Anti mhc

Manufactured by Santa Cruz Biotechnology

Sourced in Denmark

Anti-MHC is a laboratory product designed to detect and analyze major histocompatibility complex (MHC) proteins. MHC proteins play a crucial role in the immune system's ability to recognize and respond to foreign substances. This product provides a tool for researchers to study MHC expression and function in various biological systems.

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Lab products found in correlation

Anti myogenin, by Santa Cruz Biotechnology (3 mentions) Anti myog, by Santa Cruz Biotechnology (2 mentions) Igg fc specific peroxidase, by Merck Group (2 mentions) Complete mini, by Merck Group (2 mentions) Anti active caspase 3, by Cell Signaling Technology (2 mentions) Anti mcu, by Merck Group (2 mentions) Anti ki67, by Santa Cruz Biotechnology (2 mentions) Anti mcu antibody, by Merck Group (2 mentions) Anti mcam, by Proteintech (2 mentions) Anti snai2, by Proteintech (2 mentions) Bx53 microscope, by Olympus (2 mentions) Dibutylphthalate polystyrene xylene (dpx), by Merck Group (2 mentions) Haematoxylin, by Merck Group (2 mentions) Anti ldh, by Santa Cruz Biotechnology (1 mentions) Anti nnos, by Santa Cruz Biotechnology (1 mentions) Anti sod1, by Santa Cruz Biotechnology (1 mentions) Chemidoc system, by Bio-Rad (1 mentions) Dc protein assay, by Bio-Rad (1 mentions) Enhanced chemiluminescence substrate kit, by Advansta (1 mentions) Anti sirt1, by Abcam (1 mentions)

Spelling variants of this product

Anti-β-MHC (4 citations) Anti-MHC class II (2 citations) Anti-GFP and antimyosin heavy-chain (MHC) antibodies (2 citations) Mouse anti-MHC (2 citations) Mouse monoclonal anti-MHC (2 citations) Mouse anti-MHC-I (2 citations) Anti-MHC antibodies (2 citations) Anti α-MHC (2 citations)

8 protocols using anti mhc

Muscle Protein Expression Analysis

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Samples from gastrocnemius were homogenized, and C2C12 cells were lysed in lysis buffer containing 0.15 M NaCl, 10 mM HEPES (pH 7.5). Antibodies used: anti-nNOS, anti-SOD1, anti-LDH, anti-α-syntrophyn, anti-myogenin, anti-MHC (Santa Cruz), and anti-GSNOR (Millipore). Immune-reactive bands were revealed by Chemidoc System (Bio-Rad) and quantified by densitometry using Fiji^{40 (link)}.
Protein concentration was determined by the DC™ Protein Assay (Bio-Rad).

Montagna C., Rizza S., Cirotti C., Maiani E., Muscaritoli M., Musarò A., Carrí M.T., Ferraro E., Cecconi F, & Filomeni G. (2019). nNOS/GSNOR interaction contributes to skeletal muscle differentiation and homeostasis. Cell Death & Disease, 10(5), 354.

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Protein Expression Analysis by Western Blot

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The total protein was separated by SDS‐PAGE and transferred to PVDF membranes. The membranes were incubated with the corresponding primary antibodies, namely anti‐phosphorylated (p)‐AMPK (Thr172; 1:1000; CST), anti‐AMPK (1:1000, CST), anti‐SIRT‐1 (1:1000, Abcam), anti‐p‐FOXO‐3a (Ser253; 1:500; Zen‐Bio Science), anti‐FOXO‐3a (1:1000, GeneTex), anti‐Atrogin‐1 (1:1000, Abcam), anti‐MuRF‐1 (1:1000, Proteintech), anti‐p‐IRS‐1 (Ser307; 1:500; Zen‐Bio Science), anti‐IRS‐1 (1:1000, Zen‐Bio Science), anti‐GLUT‐4 (1:500, Proteintech), anti‐MHC (1:200, Santa Cruz), anti‐MyoD (1:200, Santa Cruz), anti‐Myog (1:200, Santacruz), anti‐PGC‐1α (1:1000, Abcam), anti‐FNDC‐5 (1:1000, Abcam) and anti‐GAPDH (1:5000, Proteintech) overnight at 4°C. Then, the membranes were incubated with the secondary antibodies for 1 h at 37°C. After treatment with an enhanced chemiluminescence substrate kit (Advansta), the protein bands were detected using Fusion software.

Guo A., Li K., Tian H., Fan Z., Chen Q., Yang Y., Yu J., Wu Y, & Xiao Q. (2021). FGF19 protects skeletal muscle against obesity‐induced muscle atrophy, metabolic derangement and abnormal irisin levels via the AMPK/SIRT‐1/PGC‐α pathway. Journal of Cellular and Molecular Medicine, 25(7), 3585-3600.

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Comprehensive Protein Profiling of Cell and Tumor Lysates

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Whole-cell and tumour lysates were isolated using RIPA buffer supplemented with protease inhibitors (Complete Mini, Sigma-Aldrich Inc.) and phosphatase inhibitors including sodium pyrophosphate, β-glycerophosphate, sodium fluoride and sodium orthovanadate (Sigma-Aldrich). The following primary antibodies were used: anti-MCU (#D2Z3B 1:1000, Cell Signaling), anti-MICU1 (#HPA037479 1:1000, Sigma-Aldrich), anti-MICU2 (#ab101465 1:1000, Abcam), anti-phospho-SMAD3 (#C25A9, 1:1000, Cell Signaling), anti-SMAD3 (#9513, 1:1000, Cell Signaling), anti-MYOG (#sc-12732, 1:500, Santa-Cruz), anti-MHC (#sc-32732, 1:250, Santa-Cruz) anti-HSP60 (#611563, BD Biosciences), anti-phospho-NF-κB (#3037, 1:1000, Cell Signaling), anti-NF-κB (#ab52175, 1:500, Abcam), anti-phospho-p38 MAPK (#9211, 1:1000, Cell Signaling), anti-p38 MAPK (#9212, 1:1000, Cell Signaling), and anti-β-actin (#A2228, 1:10,000, Sigma-Aldrich). Appropriate secondary antibodies (IgG-Fc Specific-Peroxidase) of mouse or rabbit origin (Sigma-Aldrich) were used.

Chiu H.Y., Loh A.H, & Taneja R. (2022). Mitochondrial calcium uptake regulates tumour progression in embryonal rhabdomyosarcoma. Cell Death & Disease, 13(4), 419.

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Protein Analysis of Whole-Cell Lysates

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For the protein analysis of whole-cell lysates, cells were lysed in radioimmunoprecipitation assay (CWBIO, China) buffer plus ethylenediaminetetraacetic acid-free protease inhibitor cocktail (04693132001; Roche). Total proteins (10–20 μg) were re-suspended in Laemmli buffer (63 mM Tris-HCl, 10% glycerol, 2% SDS, 0.0025% bromophenol blue (pH 6.8)) and electrophoresed on SDS-polyacrylamide gels. Then, the proteins were transferred to polyvinylidene difluoride membranes. Membranes were incubated with the indicated primary antibodies and anti-mouse or anti-rabbit secondary antibodies conjugated to horseradish peroxidase. The immunoreactive bands were detected using SuperSignal™ West Pico Chemiluminescent Substrate kit (Thermo Fisher Scientific, USA) and Western Blotting Detection System (BioRad, USA). To detect the protein levels of GAPDH, MHC, and myogenin, anti-GAPDH (1:5000; Santa Cruz Biotechnology, USA), anti-MHC (1:1000; Santa Cruz Biotechnology, USA), and anti-myogenin (1:2000; Santa Cruz Biotechnology, USA) antibodies were used.

Sui Y., Han Y., Zhao X., Li D, & Li G. (2019). Long non-coding RNA Irm enhances myogenic differentiation by interacting with MEF2D. Cell Death & Disease, 10(3), 181.

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Western Blot Analysis of Myogenic Regulators

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Cells were lysed using RIPA or SDS lysis buffer supplemented with protease inhibitors (Complete Mini, Sigma-Aldrich). The following primary antibodies were used: anti-EHMT2 (#3306S, 1:300, Cell Signaling), anti-MHC (#sc-32732, 1:300, Santa Cruz Biotechnology), anti-Myogenin (#sc-12732, 1:250, Santa Cruz Biotechnology), anti-DKK1 (#sc374574, 1:300, Santa Cruz Biotechnology), anti-active-ß-catenin (#05–665, 1:500, Merck Millipore), anti-H3K9me2 (#9753S, 1:1000, Cell Signaling), anti-ß-actin (#A2228, 1:10,000; Sigma-Aldrich), and anti-H3 (#ab1791, 1:10,000; Abcam). Appropriate secondary antibodies (IgG-Fc Specific-Peroxidase) of mouse or rabbit origin (Sigma Aldrich) were used.

Pal A., Leung J.Y., Ang G.C., Rao V.K., Pignata L., Lim H.J., Hebrard M., Chang K.T., Lee V.K., Guccione E, & Taneja R. (2020). EHMT2 epigenetically suppresses Wnt signaling and is a potential target in embryonal rhabdomyosarcoma. eLife, 9, e57683.

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Immunohistochemical Analysis of ERMS Tumors

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Paraffin sections of 6 archival primary ERMS tumours from KK Women’s and Children Hospital in Singapore were analysed by IHC using anti-MCU antibody (1:50, Sigma-Aldrich). Following Institutional Review Board approval (CIRB 2014/20179), specimens were obtained from patients at KK Women’s and Children Hospital who were recruited prospectively, with written parental consent and child assent obtained. TMA (SO2082b), comprising of 27 ERMS tumour specimens, 24 ARMS tumour specimens and 8 striated muscle tissue, was purchased from US Biomax, Inc. and analysed by IHC using anti-MCU antibody (1:50, Sigma-Aldrich) following the manufacturer’s protocol. Paraffin sections from mouse xenografts were stained with haematoxylin and eosin and analysed by IHC as described [68 (link), 69 ]. Sections were incubated overnight at 4 °C with anti-MCU (1:50, Sigma-Aldrich), anti-Ki67 (1:100, Santa Cruz Biotechnology), anti-MCAM (1:200, Proteintech), anti-SNAI2 (1:100, Proteintech), anti-active caspase 3 (1:200, Cell Signaling), anti-MHC (1:200, Santa Cruz Biotechnology) antibodies using Dako REAL EnVIsion-HPR, Rabbit-Mouse kit (Dako, Denmark). Sections were counterstained with haematoxylin (Sigma-Aldrich). Slides were dehydrated and mounted using DPX (Sigma-Aldrich) and imaged using BX53 Olympus microscope at ×40 magnification.

Chiu H.Y., Loh A.H, & Taneja R. (2022). Mitochondrial calcium uptake regulates tumour progression in embryonal rhabdomyosarcoma. Cell Death & Disease, 13(4), 419.

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Immunohistochemical Analysis of ERMS Tumours

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Paraffin sections of 6 archival primary ERMS tumours from KK Women's and Children Hospital in Singapore were analysed by IHC using anti-MCU antibody (1:50, Sigma-Aldrich).
Following Institutional Review Board approval (CIRB 2014/20179), specimens were obtained from patients at KK Women's and Children Hospital who were recruited prospectively, with written parental consent and child assent obtained. TMA (SO2082b), comprising of 27 ERMS tumour specimens and 8 striated muscle tissue, was purchased from US Biomax, Inc. and analysed by IHC using anti-MCU antibody (1:50, Sigma-Aldrich) following the manufacturer's protocol. Paraffin sections from mouse xenografts were stained with haematoxylin and eosin and analysed by IHC as described [57, (link)58] (link). Sections were incubated overnight at 4°C with anti-MCU (1:50, Sigma-Aldrich), anti-Ki67 (1:100, Santa Cruz Biotechnology), anti-MCAM (1:200, Proteintech), anti-SNAI2 (1:100, Proteintech), anti-active caspase 3 (1:200, Cell Signalling), anti-MHC (1:200, Santa Cruz Biotechnology) antibodies using Dako REAL EnVIsion-HPR, Rabbit-Mouse kit (Dako, Denmark). Sections were counterstained with haematoxylin (Sigma-Aldrich). Slides were dehydrated and mounted using DPX (Sigma-Aldrich) and imaged using BX53 Olympus microscope at 40X magnification.

Chiu H.Y., Loh A.H.P., & Taneja R. (2021). Mitochondrial calcium uptake regulates tumour progression in embryonal rhabdomyosarcoma.

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Molecular Mechanisms of FoxO3 Regulation

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CTX, cycloheximide and PF-3644022 were purchased from Sigma-Aldrich. The plasmids pcDNA3-Myc6-ERK3-Flag, pcDNA3-Myc6-ERK3, pcDNA3-MK5-HA, pcDNA3-MK5-Flag, pcDNA3-MK5-HA L337A have been previously described (4, 28, 45) . pcDNA3-FoxO3-Myc was a kind gift of A. Brunet (Stanford University). pcDNA3-FoxO3-Myc S214A was generated by PCR mutagenesis. To construct the bacterial expression plasmid pGEX-mFoxO3, mouse FoxO3 was amplified by PCR using pcDNA3-FoxO3-Myc as template and subcloned into the EcoRI site of pGEX-KG. All mutations and PCR products were verified by DNA sequencing.
Commercial antibodies were obtained from the following suppliers and used at the indicated concentrations: anti-ERK3 (1/1000; cat. no. ab53277) and anti-myogenin (1/1000; cat. no. 232558) from Abcam; anti-MK5 (1/500; cat. no. sc-46667), anti-Myc (1/1000; cat. no. sc-40) and anti-Hsc70 (1/2000; cat. no. sc-7298) from Santa-Cruz Biotechnology; anti-MHC (1/1000; cat. no. MF20) and anti-Pax7 (1/100) from DSHB; anti-FoxO3 (1/1000; cat. no. 2497) and anti-phospho-Hsp27(Ser82) (1/1000; cat. no.2406) from Cell Signaling Technology; anti-HA (1/1000; cat. no. 901501) from Biolegend; anti-Flag (1/1000; cat. no. F3165), anti-laminin (1/500; cat. no. L9393) and anti-actin (1/1000; cat. no. A4700) from Sigma-Aldrich.

Soulez M., Tanguay P., Dô F., Crist C., Dort J., Kotlyarov A., Gaestel M., Dumont N.A., & Meloche S. (2021). ERK3-MK5 signaling regulates myogenic differentiation and muscle regeneration by promoting FoxO3 degradation.

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