Goat anti rabbit igg

Manufactured by Santa Cruz Biotechnology

Sourced in United States, Germany, Sweden

Goat anti-rabbit IgG is a secondary antibody that recognizes and binds to rabbit immunoglobulin G (IgG) molecules. It is commonly used in various immunological techniques, such as Western blotting, ELISA, and immunohistochemistry, to detect and visualize target proteins that have been labeled with a primary rabbit antibody.

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Rabbit anti-IgG (4 citations) IgG Rabbit (3 citations) Rabbit IgGs (2 citations) Rabbit anti-TM (2 citations) Goat anti-rabbit horseradish peroxidase-conjugated IgGs (2 citations)

207 protocols using goat anti rabbit igg

Dissecting Cell Death Pathways in Viral Infection

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Human embryonic kidney cells (HEK293T, cat #SCSP-502), human lung alveolar epithelial cells (A549, cat #TCHu150) and wild type respiratory syncytial virus (RSV) long strain (Cat #GDV052) were purchased from Cell Bank of Chinese Academy of Sciences (CCTCC). Recombinant Adenovirus (ADV) that is packaged in HEK293T cells with the plasmid pSG500-GFP and pBGHlox and that could be replicated in tumor cells was provided by Sinogenomax Inc., Beijing, China. Primary antibody against forphospho-IRF-3 (S386) was purchased from Abcam. Primary antibodies for caspase-9 and -3 were purchased from Cell Signaling Technology. Primary antibodies for 6×His-tag, RSV fusion protein, RSV glycoprotein G, RIP1, RIP3 and the mixed lineage kinase domain like protein (MLKL), and horseradish peroxidase or fluorescent labeled secondary antibodies of goat anti-mouse IgG, goat anti-rabbit IgG and rabbit anti-goat IgG were purchased from Santa Cruz Biotechnology. Caspase inhibitor zVAD-fmk (zVAD), necroptosis blocking agent necrostatin-1-fmk (Nec-1) and cathepsin D inhibitor pepstatin A (PepA) were purchased from Santa Cruz Biotechnology, TNF-α and Bovine serum albumin (BSA) from Sigma-Aldrich, and propidium iodide (PI) from Beyotime Institute of Biotechnology, China.

Wang W., Wang W.H., Azadzoi K.M., Su N., Dai P., Sun J., Wang Q., Liang P., Zhang W., Lei X., Yan Z, & Yang J.H. (2016). Activation of innate antiviral immune response via double-stranded RNA-dependent RLR receptor-mediated necroptosis. Scientific Reports, 6, 22550.

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PLGA-PEG Nanoformulation for Alzheimer's

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Poly (lactide-co-glycolide) (PLGA)–PEG, sodium deoxycholate, Aβ_1–42 peptide and dichloromethane (DCM) were purchased from Sigma. All other chemicals used were of analytical grades. The anti-Bax, anti-Bcl-2, anti-APP, anti-BACE-1, anti-Nrf2, anti-HO-1, anti-p-NF-kB 65, anti-p-JNK, anti-TNFα, anti-iNOS, anti-p-P38, antibodies were purchased from Santa Cruz Biotechnology. Anti-caspase-3 and anti-actin antibodies were bought from Cell Signaling and anti-8-oxoguanine (anti-8-Oxo-G) were purchased from (Millipore, Billerica, MA, USA). The secondary antibodies used in our experiments were goat anti-mouse IgG, goat anti-rabbit IgG and rabbit anti-goat IgG, purchased from Santa Cruz Biotechnology.

Amin F.U., Shah S.A., Badshah H., Khan M, & Kim M.O. (2017). Anthocyanins encapsulated by PLGA@PEG nanoparticles potentially improved its free radical scavenging capabilities via p38/JNK pathway against Aβ1–42-induced oxidative stress. Journal of Nanobiotechnology, 15, 12.

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Western Blot Antibody Protocol

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The primary antibodies used in the Western blot analysis are explained in Table 1. The secondary antibodies used in our experiments, goat anti-mouse IgG, goat anti-rabbit IgG, and rabbit anti-goat IgG were purchased from Santa Cruz Biotechnology.

Ahmad A., Ali T., Rehman S.U, & Kim M.O. (2019). Phytomedicine-Based Potent Antioxidant, Fisetin Protects CNS-Insult LPS-Induced Oxidative Stress-Mediated Neurodegeneration and Memory Impairment. Journal of Clinical Medicine, 8(6), 850.

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Molecular Mechanisms in Colon Cancer

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The human colon cancer cell line LoVo was obtained from the American Type Culture Collection (ATCC) (Rockville, MD, USA). LoVo cells were established from a metastatic nodule resected from a 56-year-old colon adenocarcinoma patient.
We utilized antibodies against the following proteins: phospho-PI3K, phospho-Akt, COX2, GSK3β, β-catenin, LEF-1 and HADAC-1 (Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA); EP-2 and EP-4 (Cayman Chemical Company, Ann Arbor, MI, USA); and TCF-4 (Cell Signaling Technology, Inc., Beverly, MA, USA). Antibodies to α-tubulin or β-actin (Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA) were used as loading controls. The goat anti-mouse IgG, goat anti-rabbit IgG and rabbit anti-goat IgG antibodies, all conjugated to horseradish peroxidase, were purchased from Santa Cruz Biotechnology, Inc. in California, USA.

Hsu H.H., Lin Y.M., Shen C.Y., Shibu M.A., Li S.Y., Chang S.H., Lin C.C., Chen R.J., Viswanadha V.P., Shih H.N, & Huang C.Y. (2017). Prostaglandin E2-Induced COX-2 Expressions via EP2 and EP4 Signaling Pathways in Human LoVo Colon Cancer Cells. International Journal of Molecular Sciences, 18(6), 1132.

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Immunoblotting Procedure for Protein Analysis

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Immunoblotting was performed as previously described (Badshah et al., 2015 (link); Ali et al., 2018 (link)). Briefly, the protein concentrations for both cortical and hippocampi were measured through a Bio-Rad protein assay kit (Bio-Rad Laboratories, CA, USA). Equal amounts of protein (10–30 μg) underwent sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using 4–12% Bolt™ Mini Gels (Novex, Life Technologies). The membranes were blocked in 5% (w/v) skim milk to reduce nonspecific binding and incubated with primary antibodies (details available in Table 1) overnight at 4°C. After undergoing a reaction with a horseradish peroxidase-conjugated secondary antibody (goat anti-mouse IgG, goat anti-rabbit IgG, and rabbit anti-goat IgG were purchased from Santa Cruz Biotechnology), as appropriate, the proteins were detected using an ECL detection reagent according to the manufacturer’s instructions (Amersham Pharmacia Biotech, Uppsala, Sweden). Then, X-ray films were scanned, and the optical densities of the bands were analyzed through densitometry using the computer-based Sigma Gel program, version 1.0 (SPSS, Chicago, IL, USA).

Ali T., Khan A., Alam S.I., Ahmad S., Ikram M., Park J.S., Lee H.J, & Kim M.O. (2021). Cadmium, an Environmental Contaminant, Exacerbates Alzheimer’s Pathology in the Aged Mice’s Brain. Frontiers in Aging Neuroscience, 13, 650930.

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TGF-β1 Signaling Pathway Modulation

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TGF-β1 was obtained from R&D Systems (Minneapolis, MN). The TGF-β RI kinase inhibitor VI SB431542 was obtained from Calbiochem (616461, Calbiochem). The selective PKA inhibitor H-89 was obtained from abcam (Cambridge, MA). Forskolin (F6886, Sigma), and 8-bromo (Br)-cAMP (B-5380, Sigma) were each dissolved in 100% DMSO to prepare 100 mM stock solutions and were stored at -20°C. The ERK1/2 inhibitor PD98059 (513000, Calbiochem) and the p38 inhibitor SB203580 (559389, Calbiochem) were purchased from Calbiochem. Dimethylsulfoxide (DMSO) was purchased from Sigma (St. Louis, MO). Antibodies against collagen type I and FN were purchased from Abcam (Cambridge, MA). Antibodies against TGF-β1, CTGF, phosphorylated and nonphosphorylated ERK, a-smooth muscle actin (a-SMA) and β-actin were purchased from Santa Cruz Biotechnology (CA, USA). Antibodies against phosphorylated and non-phosphorylated p38, Smad3 and against phosphorylated Smad2 were purchased from Cell Signaling Technology (New England, MA). Antibodies against Smad2 were purchased from Invitrogen. Antibodies against E-cadherin were purchased from Bioworld. Goat anti-rabbit IgG, goat anti-mouse IgG and rabbit anti-goat IgG were purchased from Santa Cruz Biotechnology. BCA reagents were from Pierce (Rockford, IL). FBS was purchased from Gibco (Grand Island, NY).

Weng L., Wang W., Su X., Huang Y., Su L., Liu M., Sun Y., Yang B, & Zhou H. (2015). The Effect of cAMP-PKA Activation on TGF-β1-Induced Profibrotic Signaling. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 36(5).

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Quantitative Western Blot Analysis of ECM Proteins

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Tissues or cells were homogenized in RIPA lysis buffer containing protease inhibitor cocktail (Roche). Mitochondrial and cytosolic proteins were isolated using the Mitochondria/Cytosol Fractionation Kit according to the manufacturer's protocol (Beyotime Inst Biotech). Total protein concentrations were measured by BCA assay (Pierce) and size separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Proteins were blotted to polyvinylidene difluoride membranes (Amersham Biosciences, Piscataway, NJ, USA). Blots were incubated with antibodies against FN, collagen type I (Abcam), TGF-β1, CTGF, p-ERK, ERK2, α-smooth muscle actin (α-SMA) and β-actin (Santa Cruz), p-p38, p38, p-Smad2, p-Smad3, Smad3 (Cell Signaling Technology), Smad2 (Invitrogen), E-cadherin (Bioworld). Goat anti-rabbit IgG, goat anti-mouse IgG and rabbit anti-goat IgG (Santa Cruz) were added and the blots were developed with ECL plus kit (Amersham Biosciences).

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Quantifying MMP, TIMP, and PTEN Regulation

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MMP-2/MMP-9 inhibitor III was obtained from Merck Pharmaceuticals (Kenilworth, NJ, USA); goat MMP-9/MMP-2 polyclonal antibody, rabbit TIMP-1 polyclonal antibody, rabbit VEGF polyclonal antibody, rabbit β-actin polyclonal antibody, mouse anti-human PTEN monoclonal antibody, FITC-labeled goat anti-mouse IgG, and goat anti-rabbit IgG were from Santa Cruz Biotechnology (Dallas, TX, USA ); horseradish peroxidase-labeled goat anti-rabbit IgG, rabbit anti-goat IgG, and goat rabbit anti-mouse IgG were also from Santa Cruz Biotechnology; M-MLV reverse transcriptase was from Invitrogen Life Technologies (Carlsbad, CA, USA); human and mouse TIMP-1, mouse MMP2, mouse MMP9, human PTEN, and VEGF primers were synthesized by SBS Genetech Co., Ltd. (Beijing, China) .

Chen J.X., Cai G.Y., Chen X.M., Liu H., Chen X., Peng Y.M., Liu F.Y., Li Z, & Shi S.Z. (2015). Effect of TIMP1 transfection on PTEN expression in human kidney proximal tubular cells. Genetics and molecular research : GMR, 14(4).

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PPARγ Phosphorylation in Adipocytes

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3T3-L1 adipocyte differentiated with the above-mentioned differentiation medium were pretreated with the treatment of compounds for 24 h followed by TNFα (50 ng/mg) for 3 h. Cells were then washed with PBS and lysed with lysis buffer (Cell Signaling Technology, Danvers, MA) containing EDTA (Thermo, IL) and phosphatase inhibitors (Thermo). Aliquots of 20 μg total protein were separated on 7% SDS-PAGE gels (Life Technologies) and transferred to PVDF membranes (Life Technologies). The membranes were probed with primary antibodies followed by the appropriate HRP-conjugated secondary antibodies (goat anti-rabbit IgG and goat anti-mouse IgG, 1:3000; Santa Cruz Biotechnology, CA, USA). Blots were then developed. The primary antibodies were: anti-Ser-273 PPARγ (Bioss Antibodies) or anti-PPARγ antibody (Santa Cruz Biotechnology).

Eeda V., Wu D., Lim H.Y, & Wang W. (2019). Design, Synthesis, and Evaluation of Potent Novel Peroxisome Proliferator-Activated Receptor γ Indole Partial Agonists. Bioorganic & medicinal chemistry letters, 29(22), 126664.

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O-GlcNAc Protein Detection Protocol

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All biotinylated lectins were purchased from Vector Laboratories (CA, USA). The O-GlcNAc specific antibody CTD110.6 was purchased from Covance (WI, USA). Anti-OGT, anti-OGA, anti-Nup62 and anti-GAPDH antibodies were purchased from Cell Signaling Technology (MA, USA). HRP-conjugated goat anti-mouse IgM, goat anti-mouse IgG and goat anti-rabbit IgG were obtained from Santa Cruz Biotechnology (CA, USA). Streptavidin-HRP was purchased from Thermo (Shanghai, China). Samples were analyzed using standard procedures. Then, blots were developed with SuperSignal West Pico Chemiluminescent Substrate (Thermo).

Liu Y., Ren Y., Cao Y., Huang H., Wu Q., Li W., Wu S, & Zhang J. (2017). Discovery of a Low Toxicity O-GlcNAc Transferase (OGT) Inhibitor by Structure-based Virtual Screening of Natural Products. Scientific Reports, 7, 12334.

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