Anti spectrin mab1622

Manufactured by Merck Group

Sourced in United Kingdom

Anti-spectrin MAB1622 is a monoclonal antibody that recognizes the spectrin protein. Spectrin is a structural protein found in the cytoskeleton of cells. This antibody can be used in various laboratory applications to detect and analyze spectrin in biological samples.

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Lab products found in correlation

Mg132, by Merck Group (2 mentions) Anti ubiquitin ab134953, by Abcam (2 mentions) Anti p62 sqstm1 p0067, by Merck Group (2 mentions) Anti ha epitope tag 16b12, by BioLegend (2 mentions) Chloroquine, by Merck Group (1 mentions) Halt protease inhibitor, by Thermo Fisher Scientific (1 mentions) Irdye 800cw secondary antibody, by LI COR (1 mentions) Anti caspase 12, by Cell Signaling Technology (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Irdye 680lt, by LI COR (1 mentions) Anti p62 gp62 c, by Progen Biotechnik (1 mentions) Bestatin, by Merck Group (1 mentions) Pepstatin, by Merck Group (1 mentions) Hrp conjugated anti mouse and anti rabbit igg, by Cytiva (1 mentions)

Spelling variants of this product

MAB1622 (12 citations) Anti-spectrin (7 citations) Spectrin (5 citations)

3 protocols using anti spectrin mab1622

Analyzing Autophagy and Ubiquitination Dynamics

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Commercially available antibodies were used in Western blots (WBs), for the detection of sacsin (anti-sacsin AbC ab181190, Abcam, Cambridge, UK), spectrin (anti-spectrin MAB1622, Merck Millipore, Burlington, MA), ubiquitinated proteins (anti-ubiquitin ab134953, Abcam), p62 (anti-p62/SQSTM1 P0067, Merck Millipore), LC3I-II (anti-LC3A/B ab58610, Abcam), and HA (anti-HA Epitope Tag 16b12, Biolegend, San Diego, CA). Secondary antibodies included horseradish peroxide–conjugated anti-mouse and anti-rabbit immunoglobulin G (Amersham Bioscience, Buckinghamshire, UK).
In vitro treatments were carried out with different compounds: 1 µM MG-132, 24 or 3 hours (Merck Millipore); 20 µM chloroquine, 24 hours (Merck Millipore); or together (0.25 µM MG-132 + 10 µM chloroquine, 18 hours). After the treatments, cells were harvested and lysed for biochemical assays.

Longo F., De Ritis D., Miluzio A., Fraticelli D., Baets J., Scarlato M., Santorelli F.M., Biffo S, & Maltecca F. (2021). Assessment of Sacsin Turnover in Patients With ARSACS: Implications for Molecular Diagnosis and Pathogenesis. Neurology, 97(23), e2315-e2327.

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Western Blot Detection of Cell Proteins

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Lenses were re-suspended (50 μl, 10 min) in detergent lysis buffer (1% IGEPAL, 50 mM Tris-HCL, 150 mM NaCl, pH 7.8) containing Halt Protease Inhibitor (ThermoFisher) then centrifuged (10,000 × g, 10 min) to pellet cell nuclei. Post-nuclear lysate was removed and soluble protein concentration was determined using the Non-interfering assay (G-Bioscience, St. Louis, MO). Soluble proteins (20-40 μg) and molecular weight markers (10-250 kDa, Li-Cor, Lincoln, NE) were separated on SDS-PAGE gels (4-12% gradient mini-gels, ThermoFisher) then transferred onto nitrocellulose and serially incubated with primary antibody followed by species-appropriate IRDye 680LT and/or IRDye 800CW secondary antibody (1:30,000 dilution, Li-Cor). Protein bands were visualized using an Odyssey Infrared Imaging System (Li-Cor) running Image Studio (v 5.2) software. Primary antibodies used were, anti-caspase-12 (#2202, Cell Signaling Technology, CST, Danvers, MA), anti-spectrin (MAB1622, EMD Millipore, Billerica, MA), and anti-p62 (GP62-C, Progen, Heidelberg, Germany), and anti-β-actin (#3700, CST) to control for sample loading.

Zhou Y., Bennett T.M, & Shiels A. (2016). Lens ER-stress response during cataract development in Mip-mutant mice. Biochimica et biophysica acta, 1862(8), 1433-1442.

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Western blot analysis of autophagy markers

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Commercially available antibodies were used in Western blots (WB), for the detection of sacsin (Anti-sacsin AbC ab181190. Abcam, Cambridge, UK), spectrin (Anti-spectrin MAB1622 Merck Millipore, Burlington, MA, USA), ubiquitinated proteins (Anti-ubiquitin ab134953, Abcam), p62 (Anti-p62/SQSTM1 P0067 Merck Millipore), LC3I-II (Anti-LC3A/B ab58610. Abcam), HA (anti-HA Epitope Tag 16b12, Biolegend, San Diego, CA, USA). Secondary antibodies included HRP-conjugated anti-mouse and anti-rabbit IgG (Amersham Bioscience, Buckinghamshire, UK).
In vitro treatments were carried out with different compounds: 1 µM MG-132 24 hours or 3 hours (Merck Millipore), 20 µM Chloroquine (CQ) 24 hours (Merck Millipore) or together (0.25 µM MG-132 + 10 µM CQ, 18 hours); protease inhibitors (5 µM E64, 10 µM Bestatin, 5 µM Pepstatin, 48 hours (Merck Millipore)). After the treatments, cells were harvested and lysed for biochemical assays.

Longo F., Ritis D.D., Miluzio A., Fraticelli D., Baets J., Scarlato M., Santorelli F.M., Biffo S., & Maltecca F. (2021). Sacsin cotranslational degradation causes autosomal recessive spastic ataxia of Charlevoix-Saguenay.

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