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Calnexin

Calnexin is a molecular chaperone protein that plays a critical role in the quality control of protein folding and assembly in the endoplasmic reticulum (ER).
It binds to newly synthesized glycoproteins, preventing their premature exit from the ER and promoting proper folding and maturation.
Calnexin also interacts with other ER-resident proteins, such as calreticulin and ERp57, to facilitate the formation of disulfide bonds and the proper assembly of multimeric protein complexes.
This chaperone activity is essential for the maintenance of cellular homeostasis and the prevention of protein misfolding diseases.
Reasearchers can leverage PubCompare.ai's AI-driven tools to optimize their Calnexin-related studies, easily locate the best research protocols, and streamline their workflow to accelerate discovery.

Most cited protocols related to «Calnexin»

1
Isolation and Characterization of Murine Conjunctiva-Associated Lymphoid Tissue
Cited 22 times
The eyes and lids of mice (n=5 per experiment, in four independent sets of experiments, total of 20 per group, in NS, DS5, and DS10 groups and n=5 per experiment, in two independent sets of experiments in corneal scar and control groups) were excised, pooled, and incubated in 10ml of 5mgml−1 Dispase II (Roche Molecular Biochemicals, Indianapolis, IN) in a shaker at 37 ° C for 1 h, followed by neutralization with Hank ’s Buffered Salt Solution (Invitrogen-Gibco, Grand Island, NY) supplemented with 3% fetal bovine serum (Hyclone, Logan, UT). The bulbar and tarsal conjunctivae were scraped with cytology brushes under a dissecting microscope. Respective superficial CLNs were surgically excised, smashed in between two sterile frosted glass slides, and made into a single-cell suspension. Cell populations were individually collected, centrifuged at 2000r.p.m.×5min, filtered, and resuspended. Cells collected by this technique were used either for flow cytometry (desiccating stress experiment) or for ELISPOT (desiccating stress and corneal ulcer experiment).
De Paiva C., Chotikavanich S., Pangelinan S., Pitcher J I.I.I., Fang B., Zheng X., Ma P., Farley W., Siemasko K., Niederkorn J., Stern M., Li D.Q, & Pflugfelder S. (2009). IL-17 disrupts corneal barrier following desiccating stress. Mucosal immunology, 2(3), 243-253.
Publication 2009
Calnexin Cells Conjunctiva Corneal Ulcer Cytological Techniques dispase II Enzyme-Linked Immunospot Assay Eye Fetal Bovine Serum Flow Cytometry Medulla Oblongata Microscopy Mus Operative Surgical Procedures Population Group Sodium Chloride Sterility, Reproductive
2
Histological and Immunological Analysis of Placental Samples
Cited 17 times
Samples were fixed, paraffin embedded, sectioned, and stained with hematoxylin/eosin for histological evaluation as described [57 (link)]. Tissue sections were subject to immunological staining with avidin:biotinylated enzyme complex as described [18 (link),58 (link)]. Proteins were extracted from TS cells using M-PER reagent (PIERCE) with the addition of protease inhibitor cocktail (Sigma-Aldrich), 1 mM sodium molybdate, 1 mM sodium vanadate, and 10 mM N-ethylmaleimide, or SDS lysis buffer (2% SDS, 10% glycerol, and 50 mM Tris, pH 6.8). Protein extracts were subject to immunoblotting as described [54 (link)]. Bound primary antibodies were detected with horseradish peroxidase-conjugated secondary antibodies (Vector Lab), followed by ECL-mediated visualization (GE HealthCare) and autoradiography. Mouse monoclonal antibodies anti-actin (Thermo Fisher; 1:1,000), anti-BrdU (Thermo Fisher; 1:300), anti-Cdx2 (BioGenex; 1:1), anti-MDM2 (Santa Cruz; 1:100), and anti-SUMO-1 (Zymed; 1:2,000); rabbit polyclonal antibodies anti-calnexin (Stressgene; 1:2,000), anti-cyclin D1 (Neomarker; 1:100), anti-Ki67 (Neomarker; 1:400), anti-laminin (Sigma-Aldrich; 1:25), anti-Myc tag (CalBioChem; 1:400), anti-Oct4 (Santa Cruz; 1:200), anti-p53 (Santa Cruz; 1:50), and anti-p450scc (Chemicon; 1:200); and goat polyclonal antibody anti-lamin B (Santa Cruz; 1:100) were used as primary antibodies. BrdU incorporation analysis was performed by intraperitoneal injection of BrdU (250 μg/g of body weight) into pregnant females for 1 h. Placentas were recovered, fixed, embedded, sectioned, and subject to immunostaining as described [18 (link),57 (link)].
Chiu S.Y., Asai N., Costantini F, & Hsu W. (2008). SUMO-Specific Protease 2 Is Essential for Modulating p53-Mdm2 in Development of Trophoblast Stem Cell Niches and Lineages. PLoS Biology, 6(12), e310.
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Publication 2008
Actins Antibodies Autoradiography Avidin Body Weight Bromodeoxyuridine Buffers Calnexin Cloning Vectors Cyclin D1 Eosin Ethylmaleimide Glycerin Goat Horseradish Peroxidase immunoglobulin B Immunoglobulins Injections, Intraperitoneal Laminin Lamins Lamin Type B MDM2 protein, human Monoclonal Antibodies Multienzyme Complexes Mus Paraffin Placenta POU5F1 protein, human Pregnant Women Protease Inhibitors Proteins Rabbits sodium molybdate(VI) Sodium Vanadate SUMO1 protein, human Tissues Tromethamine
3
Immunolabeling and Antibody Characterization
Cited 12 times
Cell culture media were from GIBCO BRL. TOPRO-3 and phalloidin-Alexa 568 (Molecular Probes, Inc.) were used to label nuclei and actin. MDC was from Sigma-Aldrich. γ-Secretase inhibitors were from Calbiochem (X or L685,458), Elan (DAPT), and AstraZeneca (Compound C).
Polyclonal anti-PS1-NTF (B19.2), -CTF (B32.1) and -TLN (B36.1) have been described previously (Annaert et al., 2001 (link)). B63.1 and B59.1 were generated using a synthetic peptide mimicking the final 16 and 18 amino acids of APP and nicastrin, respectively, coupled to KLH (Pierce Chemical Co.). Mab 9C3 against nicastrin was produced by immunizing the same peptide in balb/c mice followed by generation of a hybridoma cell line according to established procedures. We acknowledge the antibody gifts of anti-calnexin (A. Helenius, ETH Zurich, Zurich, Switzerland), anti-ergic-53 (J. Saraste, University of Bergen, Bergen, Norway) -LC3 (T. Yoshimori, National Institute of Genetics, Shizuoka-ken, Japan), -Apg12 (N. Mizushima, National Institute for Basic Biology, Okazaki, Japan), PIP2 (G. Hammond, Cancer Research Institute, London, UK), -LBPA (J. Gruenberg, University of Geneva, Geneva, Switzerland), and -APP COOH terminus (c 1/6.1; P. Mathews, Nathan Kline Institute, Orangeburg, NY). Mabs to Lamp-2 (Abl-93) were obtained from Developmental Studies Hybridoma Bank (Iowa City, Iowa); anti-synaptophysin (cl.7.2) and anti-PS1-CTF (mAb 5.2) were from R. Jahn (MPI-Göttingen, Göttingen, Germany) and B. Cordell (Scios Inc., Sunnyvale, CA). mAbs to GM130 and EEA1 were from BD Biosciences, the transferrin receptor from Zymed Laboratories, β-COP from Sigma-Aldrich, and BIP from StressGen Biotechnologies.
Esselens C., Oorschot V., Baert V., Raemaekers T., Spittaels K., Serneels L., Zheng H., Saftig P., De Strooper B., Klumperman J, & Annaert W. (2004). Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway. The Journal of Cell Biology, 166(7), 1041-1054.
Publication 2004
1,2-dilinolenoyl-3-(4-aminobutyryl)propane-1,2,3-triol 2-amino-5-phosphopentanoic acid Actins alexa 568 anti-synaptophysin Antibodies, Anti-Idiotypic Calnexin Cell Culture Techniques Cell Lines Cell Nucleus Cells Culture Media Gifts Hybridomas inhibitors LAMP2 protein, human Malignant Neoplasms Mice, Inbred BALB C Molecular Probes Monoclonal Antibodies Peptides Phalloidine Secretase Transferrin Receptor
4
Chondrocyte Isolation and Gene Expression Analysis
Cited 10 times
For qRT-PCR, the rib cages from 5-day-old mice (wild type (wt) and mutant (m/m)) were dissected and treated with collagenase (type 1A, 2 mg/ml) for 1 h at 37°C in Dulbecco’s modified Eagle’s medium (DMEM). The costal cartilage was dissected from individual ribs, and the perichondrium layer was removed. The cartilage was digested a second time with collagenase for 3 h to remove the collagen matrix and release the chondrocytes. The chondrocytes were passed through a cell strainer (70 μm) and washed with DMEM containing 10% FBS and following centrifugation washed again with PBS. The cell pellet was resuspended in 500 μl TriZol (Invitrogen), and total RNA was isolated according to the manufacturer’s instructions. First-strand cDNA was synthesised using random hexamer primers (Superscript III, Invitrogen), and qPCR was performed using the SYBR® green PCR protocol. Primer sequences were: BiP: 5′-ggcaccttcgatgtgtctcttc-3′ and rev: 5′-tccatgacccgctgatcaa-3′; Grp94: 5′-taagctgtatgtacgccgcgt-3′ and rev: 5′-ggagatcatcggaatccacaac-3′; Calnexin: 5′-tga ttt cct ctc cct ccc ctt-3′ and rev: 5′-cac tgg aac ctg ttg atg gtg a-3′; Calreticulin: 5′-gct acg tga agc tgt ttc cga-3′ and rev: 5′-aca tga acc ttc ttg gtg cca g-3’; Erp72: 5′-agt atg agc cca ggt tcc acg t-3′ and rev: 5′-aga agt ctt acg atg gcc cac c-3′. Each experiment included ‘no template’ controls, was run in duplicate and had an 18S RNA control. Each independent experiment was repeated three times, and the results were analysed by independent-samples t test.
For Western blot analysis, chondrocytes were isolated as above, but aliquots of 2 × 105 chondrocytes were prepared and resuspended in 5× sodium dodecyl sulphate (SDS) loading buffer containing DTT. These protein aliquots were separated by 4–12% SDS-polyacrylamide gel electrophoresis (PAGE; Invitrogen) then transferred to nitrocellulose membranes for Western blot analysis. Ponceau staining was used to confirm equal loading of total protein isolates.
Antibodies to key chaperones associated with the unfolded protein response were used at a dilution of either 1:500 (BiP, Grp94, Erp72 and PDI; all from Santa Cruz) or 1:100 (ATF-6 from Imgenex and Bcl-2 from Abcam).
Nundlall S., Rajpar M.H., Bell P.A., Clowes C., Zeeff L.A., Gardner B., Thornton D.J., Boot-Handford R.P, & Briggs M.D. (2010). An unfolded protein response is the initial cellular response to the expression of mutant matrilin-3 in a mouse model of multiple epiphyseal dysplasia. Cell Stress & Chaperones, 15(6), 835-849.
Publication 2010
Antibodies BCL2 protein, human Buffers Calnexin Calreticulin Cartilage Cells Centrifugation Chondrocyte Collagen Collagenase Costal Cartilage DNA, Complementary Eagle endoplasmic reticulum glycoprotein p72 GRP94 Molecular Chaperones Mus Nitrocellulose Oligonucleotide Primers Proteins Rib Cage Ribs RNA, Ribosomal, 18S SDS-PAGE Sulfate, Sodium Dodecyl SYBR Green I Technique, Dilution Tissue, Membrane trizol Unfolded Protein Response Western Blot
5
Immunostaining of T. gondii Infection
Cited 8 times
Serological reagents used were: Anti-IIGP1 165 rabbit antiserum [35 (link)], anti-IIGP1 10E7, and 10D7 mouse monoclonal antibodies (mAb), anti-IGTP I68120 mAb (BD Transduction Laboratories, Lexington, Kentucky, United States), anti-TGTP1 A20 goat antiserum (Santa Cruz Biotechnology, Santa Cruz, California, United States), anti-LRG-47 A19 goat antiserum (Santa Cruz), anti-GTPI H53 rabbit antiserum raised against the N-terminal peptide MEEAVESPEVKEFEY, anti-IRG-47 2078 rabbit antiserum raised against the peptides CKTPYQHPKYPKVIF, and CDAKHLLRKIETVNVA, anti-T. gondii rabbit antiserum (BioGenex, San Ramon, California, United States), anti-LAMP1 1D4B rat mAb (University of Iowa, Iowa City, Iowa, United States), anti-GRA7 5–241–178 mouse mAb (gift from R. Ziemann, Abbott Laboratories, Abbot Park, Illinois, United States) [41 (link)], anti-ROP2/3/4 T24A7 mouse mAb (gift of J. Dubremetz, Montpellier, France) [59 (link)], anti-ctag1 2600 rabbit antiserum raised against the peptide CLKLGRLERPHRD, anti-ERP60 rabbit antiserum (gift from T. Wileman, BBSRC, Pirbright, United Kingdom), SPA-265 anti-calnexin rabbit antiserum (Stressgene), anti-PDI mAb (BD Transduction Laboratory), anti-Gm130 mAB (BD Transduction Laboratory), goat anti-mouse Alexa 546/488, goat anti-rabbit Alexa 546/488, donkey anti-goat Alexa 546/488, donkey anti-mouse Alexa 488, donkey anti-rabbit Alexa 488, donkey anti-rat Alexa 488, goat anti-rabbit Alexa 680 (Molecular Probes, Eugene, Oregon, United States).
Martens S., Parvanova I., Zerrahn J., Griffiths G., Schell G., Reichmann G, & Howard J.C. (2005). Disruption of Toxoplasma gondii Parasitophorous Vacuoles by the Mouse p47-Resistance GTPases. PLoS Pathogens, 1(3), e24.
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Publication 2005
Anti-Antibodies Calnexin Calreticulin Equus asinus Goat Immune Sera lysosomal-associated membrane protein 1, human Mice, House Molecular Probes Peptides Rabbits Thomsen-Friedenreich antibodies

Most recents protocols related to «Calnexin»

1
Quantitative ER-Mitochondria Interaction Assay
Mouse monoclonal anti ACTIN, Sigma-Aldrich, A5441; Mouse monoclonal anti c-myc, Sigma-Aldrich, M4439; Rabbit polyclonal anti Calnexin, Enzo, ADI-SPA-865-F; Mouse monoclonal anti CYTC, BD Bioscience, 556433; Rabbit DyLight 680, Thermo Fisher Scientific, 35569; Mouse DyLight 680 Thermo Fisher Scientific, 35519; Mouse DyLight 800 Thermo Fisher Scientific, 35521; Rabbit DyLight 800 Thermo Fisher Scientific, 35571; Mouse monoclonal anti eIF2α, Cell Signaling, 2103S; Rabbit polyclonal anti-E-Syt1, Sigma-Aldrich, HPA016858; Rabbit polyclonal anti-GFP, Cell Signaling, 2555S; Mouse monoclonal anti-GFP,Life technologies, A11122; HRP Mouse Bioké, Cell Signaling, 7076; HRP Rabbit Bioké, Cell Signaling, 7074; Mouse monoclonal anti IP3R3, BD Bioscience, 610312; Rabbit polyclonal anti-PERK, Cell signaling, 3192S; Rabbit polyclonal anti PERK, Cell signaling, 5683S; Rabbit monoclonal anti Phospho-eIF2α (Ser51), Cell signaling, 3597S; Rabbit polyclonal anti PDI Genetex, GTX30716; Mouse monoclonal anti PSD, Santa Cruz, sc-390070; Rabbit polyclonal anti, PSS1 (B-5), Santa Cruz, sc-515376; Rabbit polyclonal anti PSS2, Sigma-Aldrich, SAB1303408; Rabbit polyclonal VDAC1, Cell Signaling, 4866S; Rabbit polyclonal VDAC1, Abcam, ab15895; Veriblot antibody Abcam, ab131366.
The reagents used were: Antimycin A, Sigma-Aldrich, A8674; Calcium Chloride dihydrate, Sigma-Aldrich, C3881; CHAPS hydrate, Sigma-Aldrich, C3023; Conjugated GFP antibody beads, Laboratory of Chris Ulens; D-Galactose, Sigma-Aldrich, G0750; D-glucose, Sigma-Aldrich, G7021-1KG; DAPI, Thermo Fisher Scientific, 62248; Dulbecco’s Modified Eagle’s Medium - high glucose, Sigma-Aldrich, D0422; EGTA, AppliChem, A0878; FCCP, Sigma-Aldrich, C2920; Gibco DMEM/F-12, Thermo Fisher Scientific, 11320074; Glucose, Agilent Seahorse, 103577; Glutamine, Sigma-Aldrich, G7513; Glutamine, Agilent Seahorse, 103579; GSK PERK Inhibitor, Toronto Research Company, G797800; Hygromycin B, Invivogen, ant-hg-1; Lipofectamine 2000 Transfection Reagent, Thermo Fisher Scientific, 11668019; MitoTracker FarRed, Thermo Fisher Scientific, M22426; NBD-PS, Avanti Polar Lipids, 810194C; SE Cell Line 4D-Nucleofector X Kit L, V4XC-1024; Oligomycin, Sigma-Aldrich, 75351; Penicillin and streptomycin, Sigma-Aldrich, P0781; Percoll, Sigma-Aldrich, P1644; Pierce ECL Western Blotting Substrate, Thermo Fisher Scientific, 32106X4; Pierce Protein A/G Magnetic Beads, Thermo Fisher Scientific, 88802; Pierce Protease Inhibitor Tablets, EDTA-free, Thermo Fisher Scientific, 88266; Potassium Chloride, Janssen Chimica, 7447407; Protease inhibitor, Thermo Fisher Scientific, A32953; Puromycin, Thermo Fisher Scientific, A11138-03; Protein A/G PLUS-Agarose, Santa Cruz, sc-2003; XF DMEM pH7 7.4, Agilent Seahorse, 103575; Sodium Chloride, Sigma-Aldrich, A0431796; Sodium Pyruvate Solution, Agilent Seahorse, 103578; Sucrose, Acros, A0333146; Thapsigargin, Enzo Life Sciences, BML-PE180; TransIT-X2 Dynamic Delivery System, Mirus Bio, MIR 6000; Tris base, Sigma-Aldrich, 77861; Triton, Sigma-Aldrich, T9234; Tween, Sigma Aldrich, P4780.
Sassano M.L., van Vliet A.R., Vervoort E., Van Eygen S., Van den Haute C., Pavie B., Roels J., Swinnen J.V., Spinazzi M., Moens L., Casteels K., Meyts I., Pinton P., Marchi S., Rochin L., Giordano F., Felipe-Abrio B, & Agostinis P. (2023). PERK recruits E-Syt1 at ER–mitochondria contacts for mitochondrial lipid transport and respiration. The Journal of Cell Biology, 222(3), e202206008.
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Publication 2023
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Actins Antimycin A Calcium Chloride Dihydrate Calnexin Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone DAPI Eagle Edetic Acid Egtazic Acid G-substrate Galactose Glucose Glutamine Hygromycin B Immunoglobulins L Cells Lipids lipofectamine 2000 Mus N-(7-nitro-2,1,3-benzoxadiazol-4-yl)phosphatidylserine Obstetric Delivery Oligomycins Peeling Skin Syndrome Peeling skin syndrome, acral type Penicillins Percoll Potassium Chloride Protease Inhibitors Puromycin Pyruvate Rabbits Seahorses Sepharose Sodium Sodium Chloride Staphylococcal Protein A Streptomycin Sucrose SYT1 protein, human Thapsigargin Transfection Tromethamine Tweens VDAC1 protein, human
2
Extracellular Vesicle Protein Characterization
Extracellular vesicle containing fractions were lysed in 1X RIPA. Protein concentrations were determined by microBCA protein assay (Thermo Fisher, 23235). Equivalent protein amounts (extracellular vesicles and proteins) were separated on 4–15% stain-free precast SDS-PAGE gradient gels (Bio-Rad 5678083) under nonreducing conditions and transferred onto PVDF membranes (Sigma Aldrich IPVH00005). After 1 h blocking (5% nonfat milk, Bio-Rad 170–6404) at room temperature (RT), membranes were incubated with antibodies against CD63 (1 : 1000, BD Biosciences 556019), CD81 (1 : 500, Santa Cruz Biotechnology sc23962), calnexin (1 : 2000, Abcam ab22595), GM130 (1 : 1000, Abcam, ab76154), albumin (1 : 1000, Abcam ab28405), AGO2 (1 : 500, Sigma-Aldrich SAB4200085), ApoB100 (1 : 1000, Academy Bio-Medical 20A-G1b), ApoA1 (1 : 1000, Academy Bio-Medical 11A-G2b), and ApoC1 (1 : 1000, Academy Bio-Medical 31A-G1b) overnight at 4°C. Membranes were washed three times for 8 min in PBST with shaking, then incubated with HRP-conjugated secondary mouse antirabbit IgG or mouse IgG kappa binding protein antibodies (1 : 10 000, Santa Cruz Biotechnology sc-2357 and sc-516102) at RT for 1 h. After a PBST wash, membranes were incubated with SuperSignal West Pico PLUS chemiluminescent substrate (Thermo Fisher 34580) and visualized by iBright (Thermo Fisher, Waltham, Massachusetts, USA).
Huang Y., Liao Z., Dang P., Queen S., Abreu C.M., Gololobova O., Zheng L, & Witwer K.W. (2023). Longitudinal characterization of circulating extracellular vesicles and small RNA during simian immunodeficiency virus infection and antiretroviral therapy. AIDS (London, England), 37(5), 733-744.
Publication 2023
Albumins Antibodies APOA1 protein, human Apolipoprotein B-100 apolipoprotein C-I, human Binding Proteins Biological Assay Calnexin EIF2C2 protein, human Extracellular Vesicles Gels IGG-horseradish peroxidase Mice, House Milk, Cow's polyvinylidene fluoride Proteins Radioimmunoprecipitation Assay SDS-PAGE Stains Tissue, Membrane
3
Quantifying Exosome Markers by Western Blot
For western blot (WB) analysis, equal amounts of EV pellet (30-50 ug, measured by Pierce BCA protein assay kit, CAT 23227) obtained from similar PPP volumes (250 ul) were combined with a 2xlysis buffer (RayBiotech) supplemented with 1% proteinase inhibitor and 1% phosphatase inhibitors (Sigma) containing β-mercaptoethanol (1:20, Biorad). Samples were loaded and separated on 4%–20% Mini-PROTEAN TGX Precast Protein Gels (Bio-Rad) and then transferred to Trans-Blot Turbo Mini 0.2 μm Nitrocellulose Transfer Packs (Bio-Rad). The membranes were stained with Ponceau S solution (P7170, sigma) to ensure that proteins transferred from the gel to the membrane (Supplementary Figure S3), were washed and immunoblotted with the appropriate antibodies against exosome markers. Mouse monoclonal anti human-CD63 (ab59479) and CD81 (ab79559) were both used in 1:1000 dilutions. Anti-rabbit, anti-human placental lactogen hormone (hPL) (ab137099; 1;25,000 dilution) and Calnexin (ab10286, 1;10,000 dilution) endoplasmic reticulum (ER) protein, not expected to be enriched in EVs, serve as negative control (all from Abcam, USA). Secondary antibodies (anti-mouse 115-035-146 and anti-rabbit 111-035-144, both in 1:5000 dilution) were purchased from Jackson ImmunoResearch (PA, USA). The blot was imaged and quantified by myECL™ Imager and analyzed by My Image Analysis Software (both from Thermo Fisher Scientific, Waltham, MA USA).
Aharon A., Rebibo-Sabbah A., Ahmad R.S., Dangot A., Bar-Lev T.H., Brenner B., Cohen A.H., David C.B., Weiner Z, & Solt I. (2023). Associations of maternal and placental extracellular vesicle miRNA with preeclampsia. Frontiers in Cell and Developmental Biology, 11, 1080419.
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Publication 2023
2-Mercaptoethanol Antibodies Biological Assay Buffers Calnexin Endoplasmic Reticulum Exosomes Homo sapiens Hormones inhibitors Mus Nitrocellulose Phosphoric Monoester Hydrolases Placental Lactogen ponceau S Protease Inhibitors Proteins Rabbits Technique, Dilution Tissue, Membrane Western Blot
4
Extracellular Vesicle Protein Profiling
Towbin transfer buffer was used to transfer 10 µg of EV protein separated by SDS-PAGE to a PVDF membrane (Merck Millipore, Germany) at 110 V for 70 min. followed by blockade with 5% skimmed milk powder (BD, USA) for 2.5 h. The membranes were incubated with rabbit polyclonal antibodies anti-CD63 (BBI Life Sciences, D160973; 1:1500, China), anti-CD9 (BBI Life Sciences, D164336; 1:1500, China), anti-TSG101 (ZEN BIO, 381,538; 1:1500, China), anti-calnexin (Abcam, ab75801; 1:1500, UK), and monoclonal antibodies anti-MUC4 (Abcam, ab150381; 1:1500, UK), anti-ACP5 (Abcam, ab191406; 1:1500, UK), mouse monoclonal antibodies anti-MEP1B (R&D Systems, MAB28951; 1:1500, USA) overnight at 4 ℃ followed by incubation with secondary antibody for 1.5 h at room temperature. An Ecl Kit (CWBIO, China) was used to visualize immunoreactive bands and was exposed to EC3 Imaging System (UVP).
Hong L., Zang X., Hu Q., He Y., Xu Z., Xie Y., Gu T., Yang H., Yang J., Shi J., Zheng E., Huang S., Xu Z., Liu D., Cai G., Li Z, & Wu Z. (2023). Uterine luminal-derived extracellular vesicles: potential nanomaterials to improve embryo implantation. Journal of Nanobiotechnology, 21, 79.
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Publication 2023
ACP5 protein, human Anti-Antibodies Buffers Calnexin Immunoglobulins Milk, Cow's Monoclonal Antibodies MUC4 protein, human Mus polyvinylidene fluoride Powder Proteins Rabbits SDS-PAGE Tissue, Membrane TSG101 protein, human
5
Multimodal Analysis of Neuronal Markers
Mice were sacrificed and transcardially perfused with 4% paraformaldehyde (PFA) in cold phosphate-buffered saline (PBS). Mouse brains, superior cervical ganglions, and adrenal glands were collected, post-fixed in 4% PFA/PBS solution overnight, submerged in 30% sucrose in PBS for at least 72 h, and sectioned at 40 μm thickness using CM1950 cryostat (Leica)22 (link). Frozen sections were stained with antibodies specific to p150Glued (amino acid 3–202 at the N-terminus of p150Glued, BD Biosciences, #610474, 1:200, recognizing p150Glued but not p135+), p150Glued & p135+ (amino acid 1266–1278 at the C-terminus of p150Glued, Abcam, #ab11806, 1:500, recognizing both p150Glued and p135+), tyrosine hydroxylase (TH, Pel-Freez, #P40101-150, 1:2500; ImmunoStar, #22941, 1:500; Synaptic Systems, #213104, 1:500), dopamine transporter (DAT, Millipore, #MAB369, 1:500), vesicular monoamine transporter 2 (VMAT2, Synaptic Systems, #138302, 1:1000), glial fibrillary acidic protein (GFAP, Abcam, #ab7260, 1:1000), TAR DNA-binding protein 43 (TDP-43, Proteintech, #10782-2-AP, 1:500), α-synuclein (Santa Cruz, #sc-7011-R, 1:500; Santa Cruz, #sc-69977, 1:500), phosphorylated α-synuclein (Ser129) [p-α-synuclein (Ser129), Abcam, #ab51253, 1:500], neuronal nuclei (NeuN, Millipore, #ABN91, 1:500), synaptophysin (Millipore, #AB9272, 1:500), binding immunoglobulin protein (BiP, also referred to as GRP78, Abcam, #ab21685, 1:500), reticulon 3 (RTN3, Proteintech, #12055-2-AP, 1:500), 63 kDa cytoskeleton-linking membrane protein (CLIMP63, Proteintech, #16686-1-AP, 1:500), calnexin (Abcam, #ab22595, 1:500), protein disulfide isomerase (PDI, Proteintech, #11245-1-AP, 1:500), receptor binding cancer antigen expressed on SiSo cells (RCAS1, Cell Signaling Technology, #12290, 1:500), early endosome antigen 1 (EEA1, Cell Signaling Technology, #3288, 1:500), sequestosome 1 (SQSTM1, MBL, #PM066, 1:500), cathepsin D (R&D Systems, #AF1029, 1:500), ER-Golgi intermediate compartment 53 kDa protein (ERGIC53, Sigma-Aldrich, #E1031, 1:500), 130 kDa cis-Golgi matrix protein (GM130, BD Biosciences, #610822, 1:500), phosphorylated eukaryotic translation initiation factor 2α (Ser51) [p-eIF2α (Ser51), Abcam, #ab32157, 1:500], and phosphorylated inositol-requiring enzyme 1α (Ser724) [p-IRE1α (Ser724), Abcam, #ab48187, 1:500] as suggested by manufacturers. Alexa Fluor 488-, 546-, or 647-conjugated secondary antibody (Invitrogen, 1:500) was used to visualize the staining. Fluorescent images were captured using LSM 880 laser-scanning confocal microscope with Zen software (Zeiss) in conventional or Airyscan mode. As a high-resolution imaging modality, the Airyscan technology is reported to improve resolution 2-fold and signal-to-noise ratio 8-fold relative to the conventional confocal microscopy61 (link). The paired images in all the figures were collected at the same gain and offset settings. Post-collection processing was applied uniformly to all paired images. The images were presented as a single optic layer after acquisition in z-series stack scans at 1.0 μm intervals from individual fields or displayed as maximum-intensity projection or three-dimensional (3D) reconstruction to represent confocal stacks.
Yu J., Yang X., Zheng J., Sgobio C., Sun L, & Cai H. (2023). Deficiency of Perry syndrome-associated p150Glued in midbrain dopaminergic neurons leads to progressive neurodegeneration and endoplasmic reticulum abnormalities. NPJ Parkinson's Disease, 9, 35.
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Publication 2023
Adrenal Glands alexa fluor 488 alpha-Synuclein Amino Acids Antibodies Antigens Binding Proteins Brain Calnexin Cathepsin D Cell Nucleus Cells Cold Temperature Cytoskeleton Dopamine Transporter dynactin subunit 1, human early endosome antigen 1 Enzymes ERN1 protein, human Eukaryotic Initiation Factors Eye Frozen Sections Ganglia, Superior Cervical Glial Fibrillary Acidic Protein Glucose Regulated Protein 78 kDa Golgi Apparatus Golgin subfamily A member 2 Immunoglobulins Inositol Malignant Neoplasms Membrane Proteins Microscopy, Confocal Mus Neurons paraform Phosphates Protein Disulfide-Isomerases Proteins protein TDP-43, human Radionuclide Imaging Reconstructive Surgical Procedures Saline Solution SQSTM1 protein, human Sucrose Synaptophysin Tyrosine 3-Monooxygenase Vesicular Monoamine Transporter 2

Top products related to «Calnexin»

1
Calnexin by Abcam
Sourced in United Kingdom, United States, Germany, China
Calnexin is a chaperone protein found in the endoplasmic reticulum (ER) of eukaryotic cells. It is involved in the quality control of protein folding and assembly within the ER. Calnexin binds to and retains unfolded or misfolded glycoproteins, helping them to properly fold and assemble before they are transported out of the ER.
2
Calnexin by Cell Signaling Technology
Sourced in United States, United Kingdom
Calnexin is a chaperone protein that assists in the folding and quality control of newly synthesized glycoproteins in the endoplasmic reticulum. It binds to and retains misfolded or incompletely assembled glycoproteins, allowing them to undergo additional folding or targeting for degradation.
3
Pvdf membrane by Merck Group
Sourced in United States, Germany, China, United Kingdom, Morocco, Ireland, France, Italy, Japan, Canada, Spain, Switzerland, New Zealand, India, Hong Kong, Sao Tome and Principe, Sweden, Netherlands, Australia, Belgium, Austria
PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.
4
Ab22595 by Abcam
Sourced in United Kingdom, United States, China
Ab22595 is a monoclonal antibody that targets the Histone H3 (tri methyl K9) protein. It is designed for use in various immunoassay applications.
5
Anti calnexin by Abcam
Sourced in United States, United Kingdom
Anti-Calnexin is a protein-specific antibody that recognizes the calnexin protein. Calnexin is a membrane-bound chaperone protein that plays a role in the folding and quality control of newly synthesized glycoproteins in the endoplasmic reticulum.
6
Calnexin by Santa Cruz Biotechnology
Sourced in United States, Germany
Calnexin is a type I membrane protein that functions as a molecular chaperone in the endoplasmic reticulum (ER). It plays a key role in the quality control of newly synthesized glycoproteins, assisting in their proper folding and preventing the release of misfolded proteins. Calnexin interacts with monoglucosylated glycoproteins, retaining them in the ER until they achieve their native conformation.
7
Tsg101 by Abcam
Sourced in United States, United Kingdom, China, Japan, Germany
TSG101 is a protein involved in the endosomal-lysosomal pathway and functions in the sorting of ubiquitinated proteins into multivesicular bodies. It is a component of the ESCRT-I complex, which plays a role in the budding of vesicles from the limiting membrane of the endosome.
8
Ab125011 by Abcam
Sourced in United Kingdom, United States, China
Ab125011 is a laboratory product from Abcam. It is a recombinant protein.
9
Anti calnexin by Cell Signaling Technology
Sourced in United States, United Kingdom
Anti-calnexin is a laboratory reagent used to detect the presence of the calnexin protein in cellular samples. Calnexin is a chaperone protein involved in the folding and quality control of newly synthesized glycoproteins within the endoplasmic reticulum. The anti-calnexin antibody can be used to identify and quantify calnexin levels in various cell and tissue types.
10
β actin by Merck Group
Sourced in United States, United Kingdom, Germany, China, Canada, Japan, Macao, Italy, Sao Tome and Principe, Israel, Spain, Denmark, France, Finland, Australia, Morocco, Ireland, Czechia, Sweden, Uruguay, Switzerland, Netherlands, Senegal
β-actin is a protein that is found in all eukaryotic cells and is involved in the structure and function of the cytoskeleton. It is a key component of the actin filaments that make up the cytoskeleton and plays a critical role in cell motility, cell division, and other cellular processes.

More about "Calnexin"

Calnexin is a critical molecular chaperone protein that plays a pivotal role in the quality control of protein folding and assembly within the endoplasmic reticulum (ER).
This ER-resident protein binds to newly synthesized glycoproteins, preventing their premature exit from the ER and promoting proper folding and maturation.
Calnexin also interacts with other key ER proteins, such as calreticulin and ERp57, to facilitate the formation of disulfide bonds and the proper assembly of multimeric protein complexes.
This chaperone activity is essential for maintaining cellular homeostasis and preventing protein misfolding diseases.
Researchers can leverage the powerful AI-driven tools provided by PubCompare.ai to optimize their Calnexin-related studies.
These tools can help identify the best research protocols from literature, preprints, and patents, streamlining the workflow and accelerating discovery.
By utilizing PubCompare.ai's platform, scientists can easily locate the most effective products and protocols for their Calnexin research, including PVDF membranes, anti-Calnexin antibodies (e.g., Ab22595, Ab125011), and even the use of the internal control protein β-actin.
Calnexin is closely associated with the protein TSG101, which plays a critical role in the endosomal sorting complex required for transport (ESCRT) pathway.
The interplay between Calnexin and TSG101 is an area of ongoing research, as it may provide insights into the cellular mechanisms involved in protein quality control and trafficking.
PubCompare.ai's AI-powered tools empower researchers to optimize their Calnexin studies, streamline their workflows, and accelerate the pace of discovery.
Experiance the power of AI-driven protocol optimization today and unlock new insights in your Calnexin-related research.