The largest database of trusted experimental protocols
> Chemicals & Drugs > Amino Acid > Insulin Receptor

Insulin Receptor

The insulin receptor is a transmembrane protein that binds insulin and mediates its biological effects.
It is a tyrosine kinase receptor that plays a central role in glucose and lipid metabolism, cell growth and differentiation.
Dysfunction of the insulin receptor is implicated in insulin resistance and type 2 diabetes.
Reserching the insulin receptor can provide insights into the pathogenesis and tratment of metabolic disorders.
PubCompare.ai optimizes this research by helping users locate the best protocols and products from literature, pre-prints, and patents.
Thier AI-driven comparisons enhance reproducibility and accuary, ensuring your insulin receptor experiments yield reliable results.

Most cited protocols related to «Insulin Receptor»

These assays were carried out as previously described (24 ) with minor modifications. Purified GST-fused proteins (15-35 μg) or GST alone (30-45 μg) were immobilized on glutathione S-sepharose beads (GE healthcare) and incubated for 4 hours at 4°C in binding buffer (50 mM Tris-HCl, pH 7.4, 100 mM NaCl, 0.4% (v:v) NP-40, 10 mM MgCl2, 5 mM EDTA, 2 mM DTT, and 2 mM Sodium Orthovanadate) containing sham-treated or in vitro phosphorylated His-GIV CT (aa 1660-1870). After a 4 hour incubation at 4°C, the beads were washed (4.3 mM Na2HPO4, 1.4 mM KH2PO4, pH 7.4, 137 mM NaCl, 2.7 mM KCl, 0.1% (v:v) Tween 20, 10 mM MgCl2, 5 mM EDTA, 2 mM DTT, and 30 and 2 mM Sodium Orthovanadate), and bound proteins eluted in sample buffer for SDS-PAGE. When GST-Gαi3 was used in these assays, both binding and wash buffers were supplemented with 30 μM GDP. Where indicated, His-GIV CT was phosphorylated in vitro using recombinant EGFR (Invitrogen) prior to its use in pulldown assays.
For immunoprecipitations, cell lysates (~1-2 mg protein) were incubated for 4 hours at 4°C with either 2 μg anti-FLAG mAb for immunoprecipitation of GIV-FLAG, anti-GIV-CT (Girdin-T13 Ab, Santa Cruz Biotechnology) for endogenous GIV, anti-HA mAb (Covance) for immunoprecipitation of HA-tagged insulin receptor, anti-EGFR #225 mAb (65 (link)) for immunoprecipitation of endogenous EGFR, and their respective pre-immune control IgGs where indicated. Protein A (for GIV-CT Ab) or G (for all other mAbs) agarose beads (GE healthcare) were added and incubated at 4°C for an additional 60 min. Beads were washed then either resuspended and boiled in SDS sample buffer. Buffers were supplemented with 1 mM sodium orthovanadate for all steps of the assay.
Publication 2011
Biological Assay Buffers Cells Edetic Acid EGFR protein, human Glutathione Immunoprecipitation Insulin Receptor Magnesium Chloride Monoclonal Antibodies Nonidet P-40 Orthovanadate Proteins SDS-PAGE Sepharose Sodium Sodium Chloride Staphylococcal Protein A Tromethamine Tween 20
Mvt1 cells or tumor tissues were lysed in chilled lysis buffer (pH 7.4) containing 50 mM Tris, 150 mM NaCl, 1 mM EDTA, 1.25% CHAPS, 1 mM sodium orthovanadate, 10 mM sodium pyrophosphate, 8 mM B-glycerophosphate and Complete Protease Inhibitor Cocktail tablet. Protein concentration of samples was measured using the BCA protein assay kit (Thermo Scientific, Rockford, IL, USA). Protein samples were resuspended in 3× loading buffer containing DTT (Cell Signaling Technologies, Danvers, MA, USA) and denatured by boiling for five minutes at 96°C. Samples were then subjected to SDS polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to a nitrocellulose membrane. Membranes were probed with the appropriate primary antibodies: anti-phospho Akt (Ser473), Akt, c-Myc, matrix metalloprotease (MMP) -9 and β-actin (obtained from Cell Signaling Technology, Danvers, MA, USA), anti-insulin receptor (IR)-β, IGF-IR and vascular endothelial growth factor (VEGF) (obtained from Santa Cruz Biotechnology, Santa Cruz, CA, USA) before being incubated with secondary antibodies (LI-COR Biosciences, Lincoln, NE, USA) and being exposed to the LI-COR infrared detection system (LI-COR Biosciences).
Full text: Click here
Publication 2012
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Actins Antibodies Biological Assay Buffers Cells Edetic Acid Glycerophosphates Insulin Insulin-Like Growth Factor Receptor Insulin Receptor MMP9 protein, human Neoplasms Nitrocellulose Oncogenes, myc Orthovanadate Protease Inhibitors Proteins SDS-PAGE Sodium Sodium Chloride sodium pyrophosphate Tablet Tissue, Membrane Tissues Tromethamine Vascular Endothelial Growth Factors
The insulin receptor signaling assay were performed as described earlier with some modifications20 ,24 . For the activation assay, the short isoform of human IR in pCS2-MYC was used as described previously20 ,49 (link). Plasmid transfections into 293FT cells were performed with LipofectaminTM 2000 (Invitrogen). One day later, the cells were serum starved for 14 hr and treated with the indicated concentrations of insulin or S597 analogs. For IR-D707A MEFs, cells were incubated with 1 μM Tamoxifen (EMD Millipore, Cat. #508225) for 2 days, starved for 14 h, and treated with the insulin or S597 analogs.
The cells were incubated with the lysis buffer B [50 mM Hepes pH 7.4, 150 mM NaCl, 10% Glycerol, 1% Triton X-100, 1 mM EDTA, 100 mM sodium fluoride, 2 mM sodium orthovanadate, 20 mM sodium pyrophosphate, 0.5 mM dithiothreitol (DTT), 2 mM phenylmethylsulfonyl fluoride (PMSF)] supplemented with cOmplete Protease Inhibitor Cocktail (Roche), PhosSTOP (Sigma), and 25 U/ml turbo nuclease (Accelagen) on ice for 1 h. After centrifuging at 20,817×g at 4 °C for 10 min, the concentrations of cell lysate were measured using Micro BCA Protein Assay Kit (Thermo Scientific). About 50–60 μg total proteins were analyzed by SDS-PAGE and quantitative Western blotting. The following antibodies were purchased from commercial sources: Anti-IR-pY1150/1151 (WB, 1:1000; 19H6; labeled as pY IR, Cat. #3024), anti-AKT (WB, 1:1000; 40D4, Cat. #2920), anti-pS473 AKT (WB, 1:1000; D9E, Cat. #4060), anti-ERK1/2 (WB, 1:1000; L34F12, Cat. #4696), anti-pERK1/2 (WB, 1:000; 197G2, Cat. #4377), anti-IRS1-pS616 (WB, 1:1000; C15H5, Cell Signaling, Cat. #3203); anti-IRS1 (WB, 1:1000; A301-158A, Bethyl Laboratory); anti-IR (WB, 1:500, CT-3, Santa Cruz; labeled as IR for primary hepatocytes and MEFs, Cat. #sc-57342); anti-IR (WB, 1:1000; EPR23566-103; labeled as IR for Fig. S10, ab278100, Abcam); anti-Myc (WB, 1:2000; 9E10, Cat. #11667149001, Roche; labeled as IR for 293FT cells). For quantitative western blots, anti-rabbit immunoglobulin G (IgG) (H + L) (WB, 1:5000; Dylight 800 conjugates, Cat. #5151) and anti-mouse IgG (H + L) (WB, 1:5000; Dylight 680 conjugates, Cat. #5470) (Cell Signaling) were used as secondary antibodies. The membranes were scanned with the Odyssey Infrared Imaging System (Li-COR, Lincoln, NE).
Full text: Click here
Publication 2022
A-301 Antibodies Antibodies, Anti-Idiotypic Biological Assay Buffers Cells Dithiothreitol Edetic Acid Glycerin Hepatocyte HEPES Homo sapiens Immunoglobulin G Insulin Insulin Receptor IRS1 protein, human Mitogen-Activated Protein Kinase 3 Mus Orthovanadate Phenylmethylsulfonyl Fluoride Plasmids Protease Inhibitors Protein Isoforms Proteins Rabbits SDS-PAGE Serum Sodium Sodium Chloride Sodium Fluoride sodium pyrophosphate Tamoxifen Tissue, Membrane Transfection Triton X-100 Western Blot
The RNA‐Bee Total‐RNA Isolation Kit (Bio‐Connect, Huissen, the Netherlands) was used for RNA extraction from snap‐frozen liver tissue (left lobe). RNA concentration was determined spectrophotometrically using Nanodrop 1000 (Isogen Life Science, De Meern, Netherlands), and RNA quality was assessed using the 2100 Bioanalyzer (Agilent Technologies, Amstelveen, Netherlands). RNA was then used to generate strand‐specific messenger RNA (mRNA)–seq libraries for next generation sequencing at GenomeScan B.V. (Leiden, the Netherlands). Libraries were multiplexed, clustered, and sequenced on an Illumina NextSeq 500 with a single‐read 75‐cycles sequencing protocol, 13 million reads per sample, and indexing. Differentially expressed genes were determined for HFD versus chow at t = 24 weeks, HFD versus chow at t = 34 weeks, and HFD+OCA versus HFD at t = 34 weeks, using the DESeq‐method34 with statistical cut‐off false discovery rate < 0.05.
To evaluate the representation of human pathophysiological pathways in HFD‐fed Ldlr‐/‐.Leiden mice, murine hepatic gene expression profiles were compared with published data on hepatic gene expression profiles in human NASH: a disease signature for NASH versus control10 that was downloaded from the Gene Expression Omnibus (GEO) with accession number GSE48452 and a gene profile that differentiates severe “progressive” NASH patients (fibrosis stage 3 or 4) from mild NASH patients (fibrosis stage 0 or 1)9 (GEO accession number GSE31803).
The effects of OCA on hepatic gene expression were analyzed by gene enrichment analysis across pathways and biological processes using Ingenuity Pathway Analysis (IPA) suite (www.ingenuity.com, accessed 2016) as described previously.19, 35 The upstream regulator analysis tool of IPA was used to assess the activity of transcription factors as well as other upstream regulators (e.g., receptors, enzymes, metabolites) essentially as reported.36 Gene expression data were used to predict activation or deactivation of upstream regulators (e.g., of TGF‐β or the insulin receptor). A negative z‐score of less than −2 indicates significantly reduced transcriptional activity based on the direction of gene expression changes of target genes. A positive z‐score of greater than 2 indicates significant activation of the upstream regulator. In addition, the effects of OCA on the gene expression profiles for human NASH9, 10 were investigated.
Publication 2018
Biological Processes Enzymes Fibrosis Freezing Gene Expression Genes Homo sapiens Insulin Receptor isolation LDLR protein, human Liver Mus Nonalcoholic Steatohepatitis Patients RNA, Messenger Tissues Transcription, Genetic Transcription Factor Transforming Growth Factor beta
Insulin receptor-A phosphorylation was detected essentially as described by Ref. (6 (link)). Briefly, RIR-A cells (5 × 104 cells/well) were plated in a 96-well flat-bottom plate and grown overnight at 37°C, 5% CO2. Cells were starved in serum-free medium (SFM) for 4 h before treatment with insulin, IGF-II, qIGF-I, or S597 in 100 μl of Dulbecco’s minimal essential medium with 1% bovine serum albumin for 10 min or in a time course (0, 2, 5, 8, 12, 20, 30 min) at 37°C, 5% CO2. Cells were lysed with ice-cold lysis buffer containing 2 mM Na3VO4 and 100 mM NaF, and receptors were captured onto white Greiner Lumitrac 600 96-well plates pre-coated with anti-IR antibody 83-7 (500 ng/well) (34 (link)) and blocked with 20 mM Tris, 150 mM NaCl, and 0.1% (v/v) Tween 20 (TBST)/0.5% bovine serum albumin. Following overnight incubation at 4°C, the plates were washed three times with TBST. Phosphorylated receptor was detected by incubation with EU-pY20 (76 ng/well) at room temperature for 2 h. Wells were washed four times with TBST, and time-resolved fluorescence was detected as described above. Assays were performed in triplicate at least three times.
Full text: Click here
Publication 2015
Antibodies, Anti-Idiotypic Biological Assay Buffers Cells Cold Temperature Fluorescence Insulin insulin-like growth factor 2, human Insulin Receptor Phosphorylation Serum Serum Albumin, Bovine Sodium Chloride Tromethamine Tween 20

Most recents protocols related to «Insulin Receptor»

Cell lysates and epididymal fat lysates were prepared with lysis buffer containing protease inhibitor. The protein concentrations were quantified via a BCA assay kit, and 20 μg of protein was separated by SDS-PAGE gels and then transferred onto the PVDF membrane. The membranes were then blocked using 3% nonfat dry milk in Tris-buffered saline-Tween 20 (TBS-T) for 1 h and then probed overnight with the primary antibodies (1:1000) at 4 °C. In this experiment, we used primary antibodies including: p-IGF-1 receptor (#4568, Cell Signaling Technology), Phospho-Insulin Receptor β (Tyr1345) (#3026, Cell Signaling Technology), p-Akt (#9271, Cell Signaling Technology), Akt (#4691, Cell Signaling Technology), p-ERK1/2 (#4377, Cell Signaling Technology), ERK1/2 (#4695, Cell Signaling Technology), PPAR-γ (#2443, Cell Signaling Technology), C/EBP-α (#2295, Cell Signaling Technology) and β-actin (#4967, Cell Signaling Technology). The membranes were washed and incubated with anti-Rabbit IgG, HRP-linked Secondary Antibody (#7074, Cell Signaling Technology) for 2 h at RT, and specific protein bands were detected with Amersham™ ECL™ Prime Western Blotting Detection Reagent (RPN2236, GE Healthcare) and visualized on Image Quant LAS 500 or 4000 (GE healthcare, UK). Band intensities were quantified and calculated using Image J software (1.52a version, National Institutes of Health, Bethesda, MD, USA).
Full text: Click here
Publication 2023
Actins anti-IgG Antibodies Biological Assay Buffers Cells Epididymis Gels Immunoglobulins Insulin-Like-Growth Factor I Receptor Insulin Receptor Milk, Cow's Mitogen-Activated Protein Kinase 3 polyvinylidene fluoride PPAR gamma Protease Inhibitors Proteins Rabbits Saline Solution SDS-PAGE Tissue, Membrane Tween 20
Liver and isolated hepatocytes were homogenized in RIPA buffer containing a protease inhibitor cocktail (Thermo Scientific, Waltham, MA, USA) and incubated on ice for 10 min. After centrifuging for 15 min at a maximum speed, the protein concentration of the supernatant was determined using the PierceTM BCA Protein Assay Kit (Thermo Fisher Scientific). Twenty micrograms of liver protein or 5 μg of hepatocyte protein were used for immunoblotting with primary antibodies for fatty acid translocase (FAT/CD36) (AF2519, R&D Systems, Minneapolis, MN, USA), fatty acid binding protein 1 (FABP1) (ab7366, Abcam), fatty acid synthase (FASN) (3180, Cell Signaling Technology, Beverly, MA, USA), acetyl-CoA carboxylase (ACC) (3676, Cell Signaling Technology), insulin receptor (IR) (3025, Cell Signaling Technology), PY99 (p-Tyr, 7020, Santa Cruz Biotechnology, Dallas, TX, USA), insulin receptor substrate-1 (IRS-1) (611394, BD Bioscience, Franklin Lakes, NJ, USA), phosphatidylinositol-3-kinase (PI3-K) (610045, BD Bioscience), sterol regulatory element-binding protein-1c (SREBP-1c) (NB600-582, NB100-2215, Novus Biologicals, Centennial, CO, USA), protein kinase B (Akt) (9272, Cell Signaling Technology), phospho-Akt (Ser473, 9271, Cell Signaling Technology), mammalian target of rapamycin (mTOR) (2983, Cell Signaling Technology), phospho-mTOR (Ser2448, 2971, Cell Signaling Technology), AMP-activated protein kinase α (AMPKα) (2603, Cell Signaling Technology), phospho-AMPKα (Thr172, 2535, Cell Signaling Technology), or β-Actin (A5441, Sigma-Aldrich, St. Louis, MO, USA), at dilutions suggested by the manufacturers. Densitometric analysis was performed by ImageQuantTM LAS 4000 (GE Healthcare Bioscience, Piscataway, NJ, USA), and quantification values were normalized against β-Actin.
Full text: Click here
Publication 2023
1-Phosphatidylinositol 3-Kinase Acetyl-CoA Carboxylase Actins AKT1 Protein Kinase AMP-Activated Protein Kinases Antibodies Biological Assay Biological Factors Buffers Densitometry FABP1 protein, human FASN protein, human Fatty Acids FRAP1 protein, human Hepatocyte Insulin Receptor Insulin Receptor Substrate-1 Protein Liver Novus Protease Inhibitors Protein Kinases Proteins Radioimmunoprecipitation Assay Sterol Regulatory Element Binding Protein 1c Technique, Dilution
RT-qPCR was used to measure mRNA expression levels of leptin (Lep), leptin receptor (Lepr), insulin receptor (Insr), peroxisome proliferator-activated receptor gamma (Pparγ), patatin-like phospholipase domain containing 2 (Pnpla2) and Cd36 molecule (Cd36) in rWAT, and of insulin receptor substrate 1 (Irs1), sterol regulatory element binding transcription factor 1 (Srebp1), carnitine palmitoyltransferase 1 (Cpt1), Insr, stearoyl-CoA desaturase 1 (Scd1), peroxisome proliferator-activated receptor alpha (Pparα), Lepr, Cd36 and sterol regulatory element binding transcription factor 2 (Srebp2) in liver, as previously described [9 (link)]. As housekeeping gene, guanosine diphosphate dissociation inhibitor (Gdi) was selected. Sequences and amplicon size of primers used (Sigma; Madrid, Spain) are detailed in Supplementary Materials Table S1.
Full text: Click here
Publication 2023
Carnitine Palmitoyltransferase I fatty acid desaturase 1, human Genes, Housekeeping Guanosine Diphosphate HNF1B protein, human Insulin Receptor IRS1 protein, human Leptin leptin receptor, human Liver Oligonucleotide Primers Phospholipase PPAR alpha PPAR gamma Regulatory Sequences, Nucleic Acid RNA, Messenger SREBF1 protein, human Sterols
Salts and organic solvents used in solution preparations were purchased from Fisher Scientific (Leicestershire, UK), Sigma Chemicals (St. Louis, MO, USA, EUA), or Merck (Darmstad, Germany), with the highest grade of purity commercially available. It used antibodies to analyze D1R, D2R, DARPP32 (ab81296, ab85367, and ab40801 respectively, Abcam, UK), and tyrosine hydroxylase (TH), (T1299, Sigma Aldrich, St. Louis, MO, USA) at a 1:1000 dilution. Moreover, antibodies against GLP-1 and GLP-1R and against the phosphorylated form of insulin receptor were used (ab22625, ab218532, and InsR-Tyr972, ab5678 respectively, Abcam, UK) as well, against phosphorylated AMPK form (Thr172, 2535S, Cell Signalling Technology, Danvers, MA, USA, EUA). Calnexin was used as loading control (AB0037, Sicgen, Cantanhede, Portugal). Plasma dopamine levels and plasma GLP-1 levels were assessed through the Dopamine ELISA Kit, (Abnova, Taiwan) and Rat GLP1/Glucagon-like Peptide 1 ELISA Kit, (LifeSpan BioScience, Inc., Washington, DC, USA) respectively.
Full text: Click here
Publication 2023
Antibodies Calnexin Dopamine Dopamine and cAMP-Regulated Phosphoprotein 32 EHMT1 protein, human Enzyme-Linked Immunosorbent Assay Glucagon-Like Peptide 1 INSR protein, human Insulin Receptor Plasma Salts Solvents Technique, Dilution Tyrosine 3-Monooxygenase
Western blot analysis and immunoprecipitation were carried out as described previously73 (link)–75 . Total proteins were prepared from the tissues and cells with RIPA buffer containing protease and phosphatase inhibitors. The lysates were subjected to western blotting and the protein was separated with SDS-PAGE and transferred to PVDF transfer membranes (Millipore, Bedford, MA, USA). Corresponding antibodies were used to detect proteins. The protein bands were measured by ChemiDocTM Touch Imaging System (Bio-Rad, Richmond, CA, USA). All experiments were repeated at least three times and amount of phosphorylated protein was quantified by Image J and normalized to amount of total protein.
For immunoprecipitation and ubiquitination, HEK293T and adipocytes were homogenized in lysis buffer. 1 mg of cell lysate protein was immunoprecipitated with indicated antibodies at 4 °C overnight. Immunoprecipitations were pulled down with Protein A/G Agarose followed by western blot analysis. For ubiquitination assays, cells were lysed with lysis buffer plus 2 mM N-Ethylmaleimide (NEM) and denudated by heating for 10 min, and centrifuged at 14,000 g for 15 min at 4 °C. The subsequent steps for the in vivo ubiquitination assay were carried out as described above in methods of immunoprecipitation and western blotting experiments.
The following antibodies were used: anti-TRPM7 (Sigma-Aldrich, AB15562), WB 1:500; anti-phospho-IRS-1 (Ser307) (Cell Signaling Technology, 2381), WB 1:1000; anti-IRS-1 (Cell Signaling Technology, 2382), WB 1:1000; anti-phospho-Insulin Receptor β (Tyr1345) (Cell Signaling Technology, 3026), WB 1:1000; anti-Insulin Receptor β (Cell Signaling Technology, 3025), WB 1:1000; anti-phospho-Akt (Ser473) (Cell Signaling Technology, 4060), WB 1:1000; anti-Akt (Cell Signaling Technology, 9272), WB 1:1000; anti-phospho-NFκB-p65 (Ser536) (Cell Signaling Technology, 3033), WB 1:1000; anti-NFκB-p65 (Cell Signaling Technology, 8242),WB 1:1000; anti-phospho-IKKβ (Ser180) (Cell Signaling Technology, 2694), WB 1:1000; anti-IKKβ (Cell Signaling Technology, 8943),WB 1:1000; anti-IκBα (Cell Signaling Technology, 9242), WB 1:1000; anti-phospho-TAK1 (Ser412) (Cell Signaling Technology, 9339), WB 1:1000; anti-TAK1 (Cell Signaling Technology, 5206), WB 1:1000, IP 1:50; anti-phospho-CaMKII (Thr286) (Cell Signaling Technology, 12716) WB 1:1000; anti-CaMKII (Cell Signaling Technology, 50049) WB 1:1000; anti-Ub (Cell Signaling Technology, 3936), WB 1:1000; anti-Flag (Sigma, F1804), WB 1:1000, IP 10 μl for 1 mg protein; anti-HA (Sigma, H3663), WB 1:1000; anti-TRAF6 (Santa Cruz, sc-8409), WB 1:1000, IP 4 μg for 1 mg protein; anti-c-Cbl (Santa Cruz, sc-1651), WB:1:1000; anti-GAPHD (Proteintech, 60004-1-Ig), WB 1:2000; anti-α-tubulin (Proteintech, 11224-1-AP), WB 1:2000; anti-rabbit (Cell Signaling Technology, 7074), WB 1:2000; anti-mouse (Cell Signaling Technology, 7076), WB 1:2000.
Full text: Click here
Publication 2023
Adipocytes alpha, NF-KappaB Inhibitor alpha-Tubulin Antibodies Biological Assay Buffers Calmodulin-Dependent Protein Kinase II Cells Chemokine CXCL10 Ethylmaleimide G-substrate IkappaB Kinase beta Immunoprecipitation inhibitors Insulin Receptor IRS1 protein, human Mus Pancreatic beta Cells Peptide Hydrolases Phosphoric Monoester Hydrolases polyvinylidene fluoride Proteins Rabbits Radioimmunoprecipitation Assay SDS-PAGE Sepharose Staphylococcal Protein A Tissue, Membrane Tissues TNF Receptor Associated Factor 6 Touch Transcription Factor RelA TRPM7 protein, human Ubiquitination Western Blot

Top products related to «Insulin Receptor»

Sourced in United States, United Kingdom, China, Germany, Japan, Italy, Macao, Switzerland, Canada
The Anti-AKT product is a primary antibody that specifically binds to the AKT protein. AKT is a serine/threonine kinase that plays a crucial role in various cellular processes, such as cell growth, proliferation, and survival. The Anti-AKT antibody can be used for the detection and analysis of AKT in various experimental applications, including Western blotting, immunoprecipitation, and immunohistochemistry.
Sourced in United States, United Kingdom, Japan, Germany, France, Canada
The Anti-phospho-Akt (Ser473) is a primary antibody that specifically recognizes the Akt protein when phosphorylated at serine 473. It is used for the detection and analysis of the activated form of Akt in various cellular and experimental contexts.
Sourced in United States, United Kingdom, China, Germany, Canada, Morocco, Japan, Italy, Switzerland, France, Israel, Singapore, Hong Kong, Sweden, Macao, Panama
β-actin is a cytoskeletal protein that is ubiquitously expressed in eukaryotic cells. It is a component of the microfilament system and plays a crucial role in various cellular processes, such as cell motility, maintenance of cell shape, and intracellular trafficking.
Sourced in United States
The insulin receptor β is a membrane-bound protein that plays a crucial role in insulin signaling. It is the primary receptor for insulin, a hormone responsible for regulating glucose metabolism and energy homeostasis.
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.
Sourced in United States
The Anti-insulin receptor β is a primary antibody that recognizes the β subunit of the insulin receptor. It is used in research applications to detect and study the insulin receptor protein.
Sourced in United States
Anti-IRS-1 is a laboratory equipment product. It is a tool used for the detection and quantification of IRS-1 protein levels in biological samples. The core function of this product is to provide researchers with a reliable method to measure the expression of IRS-1, a key mediator of insulin signaling pathways.
Sourced in United States, United Kingdom, China, Canada
Total AKT is a quantitative sandwich immunoassay designed to measure the total AKT protein levels in cell and tissue lysates. It provides a reliable method for determining the overall expression of AKT, a key signaling molecule involved in various cellular processes.
Sourced in United States, China, United Kingdom, Germany, Australia, Japan, Canada, Italy, France, Switzerland, New Zealand, Brazil, Belgium, India, Spain, Israel, Austria, Poland, Ireland, Sweden, Macao, Netherlands, Denmark, Cameroon, Singapore, Portugal, Argentina, Holy See (Vatican City State), Morocco, Uruguay, Mexico, Thailand, Sao Tome and Principe, Hungary, Panama, Hong Kong, Norway, United Arab Emirates, Czechia, Russian Federation, Chile, Moldova, Republic of, Gabon, Palestine, State of, Saudi Arabia, Senegal
Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
Sourced in United States, United Kingdom, China, Germany, Japan, Canada, Morocco, France, Netherlands, Ireland, Israel, Australia, Sweden, Macao, Switzerland
GAPDH is a protein that functions as an enzyme involved in the glycolysis process, catalyzing the conversion of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. It is a common reference or housekeeping protein used in various assays and analyses.

More about "Insulin Receptor"

The insulin receptor (IR) is a critical transmembrane protein that binds to insulin and mediates its vital biological effects.
It is a tyrosine kinase receptor that plays a central role in regulating glucose and lipid metabolism, as well as cell growth and differentiation.
Dysfunction of the IR is implicated in insulin resistance and the development of type 2 diabetes.
Research on the IR can provide valuable insights into the pathogenesis and treatment of metabolic disorders.
Optimizing IR research is crucial, and PubCompare.ai is a powerful tool that helps users locate the best protocols and products from literature, preprints, and patents.
Their AI-driven comparisons enhance reproducibility and accuracy, ensuring that your IR experiments yield reliable results.
When studying the IR, it's important to consider related proteins and markers such as Anti-AKT, Anti-phospho-Akt (Ser473), β-actin, Insulin receptor β, Anti-insulin receptor β, Anti-IRS-1, Total AKT, FBS, and GAPDH.
These molecules can provide valuable insights into the complex signaling pathways and cellular processes involving the IR.
By leveraging the power of PubCompare.ai and incorporating a comprehensive understanding of the IR and its related components, researchers can optimize their investigations and make significant strides in unraveling the mysteries of metabolic disorders.
This knowledge can ultimately lead to the development of more effective treatments and improved patient outcomes.