaling, 12648S), anti-eGFP (Cell Signaling, 2956), anti-V5-tag (ThermoFisher Scientific, MA5–15253), anti-Streptavidin (Sigma, 71591–3), anti-Mouse 800CW (LI-COR Biosciences, 926–32211), anti-Rabbit 680LT (LI-COR Biosciences, 925–68021), anti-mouse Alexa Fluor 633 (ThermoFisher Scientific, A-21052), and Alexa anti-mouse 488 (Biolegend, 405319).
Słabicki M., Yoon H., Koeppel J., Nitsch L., Roy Burman S.S., Di Genua C., Donovan K.A., Sperling A.S., Hunkeler M., Tsai J.M., Sharma R., Guirguis A., Zou C., Chudasama P., Gasser J.A., Miller P.G., Scholl C., Fröhling S., Nowak R.P., Fischer E.S, & Ebert B.L. (2020). Small molecule-induced polymerization triggers degradation of BCL6. Nature, 588(7836), 164-168.
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4

Western Blot Analysis of Signaling Proteins

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Western blots were done following previously used protocols21 ,22 (link) and the primary antibody for IκBα (Santa Cruz Biotechnology, Dallas, TX, USA #sc371), and STAT3 (#9139), phospho-STAT3-Tyr705 (#9145) or TBP (#8415) all from Cell Signaling Technology (Danvers, MA, USA), were used at a 1:1000 dilution, and the secondary antibodies were anti-rabbit-HRP (Dako, Agilent technology, Santa Clara, CA, USA) or anti-rabbit-680LT or anti-mouse-800CW (LI-COR Bioscience, Lincoln, NE, USA). Band densities were analyzed using ImageJ and displayed with GraphPad Prism software, representing the mean and standard deviation and analyzed using two-sided Student’s t-test. (GraphPad Software Inc., La Jolla, CA, USA).
Melin N., Sánchez-Taltavull D., Fahrner R., Keogh A., Dosch M., Büchi I., Zimmer Y., Medová M., Beldi G., Aebersold D.M., Candinas D, & Stroka D. (2021). Synergistic effect of the TLR5 agonist CBLB502 and its downstream effector IL-22 against liver injury. Cell Death & Disease, 12(4), 366.
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5

Detailed Immunoblotting Protocol with Antibody Dilutions

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An equal fraction (e.g., 2%) of each sample was analyzed by immunoblotting. Samples were boiled in Laemmli sample buffer for 5 min and electrophoresed for 45 min on a 4-20% SDS-PAGE gel (Pierce, Rockford, IL) at 120 volts and then transferred to nitrocellulose membranes for 1 h at room temperature at 100 volts followed by blocking with 5% BSA in PBS for 1 h at room temperature. Blots were then incubated overnight with agitation with primary antibody, washed 3 times in 5% non-fat dry milk/0.1% (v/v) Tween-20/PBS (diluent buffer), incubated for 1 h at room temperature with secondary antibody, washed 3 times with diluent buffer, once with PBS, and then imaged on a Li-Cor Odyssey imager. Primary antibodies, all diluted 1:2,000 in diluent buffer, were SMI-26, RACK1 rabbit monoclonal (D59D5, Cell Signaling Technology, Danvers, MA), eIF4A rabbit monoclonal (C32B4, Cell Signaling Technology), Cyclin D2 rabbit monoclonal (D52F9, Cell Signaling Technology) and DDX3X rabbit monoclonal (D19B4, Cell Signaling Technology); secondary antibodies, diluted 1:15,000, were an anti-mouse 800 CW for GFAP immunoblots or an anti-rabbit 800 CW for all other blots (Li-Cor Biosciences, Lincoln, NE). All samples presented in a figure panel were run on the same gel as indicated, but for some of the mouse sample immunoblots a lane not relevant to this study was deleted.
Heaven M.R., Flint D., Randall S.M., Sosunov A.A., Wilson L., Barnes S., Goldman J.E., Muddiman D.C, & Brenner M. (2016). The Composition of Rosenthal Fibers, the Protein Aggregate Hallmark of Alexander Disease. Journal of proteome research, 15(7), 2265-2282.
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6

Western Blot Analysis of Nulp1 and β-Actin

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Proteins separated by 12.5% SDS‒PAGE were transferred to PVDF membranes using a Bio-Rad TRANS-BLOT semidry system in transfer buffer (25 mM Tris, 192 mM glycine, 0.1% SDS, 20% methanol, pH 8.3). Membranes were blocked using LI-COR blocking buffer for 2 h at 4 °C. Incubation with primary antibodies was performed at 4 °C overnight. Membranes were incubated in LI-COR Odyssey secondary antibodies for at least 3 h and then observed in an Odyssey scanner. The primary antibodies used were anti-Nulp1 (TCF25) mouse (Invitrogen; 1:3000 dilution) and anti-β-actin mouse (Thermo Scientific; 1:5000 dilution). The secondary antibody was anti-mouse 800 CW LI-COR (1:5000 dilution).
Dos Santos O.A., Carneiro R.L., Requião R.D., Ribeiro-Alves M., Domitrovic T, & Palhano F.L. (2024). Transcriptional profile of ribosome-associated quality control components and their associated phenotypes in mammalian cells. Scientific Reports, 14, 1439.
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7

Antibody Detection Protocol

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The following antibodies were used: anti-BRD4 (Bethyl Laboratories, A301-985A100), anti-β-actin (Cell Signaling Technology, #3700), anti-Flag (Sigma-Aldrich, M8823), anti-HA (Cell Signaling Technology, #3724), anti-mouse 800CW (LI-COR Biosciences, 926-32211), anti-rabbit 680LT (LI-COR Biosciences, 925-68021).
Li Y.D., Ma M.W., Hassan M.M., Hunkeler M., Teng M., Puvar K., Lumpkin R., Sandoval B., Jin C.Y., Ficarro S.B., Wang M.Y., Xu S., Groendyke B.J., Sigua L.H., Tavares I., Zou C., Tsai J.M., Park P.M., Yoon H., Majewski F.C., Marto J.A., Qi J., Nowak R.P., Donovan K.A., Słabicki M., Gray N.S., Fischer E.S, & Ebert B.L. (2023). Template-assisted covalent modification of DCAF16 underlies activity of BRD4 molecular glue degraders. bioRxiv.
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8

Western Blot Analysis of Phosphorylated MLH1

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Proteins were separated on 10% polyacrylamide gels, followed by Western blotting on nitrocellulose membranes and antibody detection using standard procedures. Nitrocellulose membranes on which immunoprecipitated proteins were blotted were cut between 50 and 75 kDa, only the upper part of the membrane was incubated with antibody. This prevented hybridisation of the antibody of interest to the antibody used for precipitation.
Fluorescent-labeled secondary antibodies (anti-mouse 680 LT from LiCor Bioscience, anti-mouse 800 CW from LiCor Bioscience, anti-rabbit 680 LT from LiCor Bioscience) were used to detect signals in a FLA-9000 scanner (Fujifilm, Tokyo, Japan). If indicated, the band intensity of the protein expression was quantified using the Multi Gauge V3.2 program (Fujifilm, Tokyo, Japan).
The amount of p-MLH1S477 was detected after immunoprecipitation and quantified in correlation to total MLH1 levels as previously described14 (link) using Multi Gauge V3.2. p-MLH1S477 levels were calculated in relation to MLH1 set to 100%. Thereafter, all p-MLH1S477 level were normalized to the p-MLH1S477 level of the MLH1 wt. All experiments were performed at least three times.
Firnau M.B., Plotz G., Zeuzem S, & Brieger A. (2023). Key role of phosphorylation sites in ATPase domain and Linker region of MLH1 for DNA binding and functionality of MutLα. Scientific Reports, 13, 12503.
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9

Comprehensive Antibody Panel for Protein Analysis

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The following antibodies were used in this study: anti-BCL6 (Santa Cruz Biotechnology, sc-7388), anti-beta-tubulin (Cell Signaling, 2146S), anti-Hsp90 (Cell Signaling, 4874S), anti-HDAC1 (Cell Signaling, 2062S), anti-Histone H3 (Cell Signaling, 12648S), anti-eGFP (Cell Signaling, 2956), anti-V5-tag (ThermoFisher Scientific, MA5–15253), anti-Streptavidin (Sigma, 71591–3), anti-Mouse 800CW (LI-COR Biosciences, 926–32211), anti-Rabbit 680LT (LI-COR Biosciences, 925–68021), anti-mouse Alexa Fluor 633 (ThermoFisher Scientific, A-21052), and Alexa anti-mouse 488 (Biolegend, 405319).
Słabicki M., Yoon H., Koeppel J., Nitsch L., Roy Burman S.S., Di Genua C., Donovan K.A., Sperling A.S., Hunkeler M., Tsai J.M., Sharma R., Guirguis A., Zou C., Chudasama P., Gasser J.A., Miller P.G., Scholl C., Fröhling S., Nowak R.P., Fischer E.S, & Ebert B.L. (2020). Small molecule-induced polymerization triggers degradation of BCL6. Nature, 588(7836), 164-168.
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10

Quantitative Western Blot Analysis

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After removing the media, HEK293 cells were detached by pipetting up and down 1 ml per well of serum free media and diluted further with an extra 1 ml per well of serum-free media. 1 ml of cells in suspension was added to derivatised collagen films coated on 12-well plates (prepared as described above) for 90 min at 37 °C with 5% CO2. Cell were lysed with 80 μl of lysis buffer (150 mM NaCl, 50 mM Tris pH 7.4, 1 mM EDTA, 1 mM PMSF, 50 μg/ml aprotinin, 5 mM NaF and 1 mM NaVO3) for 20 min on ice and kept at −80 °C overnight. Cell lysates and a blue pre-stained protein ladder (Broad range 11–190 kDa, NEB) were separated on a SDS-PAGE 4–12% gel and transferred to a PVDF membrane. Membranes were blocked with Odyssey blocking buffer (LICOR Bioscience), probed with both anti-Flag 1:500 and anti-pY740 1:1000 antibodies overnight at 4 °C, washed with blocking buffer 3 × 10 min, probed with anti-mouse 800CW (LICOR Bioscience) and anti-rabbit 680RD (LICOR Bioscience) for 1 h, and washed 3 × 5 min. Signals were acquired and quantified using the Odyssey instrument (LICOR Bioscience).
Malcor J.D., Juskaite V., Gavriilidou D., Hunter E.J., Davidenko N., Hamaia S., Sinha S., Cameron R.E., Best S.M., Leitinger B, & Farndale R.W. (2018). Coupling of a specific photoreactive triple-helical peptide to crosslinked collagen films restores binding and activation of DDR2 and VWF. Biomaterials, 182, 21-34.
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