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Anti actinin h 2

Manufactured by Santa Cruz Biotechnology
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Sourced in Japan

Anti-actinin (H-2) is a mouse monoclonal antibody that recognizes the alpha-actinin protein. Alpha-actinin is a structural protein involved in the organization of the actin cytoskeleton.

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Lab products found in correlation

Goat anti mouse igg hrp, by Santa Cruz Biotechnology (2 mentions) Anti sma clone 1a4, by Merck Group (2 mentions) Anti pdcd4, by Merck Group (2 mentions) Goat anti rabbit igg hrp, by Santa Cruz Biotechnology (2 mentions) Ripa buffer, by Merck Group (2 mentions) Protease inhibitor cocktail, by Roche (2 mentions) Chemidoc xrs system, by Bio-Rad (2 mentions) Anti alk, by Cell Signaling Technology (1 mentions) Anti hsc70, by Santa Cruz Biotechnology (1 mentions) Anti mycn, by Santa Cruz Biotechnology (1 mentions) Anti met, by Cell Signaling Technology (1 mentions) Anti stat3, by Cell Signaling Technology (1 mentions) Anti gapdh clone 6c5, by Merck Group (1 mentions) Anti palk y1604, by Cell Signaling Technology (1 mentions) Anti pstat3 y705, by Cell Signaling Technology (1 mentions) Anti β actin clone ac 15, by Merck Group (1 mentions) Anti erk1 2, by Cell Signaling Technology (1 mentions) Anti p erk1 2, by Cell Signaling Technology (1 mentions) Phosstop, by Roche (1 mentions) Complete mini, by Roche (1 mentions)

3 protocols using anti actinin h 2

1

Protein Extraction and Analysis Protocol

Cited 1 time
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Total cell lysates were obtained with NP-40 lysis buffer (150 mM sodium chloride, 1.0% NP-40, 50 mM Tris, pH 8.0), supplemented with protease inhibitor cocktail (cOmplete mini, Roche) and phosphatase inhibitors (PhosSTOP, Roche). Protein samples were denatured with 2-mercaptoethanol at 95 °C for 5 min. The following antibodies were used for detection: anti-pALK Y1604 (Cell Signaling Technology), anti-ALK (Cell Signaling Technology), anti-pSTAT3Y705 (Cell Signaling Technology), anti-STAT3 (Cell Signaling Technology), anti-pERK1/2 (Cell Signaling Technology), anti-ERK1/2 (Cell Signaling Technology), anti-pAkt Y473 (Cell Signaling Technology), anti-AKT, anti-human PARP (Santa Cruz Biotechnology), anti-HDAC8 (H-145;polyclonal; Santa Cruz, Santa Cruz, CA, USA), anti-p-mTOR (Ser2448; Upstate), anti-p-S6K1 (Thr412; Upstate), anti-MET (Cell Signaling Technology), anti-MYCN (Santa Cruz), anti-ac-SMC3 (provided by Prof. K Shirahige, University of Tokyo, Tokyo, Japan) [55 (link)], anti-HSC70 (Santa Cruz), anti-β-actin (clone AC-15; Sigma), anti-actinin (H-2; Santa Cruz) and anti-GAPDH (clone 6C5; Merck).
Shen J., Najafi S., Stäble S., Fabian J., Koeneke E., Kolbinger F.R., Wrobel J.K., Meder B., Distel M., Heimburg T., Sippl W., Jung M., Peterziel H., Kranz D., Boutros M., Westermann F., Witt O, & Oehme I. (2018). A kinome-wide RNAi screen identifies ALK as a target to sensitize neuroblastoma cells for HDAC8-inhibitor treatment. Cell Death and Differentiation, 25(12), 2053-2070.
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2

Immunoblotting of Cellular Proteins

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Cell extracts were prepared with radioimmunoprecipitation assay (RIPA) buffer (Sigma) supplemented with a protease-inhibitor cocktail (Roche). For immunoblot analysis, protein samples were resolved on a 10% polyacrylamide Bis-Tris gel and transferred onto a nitrocellulose membrane. The following primary antibodies were used: anti-SMA (clone 1A4, Sigma), anti-PDCD4 (SAB1407349 Sigma), anti-SUMO (GeneScript A00640) and anti-actinin (H-2) (sc-17829, 1:2000, Santa Cruz Biotechnology). Goat anti-rabbit IgG-HRP (1:3000, Santa Cruz Biotechnology) and goat anti-mouse IgG-HRP (sc-2005, 1:3000, Santa Cruz Biotechnology) were used as secondary antibodies. All Western blots were analyzed with the ChemiDoc XRS+ System (Bio-Rad).
Chen Y., Yang F., Zubovic L., Pavelitz T., Yang W., Godin K., Walker M., Zheng S., Macchi P, & Varani G. (2016). Targeted inhibition of oncogenic miR-21 maturation with designed RNA-binding proteins. Nature chemical biology, 12(9), 717-723.
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3

Immunoblotting of Cellular Proteins

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Cell extracts were prepared with radioimmunoprecipitation assay (RIPA) buffer (Sigma) supplemented with a protease-inhibitor cocktail (Roche). For immunoblot analysis, protein samples were resolved on a 10% polyacrylamide Bis-Tris gel and transferred onto a nitrocellulose membrane. The following primary antibodies were used: anti-SMA (clone 1A4, Sigma), anti-PDCD4 (SAB1407349 Sigma), anti-SUMO (GeneScript A00640) and anti-actinin (H-2) (sc-17829, 1:2000, Santa Cruz Biotechnology). Goat anti-rabbit IgG-HRP (1:3000, Santa Cruz Biotechnology) and goat anti-mouse IgG-HRP (sc-2005, 1:3000, Santa Cruz Biotechnology) were used as secondary antibodies. All Western blots were analyzed with the ChemiDoc XRS+ System (Bio-Rad).
Chen Y., Yang F., Zubovic L., Pavelitz T., Yang W., Godin K., Walker M., Zheng S., Macchi P, & Varani G. (2016). Targeted inhibition of oncogenic miR-21 maturation with designed RNA-binding proteins. Nature chemical biology, 12(9), 717-723.
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