Anti laminin a c

Manufactured by Santa Cruz Biotechnology

Sourced in United States

Anti-laminin a/c is a laboratory reagent used to detect the presence of laminin a/c in biological samples. Laminin a/c is a structural protein found in the extracellular matrix. This antibody can be used in various analytical techniques, such as western blotting, immunohistochemistry, and immunocytochemistry, to identify and quantify laminin a/c expression.

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Lab products found in correlation

Ab261851, by Abcam (1 mentions) Anti rabbit igg hrp linked antibody, by Cell Signaling Technology (1 mentions) Anti flag, by Merck Group (1 mentions) Anti gapdh, by Cell Signaling Technology (1 mentions) Passive lysis buffer (plb), by Promega (1 mentions) Anti scd1, by Abcam (1 mentions) Anti yap taz, by Santa Cruz Biotechnology (1 mentions) Ecl western blotting substrate, by GE Healthcare (1 mentions) Anti akt, by Cell Signaling Technology (1 mentions) Anti erk, by Cell Signaling Technology (1 mentions) Anti p akt, by Cell Signaling Technology (1 mentions) Anti tubulin, by Merck Group (1 mentions) Anti p erk, by Cell Signaling Technology (1 mentions) Anti vinculin, by Merck Group (1 mentions) Ripa buffer, by Merck Group (1 mentions) Anti gapdh, by Merck Group (1 mentions) Protease inhibitor cocktail, by Roche (1 mentions)

Close spelling variants of this product

Anti-laminin Laminin

2 protocols using anti laminin a c

Luciferase Assay and ELISA Protocol

Cited 1 time

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To evaluate luciferase activity, cells were washed with PBS and lysed in 200 μL of Passive Lysis Buffer (E1941 Promega). Additionally, three cycles of freezing and thawing at −80°C and 37°C respectively were performed to enhance cell lysis. Finally, Renilla and Firefly luciferases were measured according to manufacturer’s instructions of the Dual Renilla Luciferase Reporter Assay (E1960 Promega) in a luminometer (Orion L Microplate Luminometer; Berthold Detection Systems).
For ELISA, cell supernatant was collected 48 h post transfection, centrifuged at 4,000 ×g for 10 min at 4°C, aliquoted, and stored at −20°C. Human CTGF ELISA was performed with a commercial kit (ab261851; Abcam) following manufacturer’s instructions. Antibodies used for western-blot⁴³ (link) were anti-FLAG (F3165; Sigma) diluted 1:1,000, anti-U1A (sc101149 from Santa Cruz and ab166890 from Abcam) diluted 1:1,000, anti-U170K (sc-9571; Santa Cruz) diluted 1:200, anti-U1C (sc-101549; Santa Cruz) diluted 1:200, anti-GAPDH (5174; Cell Signaling) diluted 1:10,000, anti-laminin a/c (sc-7292; Santa Cruz) diluted 1:1,000, and anti-HSP90 (13171-1-AP; Cell Signaling) diluted 1:1,000, and secondary antibodies used were anti-rabbit IgG HRP-linked antibody (#7074; Cell Signaling) diluted 1:10,000 and anti-mouse IgG HRP-linked antibody (A0168; Merck) diluted 1:20,000.

Rovira E., Moreno B., Razquin N., Hjerpe R., Gonzalez-Lopez M., Barrio R., Ruiz de los Mozos I., Ule J., Pastor F., Blazquez L, & Fortes P. (2022). U1A is a positive regulator of the expression of heterologous and cellular genes involved in cell proliferation and migration. Molecular Therapy. Nucleic Acids, 28, 831-846.

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Protein Expression Assay Protocol

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Protein expression assays were performed as described in Fattore et al. 2015 [39 (link)]. Briefly, cells were lysated in RIPA buffer (Sigma, St. Louis, MO, USA) containing the protease inhibitor cocktail (Hoffman-La Roche Ltd) for total lysate or using NE-PER Nuclear Cytoplasmic Extraction Reagent kit (Pierce, Rockford, IL, USA) to separate nuclear fraction from cytosol and the protein lysates were separated on SDS/PAGE acrylamide gel and transferred on Polyvinylidenedifluoride (PVDF) membranes. Membranes were blotted with different antibodies and developed with ECL western blotting substrate (GE Healthcare Life Sciences Marlborough, MA, USA). The primary antibodies used were the following: anti-GAPDH, anti-tubulin, anti-vinculin (Sigma, St. Louis, MO, USA), anti-SCD1 (Abcam, UK), anti-pAKT, anti-AKT, anti-pERK, anti-ERK (Cell Signaling Technology, Beverly, MA, USA), anti-YAP/TAZ and anti-Laminin A/C (Santa Cruz Biotechnologies, Dallas, Texas, USA). All results (mean ± SD of three independent experiments) were normalized over GAPDH, vinculin or tubulin, as specified, and expressed as fold change relative to density of control protein levels.

Pisanu M.E., Maugeri-Saccà M., Fattore L., Bruschini S., De Vitis C., Tabbì E., Bellei B., Migliano E., Kovacs D., Camera E., Picardo M., Jakopin Z., Cippitelli C., Bartolazzi A., Raffa S., Torrisi M.R., Fulciniti F., Ascierto P.A., Ciliberto G, & Mancini R. (2018). Inhibition of Stearoyl-CoA desaturase 1 reverts BRAF and MEK inhibition-induced selection of cancer stem cells in BRAF-mutated melanoma. Journal of Experimental & Clinical Cancer Research : CR, 37, 318.

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