Mab3126

Manufactured by Merck Group

Sourced in United States

MAB3126 is a laboratory equipment product from Merck Group. It is a monoclonal antibody that can be used in various research and diagnostic applications. The core function of MAB3126 is to specifically bind and detect target molecules in biological samples.

Automatically generated - may contain errors

Lab products found in correlation

Ab24586, by BD (3 mentions) Clone35, by Merck Group (3 mentions) Mab1501, by Roche (3 mentions) Pw0930, by Roche (3 mentions) T5168, by Merck Group (3 mentions) Mg132, by Merck Group (3 mentions) Ab179513, by Abcam (1 mentions) Serca2, by Cell Signaling Technology (1 mentions) Sc 6217, by Santa Cruz Biotechnology (1 mentions) Calnexin, by Merck Group (1 mentions) Calreticulin, by Thermo Fisher Scientific (1 mentions) Phospho eif2α, by Cell Signaling Technology (1 mentions) Eif2α, by Cell Signaling Technology (1 mentions) Mab3540, by Merck Group (1 mentions) Sab4200236, by Merck Group (1 mentions) β tubulin, by Abcam (1 mentions) Pa3 900, by Thermo Fisher Scientific (1 mentions) Pa1 16927, by Thermo Fisher Scientific (1 mentions) Flag tag (flag), by Merck Group (1 mentions) β actin, by Merck Group (1 mentions)

5 protocols using mab3126

Studying Protein Modifications in Cells

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The following primary antibodies were used: mouse anti-Calnexin (Millipore, MAB3126, RRID: AB_2069152), mouse anti-Tubulin (Sigma, T5168, RRID: AB_477579), mouse anti-Actin (Millipore,MAB1501, RRID: AB_2223041), rat anti-HA-HRP (Roche, 12013819001, RRID: AB_390917), mouse anti-Myc (SIGMA, 9E10 M4439, RRID: AB_439694), mouse anti-Ubiquitin (Enzo, P4D1, PW0930, RRID: AB_1181462), rat anti-HA (Roche, 3F10, RRID: AB_390918), rabbit anti-Giantin (Abcam, ab24586, RRID: AB_448163), anti-GM130 (BD, clone35, RRID_398141), anti-FLAG (Sigma, M2, RRID_259529). The anti-HA affinity gel (Roche, 1815016001, RRID: AB_390914) or anti-MYC affinity agarose (Pierce, PIER20169) were used for immunoprecipitation.
Drugs were used as follows: MG132 at 10 µM (Sigma, C2211), 4 h at 37°C; Palmostatin B at 1 µM (Calbiochem, 178501), indicated time at 37°C; 2-Bromopalmitate at 100 µM (2-BP; Focus Biomolecules, FBM-10-3284), indicated time at 37°C.

Abrami L., Audagnotto M., Ho S., Marcaida M.J., Mesquita F.S., Anwar M.U., Sandoz P.A., Fonti G., Pojer F., Peraro M.D, & van der Goot F.G. (2021). Palmitoylated acyl protein thioesterase APT2 deforms membranes to extract substrate acyl chains. Nature chemical biology, 17(4), 438-447.

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Studying Protein Modifications in Cells

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Immunoprecipitation and Western Blotting Techniques

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The following primary antibodies are used: mouse anti-Calnexin (Millipore, MAB3126, RRID: AB_2069152), mouse anti-Tubulin (Sigma, T5168, RRID: AB_477579), mouse anti-Actin (Millipore,MAB1501, RRID: AB_2223041), rat anti-HA-HRP (Roche, 12013819001, RRID: AB_390917), mouse anti-Myc (SIGMA, 9E10 M4439, RRID: AB_439694), mouse anti-Ubiquitin (Enzo, P4D1, PW0930, RRID: AB_1181462), rat anti-HA (Roche, 3F10, RRID: AB_390918), rabbit anti-Giantin (Abcam, ab24586, RRID: AB_448163), anti-GM130 (BD, clone35, RRID_398141), anti-FLAG (sigma, M2, RRID_259529). The anti-HA affinity gel (Roche, 1815016001, RRID: AB_390914) or anti-MYC affinity agarose gel (Pierce, PIER20169) were used for immunoprecipitation.
Drugs were used as follows: MG132 at 10 µM (Sigma, C2211), 4 h at 37°C. Palmostatin B at 1 µM (Calbiochem, 178501), indicated time at 37°C. 2-Bromopalmitate (2-BP; Focus Biomolecules, FBM-10-3284) at 100 µM at 37°C during the indicated time.

Abrami L., Audagnotto M., S H., Marcaida M.J., Mesquita F.S., Anwar M., Sandoz P.A., Fonti G., Pojer F., Peraro M.D., & Goot F.G.v.d. (2020). Molecular mode of action of an Acyl Protein thioesterase.

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Protein Expression Detection Methods

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Expression of proteins were detected using antibodies against mouse lamin A/C (SAB4200236, Sigma‐Aldrich, St. Louis, MO, USA), human lamin A (MAB3540, Millipore, Burlington, MA, USA), Sarcolipin (ABT13, Millipore), β‐tubulin (ab179513, Abcam, Cambridge, UK), FLAG (F7425, Sigma‐Aldrich), HA (H6908, Sigma‐Aldrich), lamin B1 (ab133741, Abcam), lamin B (sc‐6217, Santa Cruz, Dallas, TX, USA), Calnexin (MAB3126, Millipore), Calreticulin (PA3‐900, Thermo Fisher Scientific), SERCA2 (4388, Cell Signaling, Danvers, MA, USA), β‐ACTIN (A5441, Sigma‐Aldrich), Grp78 (ab108613, Abcam), Chop (2891, Cell Signaling), eIF2α (2103, Cell Signaling), phospho‐eIF2α (3398, Cell Signaling), Atf4 (SC‐200, Santa Cruz), IRE1α (3294, Cell Signaling), phospho‐IRE1α (PA1‐16927, Thermo Fisher Scientific), and Gapdh (GTX100118, GeneTex, Hsinchu, Taiwan).

Wang W., Wang J., Lin W., Kao C., Hung M., Teng Y., Tsai T, & Chi Y. (2019). Progerin in muscle leads to thermogenic and metabolic defects via impaired calcium homeostasis. Aging Cell, 19(2), e13090.

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Western Blot Protein Detection Protocol

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25 µg of gradient-purified fractions were loaded onto a Bolt^TM 4–12% Bis-Tris Plus gels using a Mes buffer (Invitrogen), according to the manufacturer’s instructions. After wet electrophoretic transfer onto a Polyvinylidene Difluoride (PVDF) membrane, the membrane was blocked in a PBS containing 0,1% Tween 20 (v/v) and 5% (w/v) non-fat dried milk for 1 hour at room temperature, then soaked in a primary antibody diluted in PBS + 0,1% Tween 20 + 1% milk for 1 hour at room temperature. After three washes in PBS + 0,1% Tween 20, membranes were soaked in a secondary antibody diluted in PBS + 0,1% Tween 20 + 1% milk for 1 hour at room temperature. Membranes were processed for chemiluminescence detection using SuperSignal^TM West Dura Extended Duration Substrate (Thermo Scientific), according to manufacturer’s instructions. The immuno-reactive bands were visualized using the Amersham Imager 600 (GE Healthcare Life Sciences).
The primary antibodies were: mouse VDAC1, 1:200 (Santa Cruz Biotechnologies, Inc., SC-58649), mouse anti-Golgin-97, 1:1000 (Molecular Probes®, A21270) and mouse anti-Calnexin, 1:3000 (Millipore, MAB 3126) and 1:1000 polyclonal rabbit anti-IP₃R Ab Rbt475 (recognizing all three IP₃R isoforms; a kind gift of Dr J.B. Parys^{30 (link)}).

Shapovalov G., Ritaine A., Bidaux G., Slomianny C., Borowiec A.S., Gordienko D., Bultynck G., Skryma R, & Prevarskaya N. (2017). Organelle membrane derived patches: reshaping classical methods for new targets. Scientific Reports, 7, 14082.

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