Calbindin

Manufactured by Merck Group

Sourced in United States

Calbindin is a calcium-binding protein that plays a role in calcium homeostasis in the body. It functions as a calcium sensor and regulator, facilitating the movement and distribution of calcium ions within cells. Calbindin is commonly used in research applications to study calcium-mediated cellular processes.

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Lab products found in correlation

Neuronal nuclei (neun), by Merck Group (6 mentions) Glial fibrillary acidic protein (gfap), by Agilent Technologies (2 mentions) β actin, by Cell Signaling Technology (2 mentions) Neuronal nuclei (neun), by Cell Signaling Technology (2 mentions) Fv1200, by Olympus (2 mentions) N cadherin, by BD (2 mentions) Phospho s6, by Cell Signaling Technology (2 mentions) Gapdh, by Merck Group (2 mentions) Iba 1, by Abcam (2 mentions) Alexa fluor 488, by Thermo Fisher Scientific (2 mentions) Imager m2, by Zeiss (1 mentions) Prolong gold antifade mountant, by Thermo Fisher Scientific (1 mentions) Apotome microscope, by Zeiss (1 mentions) 4 6 diamidino 2 phenylindole (dapi), by Cell Signaling Technology (1 mentions) G3bp1, by Proteintech (1 mentions) Synaptophysin, by Cell Signaling Technology (1 mentions) Contactin2, by R&D Systems (1 mentions) Vinculin, by Cell Signaling Technology (1 mentions) Darpp32, by Abcam (1 mentions) Alexa fluor 488, by Jackson ImmunoResearch (1 mentions)

Spelling variants of this product

Mouse anti-Calbindin (10 citations) Calbindin-D28K (10 citations) Anti-calbindin-D-28K antibody (7 citations) Rabbit anti-Calbindin-D28K (5 citations) Mouse anti-calbindin-D-28K (4 citations) Rabbit anti-calbindin D-28K antibody (2 citations) Rabbit anti-Calbindin (2 citations) Anti‐calbindin‐E‐28K (KD‐15) antibody (2 citations) Mouse monoclonal calbindin-D-28K antibody (2 citations) Anti-calbindin antibody (2 citations)

20 protocols using calbindin

Immunofluorescence Staining of Tissue Sections

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Immunofluorescence was performed using sections of formalin fixed, paraffin embedded tissue generated as described above. Antigen retrieval in tissue sections was achieved using pressure-cooking in citrate buffer pH6 for 20 minutes. Tissue sections were incubated with primary antibodies for 1 hour at room temperature.
Primary antibodies included: Ki67 (1:200; Abcam, ab15580 and 1:500; Thermo Fisher Scientific, 14-5698-82), Calbindin (1:50; Millipore, AB1778), Contactin2 (1:75; R&D Systems, AF4439), Lef1 (1:500; Abcam, ab137872), Pax6 (1:200; Biolegend, 901301), G3BP1 (1:100; Proteintech, 66486-1-Ig), Gfap (1:500; Dako, Z0334), NeuN (1:200; Millipore, MAB377), Irf1 (1:100; Abcam, ab240299), Iba1 (1:500; Wako, 013-27691) and Synaptophysin (1:100; Cell Signaling, 9020). Following washing, tissue sections where then incubated for 1 hour at room temperature in secondary antibody. Secondary antibodies included Alexa 488, 594 or 680 (1:200; Invitrogen, A-21206, A-21207 or A10043). Sections were then counterstained using DAPI (Cell Signaling, 4083) and mounted using ProLong Gold antifade mountant (Thermo Fisher Scientific, P36930). Digital images of tissue sections were captured using a Zeiss ImagerM2 and Apotome microscope.

Patmore D.M., Jassim A., Nathan E., Gilbertson R.J., Tahan D., Hoffmann N., Tong Y., Smith K.S., Kanneganti T.D., Suzuki H., Taylor M.D., Northcott P, & Gilbertson R.J. (2020). DDX3X suppresses the susceptibility of hindbrain lineages to medulloblastoma. Developmental cell, 54(4), 455-470.e5.

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Comprehensive Immunohistochemical Profiling

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Primary antibodies used in this study include: 1TBP18 (QED Bioscience, 70102, 1:1000), Calbindin (Millipore, ab1778, 1:1000), DARPP32 (Abcam, ab40801, 1:1000), NeuN (Cell Signaling Technology, 24307s, 1:2000), GFP (BD Living Colors, 632376, 1:1000), RFP (Abcam, ab62341, 1:1000), vinculin (Cell Signaling Technology, 13901, 1:5000), β-actin (Cell Signaling Technology, 4967L, 1:10,000), and INPP5A (Invitrogen, PA5-45906, 1:1000), SP1 (Santa Cruz, sc-17824 X, 1:1000). Secondary antibodies were donkey anti-rabbit and donkey anti-mouse Alexa Fluor 488 or 594 from Jackson ImmunoResearch.

Liu Q., Huang S., Yin P., Yang S., Zhang J., Jing L., Cheng S., Tang B., Li X.J., Pan Y, & Li S. (2020). Cerebellum-enriched protein INPP5A contributes to selective neuropathology in mouse model of spinocerebellar ataxias type 17. Nature Communications, 11, 1101.

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Immunohistochemical Analysis of Retinal Cell Markers

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Immunohistochemistry was performed as described^{6 (link)}. Aggregates were fixed with 4% PFA and sectioned with a cryostat (Leica). Frozen sections were treated with or without heat-based antigen retrieval in Target Retrieval solution (Dako) at 105 °C for 15 min. The primary antibodies used in this study were as follows: Chx10 (sheep; 1:500; Exalpha), Rx (guinea pig; 1:2000; Takara), Pax6 (mouse; 1:1000; BD Biosciences), Mitf (mouse; 1:500; Exalpha), Crx (rabbit; 1:200; Takara), Recoverin (rabbit; 1:1000; Proteintech), NRL (goat; 1:500; R&D Systems), RXR-gamma (rabbit; 1:500; Spring Bioscience), Rhodopsin (mouse; 1:1000; Sigma; RET-P1), S-opsin (rabbit; 1:500; Millipore), L/M-opsin (rabbit; 1:500; Millipore), PKCalpha (rabbit; 1:500; Sigma), HuNu (Ms; 1:1000; Millipore), Calbindin (rabbit; 1:500; Millipore), N-cadherin (mouse; 1:500; BD Biosciences), FoxG1 (rabbit; 1:2000; Takara), Ctip2 (rat; 1:500; abcam), Tbr1 (rabbit; 1:500; abcam). Nuclear counter-staining was performed with DAPI (Nacalai). Stained sections were analyzed with a fluorescence microscope (BIOREVO; Keyence) and a confocal microscope (FV1200; Olympus). Image analyses were performed with ImageJ 1.48 v software (NIH).

Kuwahara A., Yamasaki S., Mandai M., Watari K., Matsushita K., Fujiwara M., Hori Y., Hiramine Y., Nukaya D., Iwata M., Kishino A., Takahashi M., Sasai Y, & Kimura T. (2019). Preconditioning the Initial State of Feeder-free Human Pluripotent Stem Cells Promotes Self-formation of Three-dimensional Retinal Tissue. Scientific Reports, 9, 18936.

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Immunohistochemistry of Neural Markers

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Fixed rat and mouse brains were frozen in Tissue‐Tek OCT and cryo‐sectioned into transverse 35‐μm‐thick slices. Slices were permeabilized for 2 hrs (3% bovine serum albumin and 0.2% Triton in PBS), then incubated overnight at 4°C with primary antibodies, washed in PBS and incubated 1.5 hrs in Cy3‐ and FITC‐linked secondary antibodies (Jackson Immuno‐research, West Grove, PA, USA). Primary antibodies included doublecortin (DCX), Mash1, Ngn2, calretinin (CR; Santa Cruz, Dallas, TX, USA), GFAP (BD Biosciences, San Jose, CA, USA), calbindin (CB) and NeuN (Millipore, Billerica, MA, USA). Antibody specificity was attested by published reports and manufacturer's data or tested by double labelling. Slices were mounted on slides and imaged using an Olympus‐80 fluorescence microscope equipped with FITC and Cy3 filters. Bleed‐through was minimized by dual scanning on two different FITC‐Cy3 filter sets with slightly different bandpass windows.

Rusanescu G, & Mao J. (2016). Peripheral nerve injury induces adult brain neurogenesis and remodelling. Journal of Cellular and Molecular Medicine, 21(2), 299-314.

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Purkinje Cell Quantification in Tsc1 Mutant Mice

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Mice were perfused and post-fixed with 4% paraformaldehyde. Sections were prepared by cryostat sectioning and were stained with the following antibodies: PhosphoS6 (Cell Signaling, #2211) and calbindin (Sigma, #CB955). Anti-calbindin staining was performed to identify Purkinje cells while PhosphoS6 staining was performed as a marker for mTOR signaling (increased with loss of Tsc1; reduced with rapamycin administration). Purkinje cell numbers were quantified by totaling all Purkinje neurons from midline vermis sections from mice that had been treated for 5 weeks with treatment initiation commencing at either 6 or 10 weeks of age depending on cohort in order to mirror behavioral testing paradigms.

Tsai P.T., Rudolph S., Guo C., Ellegood J., Gibson J.M., Schaeffer S.M., Mogavero J., Lerch J.P., Regehr W, & Sahin M. (2018). Sensitive Periods for Cerebellar-Mediated Autistic-like Behaviors. Cell reports, 25(2), 357-367.e4.

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Western Blot Analysis of Kidney Proteins

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Western blot analysis was performed on stage E13.5 Nf2^UB−/− kidneys or cultured Yap^UB-OE kidneys following doxycycline induction. Unless stated otherwise each western blot lane represents one animal (two kidneys). Kidneys were mechanically homogenized and lysed in RIPA buffer supplemented with proteasome and phosphatase inhibitors. Western blot analysis was performed following standard protocols with the following primary antibodies: CALBINDIN (C9848, Sigma, 1:1,000), BAF155 (SC-9748, SantaCruz Biotechnology, 1:2,000), GAPDH (R9545, Sigma, 1:7,500), HA (11867423001, Roche, 1:1,000), LATS1 (#3477, Cell Signaling Technology, 1:1,000), MST1 (#3682, Cell Signaling Technology, 1:2,000), NF2 (HPA003097, Sigma Prestige Antibodies, 1:2,000), phosho-LATS1 S909 (#9157, Cell Signaling Technology, 1:500), phospho-MST1/2 T183/T180 (#3681, Cell Signaling Technology, 1:2,000), phospho-YAP S127 (#4911, Cell Signaling Technology, 1:2,000) and YAP (sc-101199, SantaCruz Biotechnology, 1:2,000). All uncropped western blots can be found in Supplementary Fig. 8.

Reginensi A., Enderle L., Gregorieff A., Johnson R.L., Wrana J.L, & McNeill H. (2016). A critical role for NF2 and the Hippo pathway in branching morphogenesis. Nature Communications, 7, 12309.

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Antibody Characterization for Neuroscience Research

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In addition to the NRG2 antibodies described above, the commercial and custom antibodies against the following proteins were used in this study: ErbB4, mouse monoclonal Ab-77 (Thermo Fisher; 1 μg/ml), rabbit monoclonal mAB10 (1 μg/ml) ^{7 (link)} and rabbit polyclonal custom antibody 5721 (unpublished; 0.4 μg/ml); Kv2.1, mouse monoclonal (clone K89/34; NeuroMab; 1 μg/ml); rabbit polyclonal antibody against NRG1 (SC-348; Santa Cruz Biotechnology; 0.2 μg/ml); anti-V5 epitope tag (AbD Serotech; 1 μg/ml); Bassoon, rabbit polyclonal (Synaptic Systems; 1:1,000); Gephyrin, mouse monoclonal (clone mAb7a; Synaptic Systems; 1:500); PSD95, mouse monoclonal (clone 7E3-1B8; Pierce; 1:500); Calbindin, mouse monoclonal (clone CB-955; Sigma; 1:1,000); GFP, rabbit polyclonal (Molecular Probes; 1:2,000); Erk2, rabbit polyclonal (C-14; Santa Cruz; 0.2 μg/ml); phospho-Erk2, mouse monoclonal (clone E-4; Santa Cruz; 0.2 ug/ml); GAPDH, mouse monoclonal (clone 6C5; Santa Cruz; 0.2 μg/ml); clathrin heavy chain (CHC), mouse monoclonal (SC-12734; Santa Cruz; 0.1 μg/ml); GluN2A, rabbit monoclonal (clone A12W; Millipore; 1:2,000); GluN2B (clone 13; BD Biosciences; 1 μg/ml); GluA1 (AB1504; Millipore; 0.2 μg/ml).

Vullhorst D., Mitchell R.M., Keating C., Roychowdhury S., Karavanova I., Tao-Cheng J.H, & Buonanno A. (2015). A negative feedback loop controls NMDA receptor function in cortical interneurons via neuregulin 2/ErbB4 signalling. Nature Communications, 6, 7222.

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Tracking EV Biodistribution in Brain

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The EVs were labelled with PKH26 (Sigma) as per manufacturer’s instructions, and the free dye was separated from the bound dye by ultrafiltration using 10 kDa MWCO filter columns (Sartorius, Gottingen, Germany). The rats and mice (n = 2/species) were moderately anesthetized with a cocktail of ketamine, xylazine and acepromazine, and their nostrils were treated with 10 µl of hyaluronidase (Sigma-Aldrich, St. Louis, MO, USA) to enhance the permeability of the nasal mucous membrane. Thirty minutes later, labelled EVs were administered (150 × 10⁹ [~75 µg]/rat and 25 × 10⁹ [~12.5 µg]/mouse), as detailed in our recent report [22 ]. Six hours later, the animals were perfused, the brain tissues were processed for cryostat sectioning, and thirty-micrometre-thick coronal sections through the entire forebrain, midbrain and hindbrain, were collected serially. Serial sections through the entire brain were selected and processed for immunofluorescent staining using appropriate primary antibodies against NeuN (1:1000; Millipore), IBA-1 (1:1000; Abcam), GFAP (1:3000; Dako, Glostrup, Denmark), S-100β (1:1000; Sigma) and calbindin (1:500; Sigma), as described in our previous report [22 ]. The sections were examined using Z-section analysis in a confocal microscope for the distribution of EVs in different cell types (neurons, microglia and astrocytes) in multiple regions of the brain.

Upadhya R., Madhu L.N., Attaluri S., Gitaí D.L., Pinson M.R., Kodali M., Shetty G., Zanirati G., Kumar S., Shuai B., Weintraub S.T, & Shetty A.K. (2020). Extracellular vesicles from human iPSC-derived neural stem cells: miRNA and protein signatures, and anti-inflammatory and neurogenic properties. Journal of Extracellular Vesicles, 9(1), 1809064.

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Immunohistochemical Analysis of Embryonic and Postnatal Mouse Brains

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Embryonic mice were decapitated and heads were fixed in 4% paraformaldehyde (PFA) in PBS at 4°C overnight. Postnatal animals were perfused and brains were dissected out, then fixed in 4% PFA in PBS at 4°C overnight. Parasagittal sections 7μm thick were prepared from fixed tissues embedded in paraffin. Hematoxylin and eosin (H&E), immunofluorescence, and immunohistochemical staining of tissue sections were performed as previously described (Park et al., 2016a (link); Park et al., 2016b (link)). Antibodies used were Yap (1:500; abcam ab56701), BLBP (1:200; Millipore ABN14), Calbindin (1:200; Sigma, C9848), S100β (1:200; Novus Biologicals, NB110–57478), GFAP (1:200; Thermo Scientific, RB-087), BrdU (1:500; abcam, ab6326), PCNA (1:250; Proteintech, 10205–2-P), pH3 (1:500; Millipore Sigma, 06–670), NeuN (1:250; Millipore, MAB377), Pax6 (1:200; Covance, RBP-278), Sox9 (1:200; Millipore, AB5535), Pals1 (1:200; Proteintech), Pan-Crb (1:200; (Cho et al., 2012 (link))), NMIIB (1:500; Covance, PRB-445P), N-Cadherin (1:500; BD, 610920), and β-Catenin (1:500; BD, 610153). Species-specific secondary antibodies conjugated to Alexa Fluor 488 (1:250; Invitrogen) or Cy3 (1:250; Jackson Immunochemical) were used for immunofluorescence. Nuclei were stained with Hoechst 22358 (1:500; Invitrogen).

Hughes L.J., Park R., Lee M.J., Terry B.K., Lee D.J., Kim H., Cho S.H, & Kim S. (2019). Yap/Taz are required for establishing the cerebellar radial glia scaffold and proper foliation. Developmental biology, 457(1), 150-162.

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Immunohistochemistry Antibody Panel

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Primary antibodies used in this study include the following: Flag (Sigma-Aldrich, F1804), HA (Cell Signaling Technology, 3724S), Myc (Cell Signaling Technology, 2276S), calbindin (Sigma-Aldrich, C9848), vinculin (Sigma-Aldrich, V9131), NeuN (Cell Signaling Technology, 24307s), GFAP (Cell Signaling Technology, 3670S), IBA1 (Wako, 019-19741), ubiquitin (Sigma-Aldrich, 05-1307), P62 (BD Biosciences, 610832), GFP (Invitrogen, A-11122), β-actin (Cell Signaling Technology, 3700S), Tuj1 (Abcam, ab18207), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (Proteintech, 60004-1-Ig), NOTCH2NL (Gentex, GTX117659), and hnRNPM (Santa Cruz Biotechnology, sc-20002). Secondary antibodies were donkey anti-rabbit and donkey anti-mouse Alexa Fluor 488 or 594 from Jackson ImmunoResearch.

Liu Q., Zhang K., Kang Y., Li Y., Deng P., Li Y., Tian Y., Sun Q., Tang Y., Xu K., Zhou Y., Wang J.L., Guo J., Li J.D., Xia K., Meng Q., Allen E.G., Wen Z., Li Z., Jiang H., Shen L., Duan R., Yao B., Tang B., Jin P, & Pan Y. (2022). Expression of expanded GGC repeats within NOTCH2NLC causes behavioral deficits and neurodegeneration in a mouse model of neuronal intranuclear inclusion disease. Science Advances, 8(47), eadd6391.

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