Sc 271211

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Sc-271211 is a lab equipment product manufactured by Santa Cruz Biotechnology. It is designed for use in scientific research and laboratory applications.

Automatically generated - may contain errors

Lab products found in correlation

Protease inhibitor cocktail, by Thermo Fisher Scientific (2 mentions) Protease inhibitor cocktail set 3, by Merck Group (1 mentions) Fc dual mode imaging system, by LI COR (1 mentions) Simple stop 1, by GoldBio (1 mentions) Ripa buffer, by Merck Group (1 mentions) Ripa buffer, by Cell Signaling Technology (1 mentions) Mouse m iggκ bp hrp, by Santa Cruz Biotechnology (1 mentions) Sc 47724, by Santa Cruz Biotechnology (1 mentions) Immobilon western chemiluminescent hrp substrate, by Merck Group (1 mentions) Pvdf membrane, by Bio-Rad (1 mentions) Dc protein assay, by Bio-Rad (1 mentions) Pierce western blotting substrate, by Thermo Fisher Scientific (1 mentions) Sc 6251, by Santa Cruz Biotechnology (1 mentions) Hrp conjugated secondary antibody, by Santa Cruz Biotechnology (1 mentions) Sc 7269, by Santa Cruz Biotechnology (1 mentions) Sc 55529, by Santa Cruz Biotechnology (1 mentions)

Spelling variants of this product

Anti-Bach1 (sc-271211) (2 citations)

5 protocols using sc 271211

Mitochondrial Protein Expression Analysis

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Whole-cell or tumour lysates were prepared using RIPA buffer (Sigma, R2078) with protease inhibitor cocktail set III (Millipore, 539134) and phosphatase inhibitors (SimpleStop1, Gold Biotechnology) at 4 °C and quantified using Bradford assays before blotting using antibodies for BACH1 (sc-271211, Santa Cruz), PDK1 (C47H1) (Cell Signaling, no. 3820), PDH (Cell Signaling, #2784), PDH [p-Ser293] (Novusbio, BB110–93479), ATP5D (Abcam, ab107077), SLC25A15 (Novus Biologicals, NBP2–20387), UQCRC1 (Abeam, ab118687), COX 15 (Sigma, av46442–100UL), NDUFA9 (Abeam, abl4713), and α-tubulin (Santa Cruz, sc-28199). Blots were imaged, processed and quantified using a Licor Odyssey Fc, dual-mode imaging system (Licor).

Lee J., Yesilkanal A.E., Wynne J.P., Frankenberger C., Liu J., Yan J., Elbaz M., Rabe D.C., Rustandy F.D., Tiwari P., Grossman E.A., Hart P.C., Kang C., Sanderson S.M., Andrade J., Nomura D.K., Bonini M.G., Locasale J.W, & Rosner M.R. (2019). Effective breast cancer combination therapy targeting BACH1 and mitochondrial metabolism. Nature, 568(7751), 254-258.

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Quantifying BACH1 and FOXO3A Protein Expression

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SUDHL-5 cells were collected after 48 hours of treatment with 2.5 nmol PNA equivalent NPs dose. Cells were lysed using 1X RIPA buffer (Cell Signaling Technology) with protease inhibitor cocktail (Thermo Scientific) on ice for 30 min. The whole cell lysates were then clarified to remove cellular debris by centrifugation at 10,000 rpm for 10 min at 4°C. Protein concentration was measured using DC protein assay (#5000112, Bio-Rad). Equal amount of proteins (30 μg) were separated using SDS/PAGE 4–20% MP TGX Stain-Free gels (Bio-Rad) and transferred to PVDF membrane (Bio-Rad). After the transfer of proteins, blots were blocked using 5% milk in 1X tris-buffered saline (TBS) for one hour at RT. BACH1 protein was probed using mouse monoclonal primary antibody (sc-271211, Santa Cruz Biotechnology) at 1:200 dilution. FOXO3A protein was probed by mouse monoclonal antibody (66428–1-Ig, Proteintech) at 1:100 dilution. GAPDH was used as control and was detected using mouse monoclonal GAPDH antibody (sc-47724, Santa Cruz Biotechnology) at 1:2000 dilution. The desired bands were detected using Mouse m-IgGκ BP-HRP (sc-516102, Santa Cruz Biotechnology) secondary antibody (1:3000) and immobilon western chemiluminescent HRP substrate (MilliporeSigma). Intensity of bands was measured using ImageJ 1.52a software (National Institute of Health, Bethesda, MD) and normalized against GAPDH.

Malik S., Lim J., Slack F.J., Braddock D.T, & Bahal R. (2020). Next generation miRNA inhibition using short anti-seed PNAs encapsulated in PLGA nanoparticles. Journal of controlled release : official journal of the Controlled Release Society, 327, 406-419.

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Western Blot Analysis of BACH1 and GATA1

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Protein extracted from the differentiated ES cells was separated by sodium dodecyl sulphate polyacrylamide gel electrophoresis on an 8% polyacrylamide gel and transferred to a polyvinylidene difluoride membrane. The membrane was blocked with 5% dry milk and probed with a mouse monoclonal antibody against BACH1 (F-9 (sc-271211); Santa Cruz Biotechnology, Santa Cruz, CA, USA) or a goat polyclonal antibody against the C-terminus of GATA1 (C20 (sc-1233); Santa Cruz Biotechnology). The membrane was then incubated with a horseradish-peroxidase–conjugated secondary antibody and developed with enhanced chemiluminescence reagents (Pierce Western Blotting Substrate; Thermo, Yokohama, Japan). To confirm that the amount of protein in each lane was comparable, the membrane was stripped and probed with a monoclonal antibody against α-tubulin (DM-1A; ICN Biomedicals, Santa Ana, CA, USA). HEL 92.1.7 whole cell lysate and K562 nuclear extract were used as positive controls (sc-2130 and sc-2277, respectively; Santa Cruz Biotechnology). C3H10T1/2 whole cell lysate was used as a negative control.

Kazuki Y., Yakura Y., Abe S., Osaki M., Kajitani N., Kazuki K., Takehara S., Honma K., Suemori H., Yamazaki S., Sakuma T., Toki T., Shimizu R., Nakauchi H., Yamamoto T, & Oshimura M. (2014). Down syndrome-associated haematopoiesis abnormalities created by chromosome transfer and genome editing technologies. Scientific Reports, 4, 6136.

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Immunohistochemical Analysis of KRAS-mutant NSCLC Biomarkers

Cited 1 time

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Human KRAS-mutant NSCLC biopsy sections and linked clinical data (Supplemental Table 2) for 20 patients were obtained from the Zhengzhou University Cancer Biobank. Samples were dehydrated, formalin-fixed, and paraffin-embedded, and 5 μm serial sections were mounted onto glass slides. Sections were incubated with primary antibodies recognizing BACH1 (sc-271211, Santa Cruz Biotechnology, 1:200); VEGFA (sc-7269, Santa Cruz Biotechnology, 1:200); and VEGFR2 (sc-6251, Santa Cruz Biotechnology, 1:200) at 4°C overnight, followed by incubation with HRP-conjugated secondary antibodies (Zhong-shan Golden Bridge) for 1 hour. Next, the sections were stained with 3,3′-diaminobenzidine and hematoxylin. The stained sections were then scanned using a Panoramic Confocal microscope (3DHistech). Quantification of BACH1, VEGFA, and VEGFR2 staining intensity was performed using Aipathwell digital pathology AI-based image analysis software. Each sample was assigned a score on the basis of modified H-scores [H-scores =∑ (pi × i) = (percentage of weak intensity × 1) + (percentage of moderate intensity × 2) + (percentage of strong intensity × 3)] (33 (link)–36 (link)).

Wang T., Dong Y., Huang Z., Zhang G., Zhao Y., Yao H., Hu J., Tüksammel E., Cai H., Liang N., Xu X., Yang X., Schmidt S., Qiao X., Schlisio S., Strömblad S., Qian H., Jiang C., Treuter E, & Bergo M.O. (2023). Antioxidants stimulate BACH1-dependent tumor angiogenesis. The Journal of Clinical Investigation, 133(20), e169671.

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Western Blot Analysis of BACH1 Protein

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The tissues were lysed in RIPA buffer supplemented with protease and phosphatase inhibitor at 5 mg ml⁻¹ concentration. The supernatant containing proteins was collected after centrifuging tissue lysates at 12,000 r.p.m. at 4 °C. Protein concentration was determined by the BCA protein assay kit, and 20 µg of protein samples was boiled and loaded onto SDS–PAGE gels. The gels were transferred to 0.22-µm nitrocellulose membranes and blocked with 5% non-fat milk in 1× Tris-Buffered Saline containing 0.1% Tween 20 (TBST). The membranes were incubated with primary antibodies against BACH1 (Santa Cruz Biotechnology, sc-271211) and β-tubulin (Santa Cruz Biotechnology, sc-55529) at 4 °C overnight. After three washes (15 min, 5 min and 5 min) with 1× PBS containing 0.1% Tween 20 (PBST), the membranes were incubated with a rabbit secondary antibody conjugated with horseradish peroxidase (1:2,000) for 1 h, followed by three washes (15 min, 5 min and 5 min) with PBST. A chemiluminescence reagent kit was used to visualize protein bands with horseradish peroxidase secondary antibodies.

Wan Y., Cohen J., Szenk M., Farquhar K.S., Coraci D., Krzysztoń R., Azukas J., Van Nest N., Smashnov A., Chern Y.J., De Martino D., Nguyen L.C., Bien H., Bravo-Cordero J.J., Chan C.H., Rosner M.R, & Balázsi G. (2023). Nonmonotone invasion landscape by noise-aware control of metastasis activator levels. Nature Chemical Biology, 19(7), 887-899.

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