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Anti rabbit hrp conjugate

Manufactured by Promega
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The Anti-Rabbit HRP conjugate is a secondary antibody conjugated with horseradish peroxidase (HRP). It is designed to detect and visualize primary antibodies raised against rabbit antigens in various immunoassay applications.

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Lab products found in correlation

Opti mem, by Thermo Fisher Scientific (2 mentions) D erythro sphingosine, by Santa Cruz Biotechnology (1 mentions) Anti mouse hrp conjugate, by Promega (1 mentions) Flag peptide, by Merck Group (1 mentions) Fugene 6 transfection reagent, by Promega (1 mentions) Dmem medium, by Thermo Fisher Scientific (1 mentions) Faf bsa, by Merck Group (1 mentions) Anti flag m2 affinity gel, by Merck Group (1 mentions) Rpmi 1640 medium, by Corning (1 mentions) Phosphatase inhibitor, by Merck Group (1 mentions) Ecl reagent, by GE Healthcare (1 mentions) Am4300, by Thermo Fisher Scientific (1 mentions) Anti gapdh, by Thermo Fisher Scientific (1 mentions) Protease inhibitor cocktail, by Merck Group (1 mentions) Chemidoc mp, by Bio-Rad (1 mentions) Mini protean, by Bio-Rad (1 mentions) Anti ha antibody, by Merck Group (1 mentions) H6908, by Merck Group (1 mentions)

4 protocols using anti rabbit hrp conjugate

1

Ceramide Signaling Pathway Characterization

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RPMI 1640 medium was purchased from Corning (NY, USA; #10-040-CV), DMEM medium from ThermoFisher Scientific Inc. (CA, USA). C16:0 ceramide-1-phosphate (#860533) was obtained from Avanti Polar Lipid (AL, USA), D-erythro-Sphingosine (#SC-3546) from Santa Cruz Biotechnology (TX, USA). Dynabeads M-270 Epoxy Co-IP Kit (#14321D) and OPTIMEM (#31985-062) were acquired from ThermoFisher Scientific Inc. (CA, USA). Fatty acid free (FAF)-BSA (#A6003), Anti-FLAG M2 Affinity Gel (#A2220) and FLAG peptide (#F3290) were purchased from Sigma-Aldrich (MO, USA, #SAB2701099) and Fugene 6 transfection reagent (#E2692) from Promega Corp. (WI, USA).
The following antibodies were used: Anti-SMPDL3b (GenWay Biotech, CA, USA, #GWB-2281D4), Anti-CERK (Sigma-Aldrich, MO, USA, #SAB2701099) and IgG (Sigma-Aldrich, MO, USA #I5381). Anti-ACER2 (#LS-C354506), Anti-SPTLC3 (#LS-C397341), Anti-S1PR1 (#LS-B6370), Anti-SMPD1 (#LS-C334919) antibodies were purchased from LifeSpan BioSciences, Inc. (WA, USA). Secondary antibodies, Anti-Rabbit HRP conjugate (#W401B) and Anti-Mouse HRP conjugate (#W402B) were purchased from Promega Corp. (WI, USA).
Mallela S.K., Mitrofanova A., Merscher S, & Fornoni A. (2019). Regulation of the amount of Ceramide-1-Phosphate synthesized in differentiated human podocytes. Biochimica et biophysica acta. Molecular and cell biology of lipids, 1864(12), 158517.
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2

Cardiac Protein Quantification via Western Blot

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Cell lysates were prepared from hearts in homogenization buffer (50 mM TRIS, 320 mM sucrose, 1 mM DTT, 0.1% IGEPAL CA-630, pH 7.0) containing 1% protease inhibitor cocktail (Sigma P8340) and phosphatase inhibitor (Sigma P0044). Two hearts from C57BL/6J and 1 heart from a congenital Casq2–/– mouse (7 (link)) were included as controls. Samples were separated on a 4%–20% polyacrylamide gel (Bio-Rad Mini-PROTEAN), transferred to a PVDF membrane, blocked in TBS with Tween (TBST) plus 5% milk for 1 hour at room temperature and incubated overnight at 4°C with primary antibody. Blots were washed 3 times in TBST and incubated with secondary antibody for 1 hour at room temperature, washed 3 times again in TBST, and then developed with ECL reagent (GE Healthcare) and imaged using a ChemiDoc MP (Bio-Rad). For calsequestrin 2 immunolabeling, blots were incubated with 1:2000 anti-calsequestrin2 (ab108289; Abcam) and 1:5000 anti-rabbit HRP conjugate (catalog W401B; Promega). For GAPDH, blots were incubated with 1:10,000 anti-GAPDH (catalog AM4300; ThermoFisher) and 1:5000 anti-mouse HRP conjugate (catalog 31430; Invitrogen). Full uncropped and unedited blots were provided to the reviewers.
Blackwell D.J., Faggioni M., Wleklinski M.J., Gomez-Hurtado N., Venkataraman R., Gibbs C.E., Baudenbacher F.J., Gong S., Fishman G.I., Boyle P.M., Pfeifer K, & Knollmann B.C. (2022). The Purkinje–myocardial junction is the anatomic origin of ventricular arrhythmia in CPVT. JCI Insight, 7(3), e151893.
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3

Antibody Validation for Protein Studies

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ANTI-FLAG antibody produced in mouse (clone M2, F3165, 1:3500) and Anti-HA antibody produced in rabbit (H6908, 1:1000) were purchased from MilliporeSigma (St. Louis, MO). VU101: Anti-ubiquitin Antibody (VU-0101, 1:1000) was purchased from LifeSensors (PA, USA). Anti-mouse HRP conjugate (W4021, 1:10,000) and Anti-Rabbit HRP conjugate (W4011, 1:10,000) were purchased from Promega (Madison, WI). Anti-COPI antibody was a gift from Charles Barlowe (Dartmouth Univ, 1:3000). Anti-Arf antibody (1:3000) used was reported previously (Liu et al., 2008 (link)). Anti-GST antibody (1:1000) was purchased from Vanderbilt Antibody Product Store (VAPR, Nashville, TN).
Date S.S., Xu P., Hepowit N.L., Diab N.S., Best J., Xie B., Du J., Strieter E.R., Jackson L.P., MacGurn J.A, & Graham T.R. (2022). Ubiquitination drives COPI priming and Golgi SNARE localization. eLife, 11, e80911.
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4

E. coli Protein Fractionation and Western Blotting

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E. coli cells were fractionated into periplasmic, cytoplasmic and membrane fractions using the lysozyme/cold osmotic shock method [35 (link)]. The resulting fractions were analysed by sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE).
Once the cytosolic and inner membrane samples had been analysed using SDS–PAGE, the proteins were transferred from acrylamide gels to PVDF membranes via a semi-dry western blotting apparatus. The membranes were blocked overnight in a solution of 5% (w/v) dried milk in PBS-T and then incubated with primary anti-TatA antibody (1:6000, in PBS-T) for 1 h before washing. Membranes were incubated with anti-rabbit-HRP conjugate (Promega, WI, U.S.A.) for 1 h at RT, and subsequently washed. Finally, immunoreactive bands were detected using ECL™ detection reagents according to the manufacturer's instructions. X-ray films were developed using an AGFA Curix 60 automatic developer as directed by the manufacturer's instructions.
Smith S.M., Yarwood A., Fleck R.A., Robinson C, & Smith C.J. (2017). TatA complexes exhibit a marked change in organisation in response to expression of the TatBC complex. Biochemical Journal, 474(9), 1495-1508.
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