α amylase

Manufactured by Santa Cruz Biotechnology

Sourced in United States

α-amylase is an enzyme that catalyzes the hydrolysis of starch into simpler sugar molecules. It plays a crucial role in the digestion and breakdown of complex carbohydrates.

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Lab products found in correlation

Enhanced chemiluminescence detection, by GE Healthcare (3 mentions) β actin, by Santa Cruz Biotechnology (3 mentions) E cadherin, by BD (2 mentions) Nanog, by Abcam (1 mentions) Western blotting detection system, by GE Healthcare (1 mentions) Mist 1, by Santa Cruz Biotechnology (1 mentions) Enhanced chemi luminescence (ecl), by GE Healthcare (1 mentions) Pvdf membrane, by Bio-Rad (1 mentions) Streptavidin biotin complex, by Thermo Fisher Scientific (1 mentions) P stat3ser727, by Santa Cruz Biotechnology (1 mentions) P stat3 tyr705, by Cell Signaling Technology (1 mentions) 3 3 diaminobenzidine (dab), by Merck Group (1 mentions) P mdm2, by Cell Signaling Technology (1 mentions) Fgfr2, by Santa Cruz Biotechnology (1 mentions) Bcl 2, by Abcam (1 mentions) Clone mm1, by Leica Biosystems (1 mentions) α smooth muscle actin, by Agilent Technologies (1 mentions) Clone 1a4, by Agilent Technologies (1 mentions) Clone a 2, by Santa Cruz Biotechnology (1 mentions) Clone 4a4, by Agilent Technologies (1 mentions)

6 protocols using α amylase

Profiling Protein Expression in Cells

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Samples
were isolated from lysates (30 μg), mixed in reducing buffer,
boiled, resolved on SDS-PAGE gels, and transferred to a PVDF membrane
by electroblotting. The blot was incubated overnight at 4 °C
in a blocking solution with primary antibodies to the following antigens:
α-amylase, AQP5, CK7, CK18, LGR5 and β-actin (Santa Cruz
Biotechnology), CD90, KRT5, NANOG, OCT4, and SOX2 (Abcam). The blots
were washed with 0.1% Tween 20 in 1 × PBS, incubated with horseradish
peroxidase-conjugated secondary antibodies that corresponded to each
primary antibody, and then subjected to enhanced chemiluminescence
detection (GE Healthcare Life Science). The protein band intensities
were quantified in three independent experiments, and the relative
ratio to the reference protein β-actin was calculated.

Shin H.S., Hong H.J., Koh W.G, & Lim J.Y. (2018). Organotypic 3D Culture in Nanoscaffold Microwells Supports Salivary Gland Stem-Cell-Based Organization. ACS Biomaterials Science & Engineering, 4(12), 4311-4320.

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Quantitative Protein Expression Analysis

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Following a conventional protocol, aliquots of 20 μg of each sample were mixed with loading buffer (60 mM Tris-HCl, 25% glycerol, 2% SDS, 14.4 mM 2-ME, 0.1% bromophenol blue), separated on 4–15% gradient SDS-PAGE gels, and transferred to a PVDF membrane (Bio-Rad Inc.). Membranes were blocked for 1 h with 5% non-fat dry milk and incubated with antibodies against α-amylase, Ptf1α and Mist-1 (Santa Cruz Biotechnology, Inc.). Blots were washed and then incubated for 1 h at room temperature with horseradish peroxidase (HRP)-conjugated anti-rabbit or anti-goat antibodies. Sites of antibody binding were visualized by enhanced chemiluminescence (ECL; GE Healthcare Life Sciences) western blotting detection system, and quantified using a densitometer analysis (ImageJ; http://rsb.info.nih.gov/ij).

Park Y.J., Koh J., Kwon J.T., Park Y.S., Yang L, & Cha S. (2017). Uncovering stem cell differentiation factors for salivary gland regeneration by quantitative analysis of differential proteomes. PLoS ONE, 12(2), e0169677.

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Immunohistochemical Staining of PCNA and p-STAT3

Cited 1 time

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Immunohistochemical staining for PCNA (sc-15402) and p-STAT3^Ser727 (sc-135649; both from Santa Cruz Biotechnology), α-amylase (cat. no. 3796) and p-STAT3^Tyr705 (cat. no. 9145; both from Cell Signaling Technology) was performed as previously described (20 (link),21 (link)). Briefly, paraffin-embedded sections (4 µm thick) were deparaffinized, rehydrated and microwave-heated for 10 min in 0.01 mol/l citrate buffer (pH 6.0) for antigen retrieval, and 3% H₂O₂ was applied to block endogenous peroxidase activity. After 15 min of incubation with blocking serum, the primary antibody or control IgG (dilution 1:50) was applied and incubated overnight at 4°C. Slides were washed three times with PBS for 5 min each time. The biotinylated secondary antibody and the streptavidin-biotin complex (Invitrogen, Carlsbad, CA, USA) were applied, each for 30 min at room temperature with an interval washing. After rinsing with PBS, the slides were immersed for 5 min in the coloring substrate 3,3′-diaminobenzidine (DAB; Sigma-Aldrich), then rinsed with distilled water, counterstained with hematoxylin, dehydrated and coverslipped.

Mattheolabakis G., Wang R., Rigas B, & Mackenzie G.G. (2017). Phospho-valproic acid inhibits pancreatic cancer growth in mice: Enhanced efficacy by its formulation in poly-(L)-lactic acid-poly(ethylene glycol) nanoparticles. International Journal of Oncology, 51(4), 1035-1044.

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Comprehensive Western Blot Analysis

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For western blot analysis, samples were isolated from the lysate (30 μg), mixed in reducing buffer, boiled, resolved on sodium dodecyl sulfate polyacrylamide gel electrophoresis, and transferred to a polyvinylidene difluoride membrane by blotting. The blot was incubated overnight at 4°C in a blocking solution with primary antibodies to the following antigens: α-amylase, AQP5, ZO-1, CK7, CK18, FGF7, FGFR2, p53 upregulated modulator of apoptosis (PUMA) and β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA); E-cadherin (BD Pharmingen, San Diego, CA, USA); p53, Bax (Abcam, England); Bcl-2, Cytochrome C, Cleaved caspase-9 and Cleaved caspase-3, protein kinase B (PI3K), p-PI3K, Akt, p-Akt and murine double minute 2 (MDM2), p-MDM2 (Cell signaling, Danvers, MA, USA). After washing the blots with 0.1% Tween 20 in 1×PBS, they were incubated with horseradish peroxidase-conjugated secondary antibodies corresponding to each primary antibody, after which they were subjected to enhanced chemiluminescence detection (GE Healthcare Life Science, USA).

Choi J.S., Shin H.S., An H.Y., Kim Y.M, & Lim J.Y. (2017). Radioprotective effects of Keratinocyte Growth Factor-1 against irradiation-induced salivary gland hypofunction. Oncotarget, 8(8), 13496-13508.

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Comprehensive Immunohistochemical Panel for Pancreatic Tissues

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The primary antibodies; AQP5 (1:500 dilution; #AQP-005, Alomone labs, Jerusalem, Israel), CK18 (1:100; Clone DC 10, DAKO-Agilent Technologies, Santa Clara, CA, USA), p63 (1:100; Clone 4A4, DAKO), α-Smooth Muscle Actin (1:100; Clone 1A4, DAKO), CK19 (1:100; Clone A-3, Santa Cruz Biotechnology, Santa Cruz, CA, USA), α-amylase (1:200; Clone G-10, Santa Cruz Biotechnology), SOX9 (1:100; #AB5535, Millipore, Burlington, MA, USA), SOX10 (1:100; Clone A-2, Santa Cruz Biotechnology), β-Catenin (1:100; #610154, BD Biosciences, Franklin Lakes, NJ, USA), Ki67 (1:50; Clone MM1, Leica Biosystems, Deer Park, IL, USA). The secondary antibodies; horseradish peroxidase (HRP)-conjugated polymer anti-rabbit and -mouse antibodies were purchased from DAKO-Agilent Technologies.

Yoshimoto S., Taguchi M., Sumi S., Oka K, & Okamura K. (2023). Establishment of a novel protocol for formalin-fixed paraffin-embedded organoids and spheroids. Biology Open, 12(5), bio059882.

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Western Blot Analysis of 2D and 3D SGSC

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Samples of SGSCs^2D and SGSCs^3D were isolated from the lysate (30 μg), mixed in reducing buffer, boiled, resolved on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) gels, and transferred to a polyvinylidene fluoride membrane by blotting. The blot was incubated overnight at 4 °C in blocking solution with primary antibodies to the following antigens: α-amylase, AQP5, TJP1, β-catenin, lamin-B1, and β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA); E-cadherin (BD Biosciences); KRT5, NANOG, POU5F1, and SOX2 (Abcam, Cambridge, UK); WNT3A, AXIN2, and p-GSK3β (Cell Signaling Technology, Danvers, MA, USA); and LGR5 (Thermo Scientific, Waltham, MA, USA). The blots were washed with 0.1% Tween 20 in 1× PBS, incubated with horseradish peroxidase-conjugated secondary antibodies corresponding to each primary antibody, and subjected to enhanced chemiluminescence detection (GE Healthcare Life Science, Piscataway, NJ, USA). The protein band intensities were quantified in three independent experiments, and the relative ratios were calculated using β-actin as a reference.

Shin H.S., Lee S., Hong H.J., Lim Y.C., Koh W.G, & Lim J.Y. (2018). Stem cell properties of human clonal salivary gland stem cells are enhanced by three-dimensional priming culture in nanofibrous microwells. Stem Cell Research & Therapy, 9, 74.

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