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human skeletal muscle myoblast cell lines  (Lonza)


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    Lonza human skeletal muscle myoblast cell lines
    Human Skeletal Muscle Myoblast Cell Lines, supplied by Lonza, 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/product/human+skeletal+muscle+myoblast+cell+lines/human+skeletal+myoblasts/10__1016_slash_j__aehs__2024__01__006-83-1-10
    Average 90 stars, based on 1 article reviews
    human skeletal muscle myoblast cell lines - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Cell Culture:

    Article Title: Circulating exosome-like vesicle and skeletal muscle microRNAs are altered with age and resistance training.
    Article Snippet: The samples were then heated at 95°C with Laemmli buffer (Fischer Scientific, AAJ61337AC) to dissociate the magnetic beads from the ELVs and then loaded onto gel electrophoresis columns. .. Cell culture and myoblast characteristics Two human skeletal muscle myoblast cell lines were purchased from Lonza (Basle, Switzerland, CC-2580) and cultured in a humidified incubator at 37°C and 5% CO2 in culture media. ..

    Article Title: Pericytes express markers of cellular proliferation without expansion of the pool in response to exercise-induced skeletal muscle damage
    Article Snippet: .. Two human skeletal muscle myoblast cell lines were purchased from Lonza (Basle, Switzerland, CC-2580) and cultured in a humidified incubator at 37 °C and 5% CO2 in culture media. ..



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    ( A , B ) Representative immunoblot ( n = 4–6) of immunoprecipitates (IP) of CHC22, from control HeLa cells ( A ) and differentiated human skeletal muscle cell line <t>AB1190</t> (Myotubes) ( B ). Samples were immunoblotted for CHC22, SNX5, SNX6, and tubulin. Lanes show Input (5%), bead-only (no antibody) control (Bead) and CHC22 immunoprecipitate (22 IP). The migration positions of MW markers are indicated at the left in kilodaltons (kD). ( C ) The structure of a single clathrin triskelion formed from three clathrin heavy chains with the Hub region indicated by red dotted triangle and the trimerization domain (TxD), magenta), proximal leg region (dark blue), knee and distal leg regions (grey) and terminal domain (light blue), based on PDB 31YV (Fotin et al, ). ( D ) AlphaFold-generated model of the interaction between CHC22 Hub (blue proximal leg residues 1278–1519 and magenta TxD residues 1520–1640) and the BAR domain of SNX5 (residues 202–404, orange). Two angles of view are displayed. ( E ) Representative immunoblot ( n = 3–5) of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub (22 Hub) or CHC17 Hub (17 Hub) immobilized on Ni-NTA beads. Purified protein input (2%) and bead-only (no Hub immobilized) control (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. (F) Representative immunoblot of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub or CHC22 TxD immobilized on Ni-NTA beads ( n = 3). Purified protein input (2%) and beads without CHC22 fragment added (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. .
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    ( A , B ) Representative immunoblot ( n = 4–6) of immunoprecipitates (IP) of CHC22, from control HeLa cells ( A ) and differentiated human skeletal muscle cell line <t>AB1190</t> (Myotubes) ( B ). Samples were immunoblotted for CHC22, SNX5, SNX6, and tubulin. Lanes show Input (5%), bead-only (no antibody) control (Bead) and CHC22 immunoprecipitate (22 IP). The migration positions of MW markers are indicated at the left in kilodaltons (kD). ( C ) The structure of a single clathrin triskelion formed from three clathrin heavy chains with the Hub region indicated by red dotted triangle and the trimerization domain (TxD), magenta), proximal leg region (dark blue), knee and distal leg regions (grey) and terminal domain (light blue), based on PDB 31YV (Fotin et al, ). ( D ) AlphaFold-generated model of the interaction between CHC22 Hub (blue proximal leg residues 1278–1519 and magenta TxD residues 1520–1640) and the BAR domain of SNX5 (residues 202–404, orange). Two angles of view are displayed. ( E ) Representative immunoblot ( n = 3–5) of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub (22 Hub) or CHC17 Hub (17 Hub) immobilized on Ni-NTA beads. Purified protein input (2%) and bead-only (no Hub immobilized) control (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. (F) Representative immunoblot of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub or CHC22 TxD immobilized on Ni-NTA beads ( n = 3). Purified protein input (2%) and beads without CHC22 fragment added (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. .
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    human skeletal muscle myoblasts cell line hsmm  (Lonza)
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    ( A , B ) Representative immunoblot ( n = 4–6) of immunoprecipitates (IP) of CHC22, from control HeLa cells ( A ) and differentiated human skeletal muscle cell line <t>AB1190</t> (Myotubes) ( B ). Samples were immunoblotted for CHC22, SNX5, SNX6, and tubulin. Lanes show Input (5%), bead-only (no antibody) control (Bead) and CHC22 immunoprecipitate (22 IP). The migration positions of MW markers are indicated at the left in kilodaltons (kD). ( C ) The structure of a single clathrin triskelion formed from three clathrin heavy chains with the Hub region indicated by red dotted triangle and the trimerization domain (TxD), magenta), proximal leg region (dark blue), knee and distal leg regions (grey) and terminal domain (light blue), based on PDB 31YV (Fotin et al, ). ( D ) AlphaFold-generated model of the interaction between CHC22 Hub (blue proximal leg residues 1278–1519 and magenta TxD residues 1520–1640) and the BAR domain of SNX5 (residues 202–404, orange). Two angles of view are displayed. ( E ) Representative immunoblot ( n = 3–5) of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub (22 Hub) or CHC17 Hub (17 Hub) immobilized on Ni-NTA beads. Purified protein input (2%) and bead-only (no Hub immobilized) control (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. (F) Representative immunoblot of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub or CHC22 TxD immobilized on Ni-NTA beads ( n = 3). Purified protein input (2%) and beads without CHC22 fragment added (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. .
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    ( A , B ) Representative immunoblot ( n = 4–6) of immunoprecipitates (IP) of CHC22, from control HeLa cells ( A ) and differentiated human skeletal muscle cell line <t>AB1190</t> (Myotubes) ( B ). Samples were immunoblotted for CHC22, SNX5, SNX6, and tubulin. Lanes show Input (5%), bead-only (no antibody) control (Bead) and CHC22 immunoprecipitate (22 IP). The migration positions of MW markers are indicated at the left in kilodaltons (kD). ( C ) The structure of a single clathrin triskelion formed from three clathrin heavy chains with the Hub region indicated by red dotted triangle and the trimerization domain (TxD), magenta), proximal leg region (dark blue), knee and distal leg regions (grey) and terminal domain (light blue), based on PDB 31YV (Fotin et al, ). ( D ) AlphaFold-generated model of the interaction between CHC22 Hub (blue proximal leg residues 1278–1519 and magenta TxD residues 1520–1640) and the BAR domain of SNX5 (residues 202–404, orange). Two angles of view are displayed. ( E ) Representative immunoblot ( n = 3–5) of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub (22 Hub) or CHC17 Hub (17 Hub) immobilized on Ni-NTA beads. Purified protein input (2%) and bead-only (no Hub immobilized) control (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. (F) Representative immunoblot of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub or CHC22 TxD immobilized on Ni-NTA beads ( n = 3). Purified protein input (2%) and beads without CHC22 fragment added (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. .
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    ( A , B ) Representative immunoblot ( n = 4–6) of immunoprecipitates (IP) of CHC22, from control HeLa cells ( A ) and differentiated human skeletal muscle cell line <t>AB1190</t> (Myotubes) ( B ). Samples were immunoblotted for CHC22, SNX5, SNX6, and tubulin. Lanes show Input (5%), bead-only (no antibody) control (Bead) and CHC22 immunoprecipitate (22 IP). The migration positions of MW markers are indicated at the left in kilodaltons (kD). ( C ) The structure of a single clathrin triskelion formed from three clathrin heavy chains with the Hub region indicated by red dotted triangle and the trimerization domain (TxD), magenta), proximal leg region (dark blue), knee and distal leg regions (grey) and terminal domain (light blue), based on PDB 31YV (Fotin et al, ). ( D ) AlphaFold-generated model of the interaction between CHC22 Hub (blue proximal leg residues 1278–1519 and magenta TxD residues 1520–1640) and the BAR domain of SNX5 (residues 202–404, orange). Two angles of view are displayed. ( E ) Representative immunoblot ( n = 3–5) of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub (22 Hub) or CHC17 Hub (17 Hub) immobilized on Ni-NTA beads. Purified protein input (2%) and bead-only (no Hub immobilized) control (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. (F) Representative immunoblot of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub or CHC22 TxD immobilized on Ni-NTA beads ( n = 3). Purified protein input (2%) and beads without CHC22 fragment added (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. .
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    Lonza human skeletal muscle myoblast cell line (hsmm)
    ( A , B ) Representative immunoblot ( n = 4–6) of immunoprecipitates (IP) of CHC22, from control HeLa cells ( A ) and differentiated human skeletal muscle cell line <t>AB1190</t> (Myotubes) ( B ). Samples were immunoblotted for CHC22, SNX5, SNX6, and tubulin. Lanes show Input (5%), bead-only (no antibody) control (Bead) and CHC22 immunoprecipitate (22 IP). The migration positions of MW markers are indicated at the left in kilodaltons (kD). ( C ) The structure of a single clathrin triskelion formed from three clathrin heavy chains with the Hub region indicated by red dotted triangle and the trimerization domain (TxD), magenta), proximal leg region (dark blue), knee and distal leg regions (grey) and terminal domain (light blue), based on PDB 31YV (Fotin et al, ). ( D ) AlphaFold-generated model of the interaction between CHC22 Hub (blue proximal leg residues 1278–1519 and magenta TxD residues 1520–1640) and the BAR domain of SNX5 (residues 202–404, orange). Two angles of view are displayed. ( E ) Representative immunoblot ( n = 3–5) of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub (22 Hub) or CHC17 Hub (17 Hub) immobilized on Ni-NTA beads. Purified protein input (2%) and bead-only (no Hub immobilized) control (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. (F) Representative immunoblot of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub or CHC22 TxD immobilized on Ni-NTA beads ( n = 3). Purified protein input (2%) and beads without CHC22 fragment added (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. .
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    Image Search Results


    ( A , B ) Representative immunoblot ( n = 4–6) of immunoprecipitates (IP) of CHC22, from control HeLa cells ( A ) and differentiated human skeletal muscle cell line AB1190 (Myotubes) ( B ). Samples were immunoblotted for CHC22, SNX5, SNX6, and tubulin. Lanes show Input (5%), bead-only (no antibody) control (Bead) and CHC22 immunoprecipitate (22 IP). The migration positions of MW markers are indicated at the left in kilodaltons (kD). ( C ) The structure of a single clathrin triskelion formed from three clathrin heavy chains with the Hub region indicated by red dotted triangle and the trimerization domain (TxD), magenta), proximal leg region (dark blue), knee and distal leg regions (grey) and terminal domain (light blue), based on PDB 31YV (Fotin et al, ). ( D ) AlphaFold-generated model of the interaction between CHC22 Hub (blue proximal leg residues 1278–1519 and magenta TxD residues 1520–1640) and the BAR domain of SNX5 (residues 202–404, orange). Two angles of view are displayed. ( E ) Representative immunoblot ( n = 3–5) of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub (22 Hub) or CHC17 Hub (17 Hub) immobilized on Ni-NTA beads. Purified protein input (2%) and bead-only (no Hub immobilized) control (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. (F) Representative immunoblot of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub or CHC22 TxD immobilized on Ni-NTA beads ( n = 3). Purified protein input (2%) and beads without CHC22 fragment added (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. .

    Journal: The EMBO Journal

    Article Title: CHC22 clathrin recruitment to the early secretory pathway requires two-site interaction with SNX5 and p115

    doi: 10.1038/s44318-024-00198-y

    Figure Lengend Snippet: ( A , B ) Representative immunoblot ( n = 4–6) of immunoprecipitates (IP) of CHC22, from control HeLa cells ( A ) and differentiated human skeletal muscle cell line AB1190 (Myotubes) ( B ). Samples were immunoblotted for CHC22, SNX5, SNX6, and tubulin. Lanes show Input (5%), bead-only (no antibody) control (Bead) and CHC22 immunoprecipitate (22 IP). The migration positions of MW markers are indicated at the left in kilodaltons (kD). ( C ) The structure of a single clathrin triskelion formed from three clathrin heavy chains with the Hub region indicated by red dotted triangle and the trimerization domain (TxD), magenta), proximal leg region (dark blue), knee and distal leg regions (grey) and terminal domain (light blue), based on PDB 31YV (Fotin et al, ). ( D ) AlphaFold-generated model of the interaction between CHC22 Hub (blue proximal leg residues 1278–1519 and magenta TxD residues 1520–1640) and the BAR domain of SNX5 (residues 202–404, orange). Two angles of view are displayed. ( E ) Representative immunoblot ( n = 3–5) of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub (22 Hub) or CHC17 Hub (17 Hub) immobilized on Ni-NTA beads. Purified protein input (2%) and bead-only (no Hub immobilized) control (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. (F) Representative immunoblot of in vitro binding of full-length GST-SNX5 (right lanes) or GST alone (left lanes) to CHC22 Hub or CHC22 TxD immobilized on Ni-NTA beads ( n = 3). Purified protein input (2%) and beads without CHC22 fragment added (Bead) are shown for each prey. Samples were immunoblotted for SNX5, His-tag or GST with detected proteins indicated at the right. The position of MW markers is indicated at the left in kD. .

    Article Snippet: The human myoblast cell line AB1190 was grown in complete Skeletal Muscle Cell Growth Medium (Promocell) with provided supplemental cocktail and 10% FBS (Gibco) to reach a 15% final supplement concentration (volume/volume) (Camus et al, ).

    Techniques: Western Blot, Control, Migration, Generated, In Vitro, Binding Assay, Purification