MBP fusion proteins containing human IgSF11 (aa 262-430) were used for immunization of guinea pigs (2003), and peptides containing mouse IgSF11 (aa 399-427) were used to immunize guinea pigs (2067) and rabbits (2068 and 2070). The specificity of anti-IgSF11 antibodies (2003) was confirmed by immunoblot experiments using Igsf11−/− brain lysates. The following antibodies have been described: PSD-95 (1688) 55 (link), SAP102 (1145) 52 (link), CaMKIIα (1299) 55 (link), CASK (1640) 56 (link), GluN2B (21266) 57 (link), GluA1 (1193) 56 (link), GluA2 (1195) 56 (link), and pan-GRIP (1756) 74 (link). The following antibodies were purchased: Myc and HA rabbit polyclonal, synaptophysin (Santa Cruz sc-789, sc-805, sc-9116), HA mouse monoclonal (Boehringer Mannheim 12CA5), GluA2 (75-002), PSD-95 (75-028), PSD-93 (75-057), SAP97 (75-030), SAP102 (75-058) (NeuroMab), GluA1 (Calbiochem PC246), GluA1, GluA2, synapsin I (Millipore MAB2263, MAB397, AB1543), GluN1 (BD Pharmingen 556308), GluN2B (Invitrogen 320600), GluN2A (AGC-002), GluN2B (AGC-003) (Alomone labs), SNAP-25 (BD Transduction Laboratories 610366), MAP2, and α-tubulin (Sigma M1406, T5168).
Glun1
Manufactured by BD
Sourced in United States
The GluN1 is a laboratory equipment product manufactured by BD. It is designed to detect and measure the presence of the GluN1 subunit, which is a critical component of the N-methyl-D-aspartate (NMDA) receptor in biological samples. The GluN1 product provides researchers with a tool to study the expression and distribution of this important neurological receptor.
Automatically generated - may contain errors
Lab products found in correlation
Glun2b, by BD (2 mentions)
Glun2b, by Alomone (1 mentions)
Glun2a, by Alomone (1 mentions)
Glua1, by Merck Group (1 mentions)
Glua2, by Merck Group (1 mentions)
Anti rabbit or anti mouse igg conjugated to horse radish peroxidase, by Cell Signaling Technology (1 mentions)
Glun2a, by Merck Group (1 mentions)
Polyvinylidene difluoride membrane, by Bio-Rad (1 mentions)
Image station 4000mm, by Kodak (1 mentions)
Infrared conjugated secondary antibodies, by LI COR (1 mentions)
Odyssey system, by LI COR (1 mentions)
Gapdh, by Abcam (1 mentions)
4 protocols using glun1
1
Characterization of IgSF11 Antibodies
2
Immunocytochemistry for AMPAR and NMDAR
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Immunocytochemistry was performed as described.27 (link) Cells were incubated in commercial AMPAR or NMDAR antibody (GluA2: 07-598, 1:1000, Millipore, Billerica, MA; GluA1: AB1504, 1:500, Millipore; GluN1: 556308, 1:1000, BD Biosciences, San Jose, CA) and CSF (range 1:10–1:100) in 1% bovine serum albumin in PBS overnight, 4°C. Each experiment included CSF from at least one individual without anti-AMPAR encephalitis; none showed CSF staining of AMPARs. Staining intensity was quantified using ImageJ software (National Institutes of Health, Bethesda, MD) as previously described.27 (link)
3
Immunoblotting Quantification of Glutamate Receptors
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Immunoblotting was performed as previously described [19 (link)]. Protein samples (50 μg) were denatured, subjected to PAGE, and transferred to polyvinylidene difluoride membranes (Bio-Rad, Hercules, CA, USA). Membranes were incubated with primary antibodies to GluN1 (BD Biosciences, Cayey, Puerto Rico), GluN2A (Sigma), or GluN2B (BD Biosciences) at 4 °C overnight, and then anti-rabbit or anti-mouse IgG conjugated to horseradish peroxidase (Cell Signaling Technology) for 2 h at room temperature. Chemiluminescence (Visualizer Millipore, Charlottesville, VA, USA) was captured and quantified using a Kodak Imagestation 4000 MM.
4
BNST Protein Extraction and Analysis
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For protein extraction, 0.33 mm tissue punches (slice thickness, 500 μm) obtained from the dlBNST 4–5 h following the final vapor chamber session were homogenized in homogenization buffer. Proteins were resolved by SDS-PAGE (10%) and transferred to nitrocellulose membranes, which were blocked in 5% milk in TBST and incubated with the appropriate primary and secondary antibodies; infrared-conjugated secondary antibodies (LiCor Biosciences, Lincoln, NE, United States) were used for detection with the Odyssey system (LiCor Biosciences). Densitometry was performed using Image J (National Institutes of Health, Bethesda, MD, United States) on images linearly adjusted for brightness and contrast. To combine blocks of experiments across blots, signals were normalized to GAPDH (1:10 000; Abcam, Cambridge, MA, United States) and calculated as a percentage of the control values on their respective blot. The following primary antibodies were used: GluN1 (1:2000; BD, Franklin Lakes, NJ, United States), GluN2B (1:2000; BD), and GluN2A (1:2000; Millipore Sigma, Burlington, MA, United States) (Wills et al., 2012 (link)).
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