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Goat anti rabbit igg hrp

Manufactured by Santa Cruz Biotechnology
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Sourced in United States, Germany, United Kingdom, Canada, China, Netherlands, Italy, Denmark
About the product

Goat anti-rabbit IgG-HRP is a secondary antibody conjugated with horseradish peroxidase (HRP). It is designed to detect and bind to rabbit immunoglobulin G (IgG) in various immunoassay techniques.

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Lab products found in correlation

Goat anti mouse igg hrp, by Santa Cruz Biotechnology (393 mentions) Donkey anti goat igg hrp, by Santa Cruz Biotechnology (78 mentions) Pvdf membrane, by Merck Group (40 mentions) β actin, by Santa Cruz Biotechnology (33 mentions) Fetal bovine serum (fbs), by Thermo Fisher Scientific (25 mentions) Goat anti mouse igg horseradish peroxidase hrp, by Santa Cruz Biotechnology (24 mentions) Pvdf membrane, by Bio-Rad (21 mentions) Protease inhibitor cocktail, by Merck Group (21 mentions) β actin, by Merck Group (19 mentions) Gapdh, by Santa Cruz Biotechnology (19 mentions) Dimethyl sulfoxide (dmso), by Merck Group (19 mentions) Protease inhibitor cocktail, by Roche (17 mentions) Dc protein assay, by Bio-Rad (17 mentions) Anti β actin, by Santa Cruz Biotechnology (15 mentions) Nitrocellulose membrane, by Bio-Rad (15 mentions) Lipofectamine 2000, by Thermo Fisher Scientific (13 mentions) Anti flag, by Merck Group (12 mentions) Laemmli sample buffer, by Bio-Rad (12 mentions) Goat anti rat igg hrp, by Santa Cruz Biotechnology (12 mentions) Supersignal west pico chemiluminescent substrate, by Thermo Fisher Scientific (11 mentions)
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Market Availability & Pricing

The goat anti-rabbit IgG-HRP from Santa Cruz Biotechnology (catalog number sc-2004) has been discontinued and is no longer available. Santa Cruz Biotechnology now offers a new panel of monoclonal secondary antibodies as a replacement, including the mouse anti-rabbit IgG-HRP (catalog number sc-2357), priced at $77.00.

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Spelling variants (same manufacturer)

Goat anti-rabbit HRP - 135 citations HRP-labeled goat anti-rabbit IgG - 23 citations Rabbit anti- - 18 citations Rabbit anti-IgG - 16 citations HRP-anti-goat IgG - 12 citations Goat anti - 6 citations IgG rabbit - 5 citations Goat anti-rabbit and Goat anti-mouse IgG-HRP - 5 citations HRP-labelled goat anti-rabbit IgG - 5 citations Goat anti-IgG - 4 citations

Similar products (other manufacturers)

Goat anti-rabbit IgG-HRP (by Solarbio) - 27 citations Goat anti-rabbit IgG-HRP (by CWBIO) - 14 citations Goat anti-rabbit IgG-HRP (by R&D Systems) - 9 citations Goat anti-rabbit IgG-HRP (by GeneTex) - 8 citations HRP goat anti-rabbit IgG (by Immunoway) - 7 citations Goat anti-rabbit IgG HRP (by Cytiva) - 6 citations Goat anti-rabbit IgG/HRP (by Golden Bridge) - 4 citations HRP Goat Anti-Rabbit IgG (by Abbkine) - 4 citations HRP goat anti-rabbit IgG (by Elabscience) - 4 citations Goat anti-rabbit IgG-HRP (by Agrisera) - 3 citations

The spelling variants listed below correspond to different ways the product may be referred to in scientific literature.
These variants have been automatically detected by our extraction engine, which groups similar formulations based on semantic similarity.

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892 protocols using «goat anti rabbit igg hrp»

1

Genetic Manipulation of SMARCC2 and DFP2

2025
For SMARCC2 and DFP2 genes, two sgRNAs per gene were cloned into LentiCRISPRv2 (Addgene #52961) for knockout experiments and two shRNAs per gene were cloned into pLKO1-puro (Addgene #8453) plasmid for knockdown experiments. Cells were transduced with constructs and selected with puromycin for three days. Selected cells were counted and seeded onto either 6 multiwell or 96 multiwell plates. Cell viability was measured with CellTiter Glo assay in 96 multiwell plates after 10 days for knockout experiments and after seven days for knockdown experiments. The readings were normalized to that of non-targeting control. 6 multiwell plates were stained with crystal violet solution (0.05% w/v) for 20 min, washed with tap water thoroughly and left to dry overnight. Gene knockout was confirmed by Western blot, and gene knockdowns were confirmed by RT-qPCR. GAPDH (Santa Cruz, sc-25778) and SMARCC2 (Cell Signaling, Cat.No.12760S) antibodies were used as primary antibodies. Goat anti-mouse IgG-HRP (Santa Cruz, sc-2055) and goat anti-rabbit IgG-HRP (Santa Cruz, sc-2054) were used as secondary antibodies. RT-qPCR primers are listed in Supplementary Table 3.
Gokbayrak B., Altintas U.B., Lingadahalli S., Morova T., Huang C.C., Ersoy Fazlioglu B., Pak Lok Yu I., Kalkan B.M., Cejas P., Kung S.H., Fazli L., Kawamura A., Long H.W., Acilan C., Onder T.T., Bagci-Onder T., Lynch J.T, & Lack N.A. (2025). Identification of selective SWI/SNF dependencies in enzalutamide-resistant prostate cancer. Communications Biology, 8, 169.
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2

Protein Expression Analysis in HIBECs

2025
Harvested cells were lysed for 30 min in radioimmunoprecipitation assay buffer (Sigma-Aldrich, St Louis, MO) supplemented with protease inhibitors. Total protein was extracted from the treated HIBECs using M-PER TM Mammalian Protein Extraction Reagent (ThermoFisher Scientific, Waltham, MA, USA). The extracted protein was quantified using a bicinchoninic acid assay kit (ThermoFisher Scientific, Waltham, MA, USA). The protein samples were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the resolved proteins were transferred to a polyvinylidene fluoride membrane (Millipore, Billerica, MA, USA). The membrane was sectioned before antibody hybridization and was individually probed with the following primary antibodies overnight at 4 °C: anti-VDR (ab32042, 1:500), anti-P62/SQSTM1 (ab91526, 1:1000), anti-LC3B (ab48394; 1:400), anti-C-SRC (ab109381; 1:1000), anti-Y419-phospho-SRC (ab185617; 1:1000), anti-TRIF (ab13810; 1:1000), anti-TLR3 (ab137722; 1:1000), anti-ERK1/2 (ab17942; 1:1000), anti-p-ERK1/2 (ab214362; 1:1000), and anti-GAPDH (ab8245, 1:5000) antibodies. Next, each membrane was washed twice with PBS and incubated with goat anti-rabbit IgG HRP (1:2000; Santa Cruz, CA, USA) for 1 h at room temperature. Immunoreactive signals were visualized using enhanced chemiluminescence and quantified using Image J software (NIH, Bethesda, MD, USA). GAPDH was used as the loading control.
Liu N., Zhao P., Cao P., Hui J., Pan Y, & Cheng J. (2025). Vitamin D3/VDR alleviates double-stranded RNA virus -induced biliary epithelial cell damage by inhibiting autophagy. BMC Gastroenterology, 25, 44.
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3

Molecular Mechanisms of Rolipram-Mediated Anti-Cancer Effects

2024
Rolipram (a PDE4 inhibitor), was purchased from Sigma-Aldrich, USA (Cat# R6520) and dissolved in ethanol to prepare a stock solution of 10 mM. The selective PKA inhibitor H89 was also procured from Sigma-Aldrich, USA (Cat# B1427) and dissolved in DMSO to prepare a stock solution of 1 mM. The primary antibodies used in this study are: PKA (Santa Cruz Biotechnology, USA, Cat# sc-28315), PTEN (Cell Signaling Technology, USA, Cat# 9552, RRID:AB_10694066), PI3K (Cell Signaling Technology Cat# 4249, RRID:AB_2165248), Akt (Cell Signaling Technology, USA, Cat# 9272 (also 9272S), RRID:AB_329827), p-GSK3β (Santa Cruz Biotechnology, USA, Cat# sc-373800, RRID:AB_10920410), GLI1 (Novus Biologicals Cat# NB600-600, RRID:AB_2111758), GLI2 (Novus Biologicals Cat# NB600-874, RRID:AB_10001953), GLI3 (Novus Biologicals Cat# NBP2-29627), anti-HA (Cell Signaling Technology Cat# 2367, RRID:AB_10691311), MMP2 (Cell Signaling Technology Cat# 4022, RRID:AB_2266622), MMP9 (Cell Signaling Technology Cat# 3852, RRID:AB_2144868), Ecadherin (Cell Signaling Technology Cat# 14472, RRID:AB_2728770), Vimentin (Cell Signaling Technology Cat# 3932 (also 3932S), RRID:AB_2288553). The secondary antibodies used in this study are: Goat anti-mouse IgG-HRP (Santa Cruz Biotechnology, USA, Cat# sc-2005), Goat anti-rabbit IgG-HRP (Santa Cruz Biotechnology, USA, Cat# sc-2004).
Bagchi A., Bhattacharya A., Chatterji U., & Biswas A. (2024). PDE4 inhibitor Rolipram represses hedgehog signaling via ubiquitin-mediated proteolysis of GLI transcription factors to regress breast cancer.
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4

Western Blot Analysis of PRAME, p53, and p27

2024
For WB, cells were lysed in RIPA buffer (50 mM Tris-Cl pH 7.5, 150 mM NaCl, 0.4% Nonidet P-40, 1 mM EDTA, 1 mM PMSF, 1 mM Na3VO4, and 1 mM NaF) supplemented with a protease inhibitor cocktail (Roche, Switzerland). Proteins were separated by electrophoresis on 8-15% SDS gels, transferred to nitrocellulose, and incubated with the following primary antibodies: anti-PRAME (sc-137188, Santa Cruz Biotechnology, CA, USA; ab219650, Abcam, Cambridge, UK), anti-p53 (sc-6243; Santa Cruz Biotechnology), anti-acetyl-p53 (Lys 382) (#2525; Cell Signaling Technology, MA, USA), anti-p27 (sc-528; Santa Cruz Biotechnology), and anti-β-actin (sc-47778; Santa Cruz Biotechnology). Blots were next incubated with goat anti-mouse IgG-HRP (sc-2005; Santa Cruz Biotechnology) or goat anti-rabbit IgG-HRP (sc-2004; Santa Cruz Biotechnology).
Lee Y.K., Heo H.H., Kim N., Park U.H., Youn H., Moon E.Y., Kim E.J, & Um S.J. (2024). Tumor antigen PRAME is a potential therapeutic target of p53 activation in melanoma cells. BMB Reports, 57(6), 299-304.
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5

Colon Protein Expression Analysis

2024
The 40 mg colon tissues were completely cleanout under PBS and without scraped crypts, homogenized in RIPA lysis and Extraction Buffer (Thermo Fisher Scientific). The Colon tissue samples were randomly taken from 3 animals in each group. Individual colon lysates were loaded and separated by sodium dodecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE) and then transferred to an Immobilon-P Polyvinylidene difluoride membrane (Millipore). After blocking with 5% milk in PBS, the membrane was incubated with primary antibodies: rabbit polyclonal anti-claudin 1 (1:1000 dilution, 71-7800, Invitrogen), mouse monoclonal anti-ZO-1 (1:1000 dilution, 33-9100, Thermo Fisher Scientific), mouse monoclonal anti-E cadherin (1:1000 dilution, ab231303, Abcam), Mouse monoclonal anti-GAPDH (1:1000 dilution, ab8245, Abcam) and rabbit polyclonal anti-SLC17A5 (1:1000 dilution, PA5-30517, Thermo Fisher Scientific) at 4 °C overnight. After incubation with secondary antibodies, goat anti-rabbit IgG-HRP (1:2000 dilution, SC-2004; Santa Cruz Biotechnology) or goat anti-mouse IgG-HRP (1:2000 dilution, ab205719; Abcam) at room temperature, membranes were used western ECL substrate (Bio-Rad), followed by exposure of the membranes to film and digital imaging. Image J software was used for gray scale analysis, and each independent colonic tissue lysate was technically repeated 3 times to obtain the mean value as a sample.
Wang X., Liu H., Yue M., Wang J., Zhang C., Qin L., Wang S, & Hu L. (2024). Dietary nitrate maintains intestinal epithelia homeostasis in aged mice. Biogerontology.
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Top 5 protocols citing «goat anti rabbit igg hrp»

1

Macrophage Cell Lines Generation

Cited 5 times
Immortalized macrophage cell lines were generated from wt, NLRP3−/−, ASC−/−, caspase1−/−, TLR9−/−, ctsb−/−, ctsl−/− and 3d mice (Hornung et al., 2008 (link)). Primary BMDMs were generated as described (Rathinam et al., 2010 (link)). Human PBMCs were isolated from whole blood of healthy volunteers by density gradient centrifugation. All cells, primary and cell lines were cultured in DMEM supplemented with Ciprofloxacin and 10% FBS. For all experiments for immunoblot analysis, serum-free DMEM medium was used. For stimulations, poly (dAdT) (1.5 µg/ml) or genomic DNA was transfected with lipofectamine 2000 (Invitrogen). Nigericin (10 µM) was added 1 h before supernatants were collected. 2×105 macrophages were plated and stimulated the day after with indicated amounts of CpG, sHz, nHz, sHz/CpG and sHz/Pf gDNA, iRBCs and RBCs. Cytokine measurements were performed using ELISA kits for mouse IL-1β and TNFα (R&D systems). Immunoblot analysis was performed with anti– mouse IL-1β antibody (AF-401-NA; R&D Systems) and rabbit anti-goat IgG-HRP (Santa Cruz Biotechnology).
Kalantari P., DeOliveira R.B., Chan J., Corbett Y., Rathinam V., Stutz A., Latz E., Gazzinelli R.T., Golenbock D.T, & Fitzgerald K.A. (2014). Dual engagement of the NLRP3 and AIM2 inflammasomes by plasmodial-derived hemozoin and DNA during malaria. Cell reports, 6(1), 196-210.
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2

Histological Analysis of Liver and Lens

Cited 4 times
Paraffin-embedded liver tissue was cut into 5-μm sections, which were stained with hematoxylin-eosin for histologic examination or with Sirius Red to visualize fibrosis. For analysis of adult lens, mouse skulls were fixed and decalcified in Formical-4, and processed for paraffin embedding and sections. Immunohistochemical and immunofluorescent staining were performed according to the protocols provided by the manufacturers of the respective antibodies. The following primary antibodies were used: Ki-67 (DAKO; M7249, 1/25), wide spectrum screening cytokeratin (pan-CK) (DAKO; Z0622, 1/500), Yap (Sigma; WH0010413M1, 1/100), NF2 (Sigma; HPA003097, 1/150), and cleaved Caspase-3 (Asp175) (Cell Signaling; #9661, 1/100). The secondary antibodies used were: Envision™ anti-rabbit (DAKO; K4002), and rabbit anti-goat IgG HRP (Santa Cruz Biotechnology; SC-2768, 1/100). The DAB+ (DAKO; K3467) visualization system was used for immunohistochemical staining, and Cy3- or Alexa488-conjugated rabbit secondary antibody was used for immunofluorescent staining. TUNEL staining was performed with the DeadEnd™ colorimetric TUNEL system (Promega; G7130) or In Situ Cell Death Detection Kit (Roche) according to the manufacturers' instructions.
Zhang N., Bai H., David K.K., Dong J., Zheng Y., Cai J., Giovannini M., Liu P., Anders R.A, & Pan D. (2010). The Merlin/NF2 tumor suppressor functions through the YAP oncoprotein to regulate tissue homeostasis in mammals. Developmental cell, 19(1), 27-38.
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3

Galanin Signaling in Neuropathic Pain

Cited 3 times
At the designed experimental time point, the L4-5 DRG and the corresponding SDH of the rats were surgically harvested. The levels of Gal, GalR1, and GalR2 in L4-5 DRG and the corresponding SDH were analyzed by Western blot assay. The expression of β-actin was also determined as an internal control. The DRG and SDH tissues were homogenized in 10 mmol/L Tris homogenization buffer (pH 7.4) with protease inhibitors. The samples were centrifuged at 10,000 g for 10 minutes and the supernatant collected for Western blot assay. After determining the protein concentrations of the supernatants (BCA method, standard: BSA), 50 µg protein of each sample was loaded onto the 10% SDS gel, separated by electrophoresis and transferred to nitrocellulose membrane. The membranes were blocked in blocking buffer (5% nonfat milk) for 2 hours at room temperature, and then were incubated with goat anti-Gal polyclonal IgG (1∶500, Santa Cruz Biotechnology), goat anti-GalR1 polyclonal IgG (1∶500, Santa Cruz Biotechnology), goat anti-GalR2 polyclonal IgG (1∶500, Santa Cruz Biotechnology) or mouse anti-β-actin monoclonal IgG (1∶1000, Santa Cruz Biotechnology) overnight at 4°C. After being washed three times for 10 minutes with washing solution, the membranes were incubated with rabbit anti-goat IgG-HRP (1∶4000, Santa Cruz Biotechnology) or goat anti-mouse IgG-HRP (1∶4000, Santa Cruz Biotechnology). The immunoreactive bands were visualized by an ECL Western blotting detection kit (Billerica) on light sensitive film. The films were scanned and the images were analyzed quantitatively by using an ImagJ 1.39 u image analysis software. The protein levels of Gal, GalR1, and GalR2 were expressed as the ratio of control.
Xu X., Yang X., Zhang P., Chen X., Liu H, & Li Z. (2012). Effects of Exogenous Galanin on Neuropathic Pain State and Change of Galanin and Its Receptors in DRG and SDH after Sciatic Nerve-Pinch Injury in Rat. PLoS ONE, 7(5), e37621.
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4

Gentisic Acid Modulates MAPK Signaling

Cited 3 times
HaCaT cells (106 cells) were seeded into a 90mm dish and incubated for 24hours under the same condition. The medium was exchanged with serum-free medium containing various concentrations of gentisic acid (0, 1, 5, 10, 50, and 100 μg/ml) and cells were incubated for an additional 24 hours. Equal amounts (15μg) of whole-cell lysate proteins were separated on an 8% acrylamide SDS-PAGE gel and transferred onto polyvinylidene fluoride (PVDF, Bio-Rad, USA) membrane. The membranes were blocked using 5% bovine serum albumin (BSA, GenDEPOT, Korea) and then stained with primary antibodies (p38α, p-p38, ERK1/2, JNK, p-JNK, and GAPDH from Santa Cruz Biotechnology, CA, USA; p-ERK1/2 from Cell Signaling Technology, MA, USA) overnight at 4°C. The membranes were washed three times in TBST and incubated with a secondary horseradish-peroxidase conjugated antibody (goat anti-rabbit IgG-HRP from Santa Cruz Biotechnology, CA, USA; goat anti-mouse IgG-HRP from Bio-Rad, USA) for 1 hour at room temperature. The membranes were developed using enhanced ECL (Bio-Rad, USA) on a UVITEC imaging system (UVITEC Cambridge, UK). Each lane was quantified by GAPDH 11 (link), 25 , 32 (link).
Kim M., Kim J., Shin Y.K, & Kim K.Y. (2020). Gentisic Acid Stimulates Keratinocyte Proliferation through ERK1/2 Phosphorylation. International Journal of Medical Sciences, 17(5), 626-631.
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5

Western Blot Analysis of HO-1 Protein

Cited 3 times
Protein samples from control and aniline-treated rats were subjected to Western blot analysis as described earlier [31 (link)]. Briefly, spleen tissue lysates were prepared using the lysis buffer essentially as described by the manufacturer (Cell Signaling, Beverly, MA). The lysate proteins (50 μg) were subjected to 10% SDS-PAGE and transferred to a PVDF membrane (Amersham, Arlington Heights, IL). After blocking with non-fat dry milk (5%, w/v), HO-1 protein band was detected using anti-HO-1 antibody (1:3000; Santa Cruz Biotech, Santa Cruz, CA) and goat anti-rabbit IgG-HRP (1:5000; Santa Cruz Biotech) as secondary antibody. ECL Plus (Amersham, Arlington Heights, IL) was used to detect the signals. HO-1 bands were quantitated by densitometry and normalized using the actin signal to correct for differences in loading of proteins from control and experimental groups. For densitometric analysis, the protein bands on the blot were measured by Eagle Eye II software. Protein concentration in the lysates was determined by Bio-Rad Protein Assay kit (Bio-Rad Laboratories).
Wang J., Ma H., Boor P.J., Sadagopa Ramanujam V.M., Ansari G.A, & Khan M.F. (2009). Up-Regulation of Heme Oxygenase-1 in Rat Spleen Following Aniline Exposure. Free radical biology & medicine, 48(4), 513.
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