Sc 393887

Manufactured by Santa Cruz Biotechnology

Sourced in United States

sc-393887 is a lab equipment product from Santa Cruz Biotechnology. It is a device designed for use in research and laboratory settings, but a detailed description of its core function cannot be provided while maintaining an unbiased and factual approach.

Automatically generated - may contain errors

Lab products found in correlation

Anti mouse 7076, by Cell Signaling Technology (1 mentions) Anti rabbit 7074, by Cell Signaling Technology (1 mentions) Superoxide dismutase sod assay kit, by Dojindo Laboratories (1 mentions) Prism 5, by GraphPad (1 mentions) Odyssey blocking buffer, by LI COR (1 mentions) Image studio lite 4, by LI COR (1 mentions) Bis tris gel, by Thermo Fisher Scientific (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Sc 130656, by Santa Cruz Biotechnology (1 mentions)

2 protocols using sc 393887

Acetylcholinesterase Inhibition and Neuroprotection

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Acetylthiocholine iodide, bovine serum albumin (BSA), ethylene glycol tetraacetic acid (EGTA), dimethyl sulfoxide (DMSO), thiobarbituric acid (TBA), Triton X-100, Tween 20, L-Glutathione, tetrachloro-1,1,3,3-tetraethylbenzimidazolylcarbocyanine iodide (JC-1), 5,5′-dithiobis(2-nitrobenzoic acid) (DTNB), 2′,7′-dichlorofluorescein diacetate (DCF-DA), metaphosphoric acid, and all other chemicals were obtained from Sigma-Aldrich Chemical Co. (St. Louis. MO, USA). A superoxide dismutase (SOD) assay kit was purchased from Dojindo Molecular Technologies (Kumamoto, Japan) and an adenosine triphosphate (ATP) assay kit was purchased from Promega Corporation (Madison, WI, USA). The primary antibodies [β-actin (sc-69879), phosphorylated-insulin receptor substrate (p-IRS)(ser307), phosphorylated-tau (p-tau)(ser404) (sc-12952), Acetylcholinesterase (AChE) (sc-373901), phosphorylated-protein kinase B (p-Akt) (sc-514032), amyloid-β (Aβ) (sc-28365), and insulin degradation enzyme (IDE) (sc-393887)] were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Other primary antibodies (Tumor necrosis factor alpha (TNF-α) (#3707), and phosphorylated-AMP activated kinase (p-AMPK) (#2535)) and secondary antibodies (anti-mouse (7076S) and anti-rabbit (7074S)) were purchased from Cell Signaling Technology (Danvers, MA, USA).

Park S.B., Kang J.Y., Kim J.M., Park S.K., Yoo S.K., Lee U., Kim D.O, & Heo H.J. (2019). Effect of Aruncus dioicus var. kamtschaticus Extract on Neurodegeneration Improvement: Ameliorating Role in Cognitive Disorder Caused by High-Fat Diet Induced Obesity. Nutrients, 11(6), 1319.

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Validating Insulin Degrading Enzyme in Mice

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Fifteen hypothalamic samples from a new mouse cohort (WT n = 5, KO n = 5, Atx n = 5) were used to validate insulin degrading enzyme (IDE) protein. Twenty micrograms of protein lysate was denatured in a sample buffer and heated at 95°C for 5 min. Protein samples were separated and resolved on 4–12% Bis-Tris gels (Invitrogen, Waltham, MA), and then transferred to nitrocellulose membranes overnight at 10 V. Membranes were blocked using Odyssey blocking buffer (927–40 000, LI-COR Bioscience) for 1 h at room temperature, and incubated with primary antibody against IDE protein (sc-393887, Santa Cruz) for 1 h at room temperature. The membranes were washed in TBST-T three times for 5 min each, and then incubated for 1 h at room temperature with IRDye-680 and IRDye-800 secondary antibody(925–68071 and 926–32210, LI-COR Bioscience). Membranes were scanned and visualized by Odyssey Infrared Imaging System (LI-COR Biotechnology, Lincoln, NE). Quantification was performed using LI-COR Image Studio-Lite-4.0 software. The protein density of each band was normalized to the endogenous β-actin loading control (SC-130656, Santa Cruz) on the same blot (Supporting Information Table 2). All comparisons across groups were performed by Student t-test using Prism 5.01 (GraphPad software, La Jolla, CA). Mann–Whitney correction was applied to comparisons where the variances were significantly different.

Azzam S., Schlatzer D., Nethery D., Saleh D., Li X., Akladious A., Chance M.R, & Strohl K.P. (2017). Proteomic profiling of the hypothalamus in two mouse models of narcolepsy. Proteomics, 17(13-14), 10.1002/pmic.201600478.

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