Structured Review

Novocastra anti α sarcoglycan
Immunohistochemical investigation of CAR +/+ muscle. Transverse cryostat sections from the gastrocnemius of CAR +/+ transgenic ( A , C , E , G , I ) and wild-type ( B , D , F , H , J ) mice were subjected to immunohistochemical analysis for expression of CAR ( A , B ), dystrophin ( C , D ), <t>α-sarcoglycan</t> ( E , F ), caveolin-3 ( G , H ), and desmin ( I , J ). In the CAR +/+ transgenic muscle ( A ) most fibers show conspicuous diffuse sarcolemmal and cytoplasmic CAR immunostaining. B: In normal control muscle, only endplates show CAR immunoreactivity ( arrows ). There is substantial reduction or even absence of immunoreactive dystrophin ( C ) and α-sarcoglycan ( E ) in the CAR homozygous mice compared with wild-type control ( D , F ). CAR +/+ transgenic muscle shows marked increase of caveolin-3 sarcolemmal immunoreactivity of all muscle fibers of varying caliber ( G ) in comparison with wild-type control ( H ). A similar marked increase in sarcolemmal and cytoplasmic desmin immunoreactivity is also seen in the CAR homozygote ( I ) when compared with normal muscle ( J ).
Anti α Sarcoglycan, supplied by Novocastra, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti α sarcoglycan/product/Novocastra
Average 88 stars, based on 6 article reviews
Price from $9.99 to $1999.99
anti α sarcoglycan - by Bioz Stars, 2022-10
88/100 stars

Images

1) Product Images from "Simultaneous Dystrophin and Dysferlin Deficiencies Associated with High-Level Expression of the Coxsackie and Adenovirus Receptor in Transgenic Mice"

Article Title: Simultaneous Dystrophin and Dysferlin Deficiencies Associated with High-Level Expression of the Coxsackie and Adenovirus Receptor in Transgenic Mice

Journal: The American Journal of Pathology

doi: 10.2353/ajpath.2006.060570

Immunohistochemical investigation of CAR +/+ muscle. Transverse cryostat sections from the gastrocnemius of CAR +/+ transgenic ( A , C , E , G , I ) and wild-type ( B , D , F , H , J ) mice were subjected to immunohistochemical analysis for expression of CAR ( A , B ), dystrophin ( C , D ), α-sarcoglycan ( E , F ), caveolin-3 ( G , H ), and desmin ( I , J ). In the CAR +/+ transgenic muscle ( A ) most fibers show conspicuous diffuse sarcolemmal and cytoplasmic CAR immunostaining. B: In normal control muscle, only endplates show CAR immunoreactivity ( arrows ). There is substantial reduction or even absence of immunoreactive dystrophin ( C ) and α-sarcoglycan ( E ) in the CAR homozygous mice compared with wild-type control ( D , F ). CAR +/+ transgenic muscle shows marked increase of caveolin-3 sarcolemmal immunoreactivity of all muscle fibers of varying caliber ( G ) in comparison with wild-type control ( H ). A similar marked increase in sarcolemmal and cytoplasmic desmin immunoreactivity is also seen in the CAR homozygote ( I ) when compared with normal muscle ( J ).
Figure Legend Snippet: Immunohistochemical investigation of CAR +/+ muscle. Transverse cryostat sections from the gastrocnemius of CAR +/+ transgenic ( A , C , E , G , I ) and wild-type ( B , D , F , H , J ) mice were subjected to immunohistochemical analysis for expression of CAR ( A , B ), dystrophin ( C , D ), α-sarcoglycan ( E , F ), caveolin-3 ( G , H ), and desmin ( I , J ). In the CAR +/+ transgenic muscle ( A ) most fibers show conspicuous diffuse sarcolemmal and cytoplasmic CAR immunostaining. B: In normal control muscle, only endplates show CAR immunoreactivity ( arrows ). There is substantial reduction or even absence of immunoreactive dystrophin ( C ) and α-sarcoglycan ( E ) in the CAR homozygous mice compared with wild-type control ( D , F ). CAR +/+ transgenic muscle shows marked increase of caveolin-3 sarcolemmal immunoreactivity of all muscle fibers of varying caliber ( G ) in comparison with wild-type control ( H ). A similar marked increase in sarcolemmal and cytoplasmic desmin immunoreactivity is also seen in the CAR homozygote ( I ) when compared with normal muscle ( J ).

Techniques Used: Immunohistochemistry, Transgenic Assay, Mouse Assay, Expressing, Immunostaining

2) Product Images from "Costameric proteins in human skeletal muscle during muscular inactivity"

Article Title: Costameric proteins in human skeletal muscle during muscular inactivity

Journal: Journal of Anatomy

doi: 10.1111/j.1469-7580.2008.00921.x

Compound panel showing immunostaining of longitudinal sections of skeletal muscle fibres of patients with sensitive-motor polyneuropathy. The sections were immunolabelled with antibodies against α-sarcoglycan (A), β-sarcoglycan (B), γ-sarcoglycan
Figure Legend Snippet: Compound panel showing immunostaining of longitudinal sections of skeletal muscle fibres of patients with sensitive-motor polyneuropathy. The sections were immunolabelled with antibodies against α-sarcoglycan (A), β-sarcoglycan (B), γ-sarcoglycan

Techniques Used: Immunostaining

Compound panel showing immunohistochemical findings in normal human skeletal muscle. Skeletal muscle fibres were immunolabelled with antibodies against α-sarcoglycan (A), β-sarcoglycan (B), γ-sarcoglycan (C), δ-sarcoglycan
Figure Legend Snippet: Compound panel showing immunohistochemical findings in normal human skeletal muscle. Skeletal muscle fibres were immunolabelled with antibodies against α-sarcoglycan (A), β-sarcoglycan (B), γ-sarcoglycan (C), δ-sarcoglycan

Techniques Used: Immunohistochemistry

3) Product Images from "The administration of high-mobility group box 1 fragment prevents deterioration of cardiac performance by enhancement of bone marrow mesenchymal stem cell homing in the delta-sarcoglycan-deficient hamster"

Article Title: The administration of high-mobility group box 1 fragment prevents deterioration of cardiac performance by enhancement of bone marrow mesenchymal stem cell homing in the delta-sarcoglycan-deficient hamster

Journal: PLoS ONE

doi: 10.1371/journal.pone.0202838

Immunostaining for α-sarcoglycan and α-dystroglycan in cardiomyocytes. (a), Representative photomicrographs (×600, scale bar = 50μm) of immunostaining of α-sarcoglycan and α-dystroglycan in cardiomyocytes. (b), Quantitative analysis of immunostaining showed significantly increased staining of both α-sarcoglycan and α-dystroglycan in the HMGB1 group than the control group. HMGB1, high-mobility group box 1.
Figure Legend Snippet: Immunostaining for α-sarcoglycan and α-dystroglycan in cardiomyocytes. (a), Representative photomicrographs (×600, scale bar = 50μm) of immunostaining of α-sarcoglycan and α-dystroglycan in cardiomyocytes. (b), Quantitative analysis of immunostaining showed significantly increased staining of both α-sarcoglycan and α-dystroglycan in the HMGB1 group than the control group. HMGB1, high-mobility group box 1.

Techniques Used: Immunostaining, Staining

4) Product Images from "Adipose-derived mesenchymal stem cells preserve cardiac function via ANT-1 in dilated cardiomyopathy hamster model"

Article Title: Adipose-derived mesenchymal stem cells preserve cardiac function via ANT-1 in dilated cardiomyopathy hamster model

Journal: Regenerative Therapy

doi: 10.1016/j.reth.2021.06.006

Comparison of myocardial gene expression . The expression levels of α-sarcoglycan, β-sarcoglycan, and α-dystroglycan genes were evaluated in Groups ADSC and Sham at two and four weeks after transplantation. ANOVA and Student's t -test were used to identify significant differences, with ∗ P
Figure Legend Snippet: Comparison of myocardial gene expression . The expression levels of α-sarcoglycan, β-sarcoglycan, and α-dystroglycan genes were evaluated in Groups ADSC and Sham at two and four weeks after transplantation. ANOVA and Student's t -test were used to identify significant differences, with ∗ P

Techniques Used: Expressing, Transplantation Assay

5) Product Images from "The administration of high-mobility group box 1 fragment prevents deterioration of cardiac performance by enhancement of bone marrow mesenchymal stem cell homing in the delta-sarcoglycan-deficient hamster"

Article Title: The administration of high-mobility group box 1 fragment prevents deterioration of cardiac performance by enhancement of bone marrow mesenchymal stem cell homing in the delta-sarcoglycan-deficient hamster

Journal: bioRxiv

doi: 10.1101/390864

Immunostaining for alpha-sarcoglycan and alpha-dystroglycan in cardiomyocytes. (a), Representative photomicrographs (×600, scale bar=50μm) of immunostaining of α-sarcoglycan and α-dystroglycan in cardiomyocytes. (b), Quantitative analysis of immunohistologic signals showed significantly increased staining of both α-sarcoglycan and α-dystroglycan in HMGB1 group than the control group. HMGB1, high-mobility group box 1.
Figure Legend Snippet: Immunostaining for alpha-sarcoglycan and alpha-dystroglycan in cardiomyocytes. (a), Representative photomicrographs (×600, scale bar=50μm) of immunostaining of α-sarcoglycan and α-dystroglycan in cardiomyocytes. (b), Quantitative analysis of immunohistologic signals showed significantly increased staining of both α-sarcoglycan and α-dystroglycan in HMGB1 group than the control group. HMGB1, high-mobility group box 1.

Techniques Used: Immunostaining, Staining

6) Product Images from "The administration of high-mobility group box 1 fragment prevents deterioration of cardiac performance by enhancement of bone marrow mesenchymal stem cell homing in the delta-sarcoglycan-deficient hamster"

Article Title: The administration of high-mobility group box 1 fragment prevents deterioration of cardiac performance by enhancement of bone marrow mesenchymal stem cell homing in the delta-sarcoglycan-deficient hamster

Journal: PLoS ONE

doi: 10.1371/journal.pone.0202838

Immunostaining for α-sarcoglycan and α-dystroglycan in cardiomyocytes. (a), Representative photomicrographs (×600, scale bar = 50μm) of immunostaining of α-sarcoglycan and α-dystroglycan in cardiomyocytes. (b), Quantitative analysis of immunostaining showed significantly increased staining of both α-sarcoglycan and α-dystroglycan in the HMGB1 group than the control group. HMGB1, high-mobility group box 1.
Figure Legend Snippet: Immunostaining for α-sarcoglycan and α-dystroglycan in cardiomyocytes. (a), Representative photomicrographs (×600, scale bar = 50μm) of immunostaining of α-sarcoglycan and α-dystroglycan in cardiomyocytes. (b), Quantitative analysis of immunostaining showed significantly increased staining of both α-sarcoglycan and α-dystroglycan in the HMGB1 group than the control group. HMGB1, high-mobility group box 1.

Techniques Used: Immunostaining, Staining

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 85
    Novocastra anti α sarcoglycan mouse monoclonal antibody
    I mmunohistochemistry of dystrophin-associated proteins accompanied after 9 times i.v. injections of the 10-vPMO cocktail. Dystrophin, α1-syntrophin, nNOS, <t>α-sarcoglycan,</t> and β-dystroglycan were stained on serial sections of the muscles form nontreated and treated mdx52 mice. Biceps femoris muscles were shown as representative data in 3 treated mice. Asterisks indicate the same muscle fiber between the images. Scale bar, 100 μm.
    Anti α Sarcoglycan Mouse Monoclonal Antibody, supplied by Novocastra, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti α sarcoglycan mouse monoclonal antibody/product/Novocastra
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti α sarcoglycan mouse monoclonal antibody - by Bioz Stars, 2022-10
    85/100 stars
      Buy from Supplier

    88
    Novocastra anti α sarcoglycan
    Immunohistochemical investigation of CAR +/+ muscle. Transverse cryostat sections from the gastrocnemius of CAR +/+ transgenic ( A , C , E , G , I ) and wild-type ( B , D , F , H , J ) mice were subjected to immunohistochemical analysis for expression of CAR ( A , B ), dystrophin ( C , D ), <t>α-sarcoglycan</t> ( E , F ), caveolin-3 ( G , H ), and desmin ( I , J ). In the CAR +/+ transgenic muscle ( A ) most fibers show conspicuous diffuse sarcolemmal and cytoplasmic CAR immunostaining. B: In normal control muscle, only endplates show CAR immunoreactivity ( arrows ). There is substantial reduction or even absence of immunoreactive dystrophin ( C ) and α-sarcoglycan ( E ) in the CAR homozygous mice compared with wild-type control ( D , F ). CAR +/+ transgenic muscle shows marked increase of caveolin-3 sarcolemmal immunoreactivity of all muscle fibers of varying caliber ( G ) in comparison with wild-type control ( H ). A similar marked increase in sarcolemmal and cytoplasmic desmin immunoreactivity is also seen in the CAR homozygote ( I ) when compared with normal muscle ( J ).
    Anti α Sarcoglycan, supplied by Novocastra, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti α sarcoglycan/product/Novocastra
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti α sarcoglycan - by Bioz Stars, 2022-10
    88/100 stars
      Buy from Supplier

    90
    Novocastra anti α sarcoglycan αsg
    Sialylation of muscle sialoproteins is recovered by Ac 4 ManNAc. A , membrane proteins subjected to two-dimensional electrophoresis and transferred to PVDF membrane are probed with known sialylated proteins: <t>αSG,</t> βDG, and NEP. γSG,
    Anti α Sarcoglycan αsg, supplied by Novocastra, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti α sarcoglycan αsg/product/Novocastra
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti α sarcoglycan αsg - by Bioz Stars, 2022-10
    90/100 stars
      Buy from Supplier

    Image Search Results


    I mmunohistochemistry of dystrophin-associated proteins accompanied after 9 times i.v. injections of the 10-vPMO cocktail. Dystrophin, α1-syntrophin, nNOS, α-sarcoglycan, and β-dystroglycan were stained on serial sections of the muscles form nontreated and treated mdx52 mice. Biceps femoris muscles were shown as representative data in 3 treated mice. Asterisks indicate the same muscle fiber between the images. Scale bar, 100 μm.

    Journal: Molecular Therapy. Nucleic Acids

    Article Title: Long-Term Efficacy of Systemic Multiexon Skipping Targeting Dystrophin Exons 45–55 With a Cocktail of Vivo-Morpholinos in Mdx52 Mice

    doi: 10.1038/mtna.2014.76

    Figure Lengend Snippet: I mmunohistochemistry of dystrophin-associated proteins accompanied after 9 times i.v. injections of the 10-vPMO cocktail. Dystrophin, α1-syntrophin, nNOS, α-sarcoglycan, and β-dystroglycan were stained on serial sections of the muscles form nontreated and treated mdx52 mice. Biceps femoris muscles were shown as representative data in 3 treated mice. Asterisks indicate the same muscle fiber between the images. Scale bar, 100 μm.

    Article Snippet: In systemic treatment with the 10-vPMO cocktail, the diaphragm, biceps femoris, quadriceps, gastrocnemius, tibialis anterior, biceps brachii, triceps brachii, and heart muscles were examined 2 weeks after the final injection using anti-dystrophin (P7) antibody and antibodies against dystrophin-associated proteins: anti-α1-syntrophin rabbit polyclonal antibody (1:200, Abcam, Cambridge, UK), anti-nNOS rabbit polyclonal antibody (1:100, Invitrogen), anti-α-sarcoglycan mouse monoclonal antibody (1:10, Novocastra Laboratories), and anti-β-dystroglycan mouse monoclonal antibody (1:5, Novocastra Laboratories).

    Techniques: Staining, Mouse Assay

    Immunohistochemical investigation of CAR +/+ muscle. Transverse cryostat sections from the gastrocnemius of CAR +/+ transgenic ( A , C , E , G , I ) and wild-type ( B , D , F , H , J ) mice were subjected to immunohistochemical analysis for expression of CAR ( A , B ), dystrophin ( C , D ), α-sarcoglycan ( E , F ), caveolin-3 ( G , H ), and desmin ( I , J ). In the CAR +/+ transgenic muscle ( A ) most fibers show conspicuous diffuse sarcolemmal and cytoplasmic CAR immunostaining. B: In normal control muscle, only endplates show CAR immunoreactivity ( arrows ). There is substantial reduction or even absence of immunoreactive dystrophin ( C ) and α-sarcoglycan ( E ) in the CAR homozygous mice compared with wild-type control ( D , F ). CAR +/+ transgenic muscle shows marked increase of caveolin-3 sarcolemmal immunoreactivity of all muscle fibers of varying caliber ( G ) in comparison with wild-type control ( H ). A similar marked increase in sarcolemmal and cytoplasmic desmin immunoreactivity is also seen in the CAR homozygote ( I ) when compared with normal muscle ( J ).

    Journal: The American Journal of Pathology

    Article Title: Simultaneous Dystrophin and Dysferlin Deficiencies Associated with High-Level Expression of the Coxsackie and Adenovirus Receptor in Transgenic Mice

    doi: 10.2353/ajpath.2006.060570

    Figure Lengend Snippet: Immunohistochemical investigation of CAR +/+ muscle. Transverse cryostat sections from the gastrocnemius of CAR +/+ transgenic ( A , C , E , G , I ) and wild-type ( B , D , F , H , J ) mice were subjected to immunohistochemical analysis for expression of CAR ( A , B ), dystrophin ( C , D ), α-sarcoglycan ( E , F ), caveolin-3 ( G , H ), and desmin ( I , J ). In the CAR +/+ transgenic muscle ( A ) most fibers show conspicuous diffuse sarcolemmal and cytoplasmic CAR immunostaining. B: In normal control muscle, only endplates show CAR immunoreactivity ( arrows ). There is substantial reduction or even absence of immunoreactive dystrophin ( C ) and α-sarcoglycan ( E ) in the CAR homozygous mice compared with wild-type control ( D , F ). CAR +/+ transgenic muscle shows marked increase of caveolin-3 sarcolemmal immunoreactivity of all muscle fibers of varying caliber ( G ) in comparison with wild-type control ( H ). A similar marked increase in sarcolemmal and cytoplasmic desmin immunoreactivity is also seen in the CAR homozygote ( I ) when compared with normal muscle ( J ).

    Article Snippet: All other antibodies were purchased commercially: anti-desmin, anti-α-sarcoglycan, and anti-β-dystroglycan were from NovoCastra (Vector Laboratories, Burlington, ON, Canada); anti-dysferlin was from Vector Laboratories; anti-caveolin-3 and anti-neuronal nitric-oxide synthase (anti-nNOS) were from Transduction Laboratories (BD Biosciences, Mississauga, ON, Canada).

    Techniques: Immunohistochemistry, Transgenic Assay, Mouse Assay, Expressing, Immunostaining

    Compound panel showing immunostaining of longitudinal sections of skeletal muscle fibres of patients with sensitive-motor polyneuropathy. The sections were immunolabelled with antibodies against α-sarcoglycan (A), β-sarcoglycan (B), γ-sarcoglycan

    Journal: Journal of Anatomy

    Article Title: Costameric proteins in human skeletal muscle during muscular inactivity

    doi: 10.1111/j.1469-7580.2008.00921.x

    Figure Lengend Snippet: Compound panel showing immunostaining of longitudinal sections of skeletal muscle fibres of patients with sensitive-motor polyneuropathy. The sections were immunolabelled with antibodies against α-sarcoglycan (A), β-sarcoglycan (B), γ-sarcoglycan

    Article Snippet: The following primary antibodies were used: anti-α-sarcoglycan diluted 1:100, anti-β-sarcoglycan diluted 1:200, anti-γ-sarcoglycan diluted 1:100, anti-δ-sarcoglycan diluted 1:50, and anti-dystrophin diluted 1:20 (all from Novocastra Laboratories, Newcastle Upon Tyne, Uk); anti-agrin diluted 1:100 (Santa Cruz Biotechnology Inc., Santa Cruz, CA, USA); anti-vinculin diluted 1:100, and anti-talin diluted 1:100 (both from Sigma Chemicals, St. Louis, MO, USA); anti-α7B-integrin diluted 1:50, anti-β1D-integrin diluted 1:50, and anti-α7A-integrin diluted 1:100 (synthetic peptides from the COOH terminal region; kindly provided by the laboratory of Professor Tarone, University of Turin).

    Techniques: Immunostaining

    Compound panel showing immunohistochemical findings in normal human skeletal muscle. Skeletal muscle fibres were immunolabelled with antibodies against α-sarcoglycan (A), β-sarcoglycan (B), γ-sarcoglycan (C), δ-sarcoglycan

    Journal: Journal of Anatomy

    Article Title: Costameric proteins in human skeletal muscle during muscular inactivity

    doi: 10.1111/j.1469-7580.2008.00921.x

    Figure Lengend Snippet: Compound panel showing immunohistochemical findings in normal human skeletal muscle. Skeletal muscle fibres were immunolabelled with antibodies against α-sarcoglycan (A), β-sarcoglycan (B), γ-sarcoglycan (C), δ-sarcoglycan

    Article Snippet: The following primary antibodies were used: anti-α-sarcoglycan diluted 1:100, anti-β-sarcoglycan diluted 1:200, anti-γ-sarcoglycan diluted 1:100, anti-δ-sarcoglycan diluted 1:50, and anti-dystrophin diluted 1:20 (all from Novocastra Laboratories, Newcastle Upon Tyne, Uk); anti-agrin diluted 1:100 (Santa Cruz Biotechnology Inc., Santa Cruz, CA, USA); anti-vinculin diluted 1:100, and anti-talin diluted 1:100 (both from Sigma Chemicals, St. Louis, MO, USA); anti-α7B-integrin diluted 1:50, anti-β1D-integrin diluted 1:50, and anti-α7A-integrin diluted 1:100 (synthetic peptides from the COOH terminal region; kindly provided by the laboratory of Professor Tarone, University of Turin).

    Techniques: Immunohistochemistry

    Sialylation of muscle sialoproteins is recovered by Ac 4 ManNAc. A , membrane proteins subjected to two-dimensional electrophoresis and transferred to PVDF membrane are probed with known sialylated proteins: αSG, βDG, and NEP. γSG,

    Journal: The Journal of Biological Chemistry

    Article Title: Peracetylated N-Acetylmannosamine, a Synthetic Sugar Molecule, Efficiently Rescues Muscle Phenotype and Biochemical Defects in Mouse Model of Sialic Acid-deficient Myopathy *

    doi: 10.1074/jbc.M111.297051

    Figure Lengend Snippet: Sialylation of muscle sialoproteins is recovered by Ac 4 ManNAc. A , membrane proteins subjected to two-dimensional electrophoresis and transferred to PVDF membrane are probed with known sialylated proteins: αSG, βDG, and NEP. γSG,

    Article Snippet: After boiling, supernatants (8 μg) were electrophoresed on 5–15% gradient polyacrylamide gels (Perfect NT Gel, DRC), transferred onto PVDF membranes, blocked with 5% fat-free milk, and probed with the following Abs: anti-podocalyxin (goat polyclonal Ab, AF1556, R & D Systems), anti-actin (rabbit polyclonal Ab, 01867-96, Kantokagaku), anti-mouse neprilysin (NEP) (goat polyclonal, AF1126, R & D Systems), anti-α-sarcoglycan (αSG) (clone Ad1/20A6, NCL-a-SARC, Novocastra), anti-β-dystroglycan (βDG) (clone 43DAG1/8D5, NCL-b-DG, Novocastra), and anti-γ-sarcoglycan (γSG) (clone 35DAG/21B5, NCL-g-SARC, Novocastra).

    Techniques: Electrophoresis