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AREG protein, human

AREG (Amphiregulin) is a member of the epidermal growth factor (EGF) family of proteins that plays a key role in cell proliferation, differentiation, and survival.
It is involved in various physiological and pathological processes, including tissue development, wound healing, and cancer progression.
AREG binds to and activates the EGF receptor (EGFR), triggering downstream signaling cascades that regulate gene expression and cellular behavior.
Researchers studying AREG protein and its functions can utilize PubCompare.ai, a powerful tool that helps identify the most effective protocols and procedures from literature, preprints, and patents.
This AI-driven comparison platform can enhance the reproducibility and accuracy of AREG protein experiments, allowing researchers to discover the best products and methodologies to advance their studies.

Most cited protocols related to «AREG protein, human»

To facilitate cross-species comparison of methylomes of multiple species, we converted the methylation data of mouse and chimpanzee to the corresponding locations in the human genome. The liftOver tool provided by UCSC Genome Browser http://genome.ucsc.edu/cgi-bin/hgLiftOver is used to directly convert the methylation level file at individual cytosines (output from the program methcounts ) to the human genome. Next we rerun the hmr and pmd programs on the converted methylation data file. Since the program amr works on the mapped read file, we directly liftover the list of AMRs with the liftOver program.
Publication 2013
AREG protein, human Cytosine Epigenome Genome Genome, Human Methylation Mice, House Pan troglodytes Species Specificity

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Publication 2019
Amino Acids, Essential AREG protein, human beta-D-Galactoside alpha 2-6-Sialyltransferase Bos taurus Cell Lines Cells Cloning Vectors Dietary Supplements epidermal growth factor receptor VIII Fetal Bovine Serum Gentamicin Glucose Glutamine Insulin Madin Darby Canine Kidney Cells Parent Penicillins Puromycin Serum Short Hairpin RNA Streptomycin
Survey data are derived from the World Bank’s African Migration and Remittances Surveys (AMRS), which collected standardized retrospective data on international and internal migration for ~2,000 households per country. Retrospective household-level data have a long history of successful use for investigating the determinants of migration in the developing world (Massey and Espinosa 1997 ; Smith and Thomas 2003 ). In the case of AMRS, households reported the destination of all departed household members and return migrants, as well as the timing and motivation of each move. To limit errors due to retrospection and whole-household mobility, we use data on migrants who departed in the year of data collection and in the five years prior (2004–09). In Uganda, Nigeria and Senegal the household sample is nationally representative. In Burkina Faso and Kenya, 10 provinces1 and 17 districts respectively were included as the most important sources of migrants identified by census data (Table 1; Supplement F2). In all countries, disproportionate sampling was then used within the sample areas to oversample enumeration areas that were more important sources of migration as measured by census data, and two-phase sampling was used within enumeration areas to select households, oversampling those that had sent migrants (Gray & Bilsborrow 2013 (link); Plaza et al. 2011 ). We use survey weights in all analyses to account for this sampling design. Interviews took place in late 2009 in Kenya, Burkina Faso and Senegal and early 2010 in Uganda; a small number of moves which took place in Uganda in 2010 are consolidated with those of 2009.
We use AMRS to create a household-year dataset on 9,812 households over a 6 year period (2009-2004) with information on migration and control variables (Table 1). Migration is measured as the number of migrants ages ten or older sent by the household in year t, a count which is subsequently decomposed by migrant destination, gender and reported motivation. Included control variables are standard for the literature on the determinants of migration (Massey and Espinosa 1997 ) and include household composition and characteristics of the household head at the beginning of 2004 (Table 2). These values were estimated by adding household members born before 2004 to migrants who departed during the study period and adjusting ages appropriately. Potential control variables which were likely to have been measured with error for 2004 were excluded. Given that very few households had heads under age 20 at the time of the survey, 272 households with heads under age 25 at the time of the survey were excluded from the analysis as unlikely to have been in existence in 2004. Data on one or more control variables are missing for 313 households. These values are interpolated to the country median and this interpolation was accounted for through the inclusion of missing indicators in the regression analysis. Table 2 also documents considerable heterogeneity across the five study countries, ranging from Kenya with the highest level of education, smallest household size, lowest rate of previous migration, lowest proportion rural, and lowest proportion working in the primary sector, to Burkina Faso at the opposite end of the spectrum.
Households in AMRS are linked to climate by their district-level administrative unit of residence, for a total of 140 such units. For comparison purposes, we chose two high-quality datasets that are available at high spatial resolution and extracted them as spatial means for these units: (1) the Climatic Research Unit’s (CRU) time-series 3.21 containing high-resolution monthly precipitation and temperature; and (2) monthly mean land surface temperature and total surface precipitation from the NASA Modern Era-Retrospective Analysis for Research and Applications (MERRA). CRU is a monthly global dataset at 0.5° resolution (~50km at the equator) created by interpolating data from weather stations (UEACRU et al. 2013 ). Derived from a network of over 4000 stations, including a large number in Sub-Saharan Africa, CRU data are considered to provide reliable climate information in Africa (e.g., Zhang et al. 2013 ). MERRA is a reanalysis product, produced through the integration of observed data, including satellite data, with numerical models. The MERRA data are available sub-daily at 0.5° × 0.67° lat-long resolution (Rienecker et al. 2011 ).
From these climate data sources, we extract the following values as spatial means at the district-year scale: the total annual precipitation, the month in which 50% annual precipitation was reached, and the mean annual temperature. Temperature and precipitation anomalies were also defined relative to a 1981–2010 base period. District-level units were defined as districts in Kenya and Uganda, provinces in Burkina Faso and departments in Senegal. Temperature anomalies have been shown to have robust negative effects on agricultural output across Sub-Saharan Africa, while precipitation usually but not always has positive effects (Seo et al. 2009 ). Because previous studies have shown that climate can have lagged effects on migration for at least two years (Bohra-Mishra et al. 2014 (link)), we average annual climate values across year t and t-1 as well as test for longer lags (Table 3). Substantial differences in climate anomalies extracted from CRU and MERRA (Table 3) reinforce the importance of using data from multiple climate sources (Auffhammer et al. 2013 ).
Negative binomial regression is then used to model the number of migrants per household-year as a function of climate variables and controls. This modelling approach has been widely used across the quantitative social sciences to model count outcomes (Cameron and Trivedi 2013 ), including migration (Taylor et al. 2003 ). Our core specification of climate includes linear measures of annual precipitation and temperature anomalies derived from CRU and averaged over years t and t-1 (Table 3). We also test additional plausible specifications of climate as described below. Predictors include climate variables, a set of socio-demographic controls, district-level fixed effects, a quadratic time trend (to account for potential retrospective reporting biases), and, for a small fraction of households, indicators for missing values on one or more control variables. Standard errors are corrected for clustering at the district-level unit. Socio-demographic control variables include the number of migrants sent before 2004, rural versus urban location, and various demographic characteristics of the household and household head estimated for 2004 (Table 2). The inclusion of district-level fixed effects allows each district to have a baseline rate of migration and accounts for all time-invariant district-level factors as long as these effects are linear. To account for potential errors of retrospection we allow for a quadratic time trend by including both linear and squared terms for the year (VanWey 2005 ). With inclusion of the time trend, the effects of climate variables are statistically identified by local deviations of climate from the national-scale trend.
Publication 2016
AREG protein, human Childbirth Climate Climate Change Dietary Supplements Genetic Heterogeneity Head Head of Household Households Migrants Motivation Negroid Races Range of Motion, Articular
To identify allele-specific methylated regions, we use the linkage information of the methylation status between adjacent cytosines in a read. The separation of reads into two alleles and the testing of whether a certain region fits the allele-specific model is carried out with the statistical method described by Fang et al. [17] . Additionally, a single-site profile for an allele-specific methylation “score” can be computed along the genome by testing for significance of linkage between methylation status in reads covering adjacent CpGs. The programs for identifying AMRs and computing allelic scores are amrfinder and allelicmeth.
Publication 2013
Alleles AREG protein, human cytidylyl-3'-5'-guanosine Cytosine Genome Methylation Seizures
Total RNA from KCs or frozen skin was isolated using RNeasy mini kits with on-column DNase digestion (Qiagen, Valencia, CA). Total RNA was reverse transcribed using the Applied Biosystems High Capacity cDNA Reverse Transcription Kit. cDNA equivalent to 5–40 ng of total RNA was used for QRT- PCR using pre-validated TaqMan gene expression assays (Applied Biosystems, Foster City, CA) for AREG (# Hs00155832), BTC (# Hs00156140), EREG (# Hs00914313, EPGN (# Hs02385425), HB-EGF (# Hs00181813, TGF-α (# Hs00608187) and ribosomal protein large P0 (RPLP0 or 36B4, # Hs99999902) (Laborda, 1991 (link); Minner and Poumay, 2008 ). Data are expressed as fold-change relative to 36B4 multiplied by 103 (fold-change versus 36B4 = 2 –(CT target -CT 36B4)).
Publication 2009
AREG protein, human Biological Assay Deoxyribonuclease I Digestion DNA, Complementary EREG protein, human Freezing Gene Expression Heparin-binding EGF-like Growth-Factor Reverse Transcription ribosomal protein P0 RPLP0 protein, human Skin TGFA protein, human

Most recents protocols related to «AREG protein, human»

Both cell lysates and EV preparations, which were lysed in RIPA or 1X sample buffer, were electrophoretically separated using 10% mini‐PROTEAN precast gels (BioRad). Gels were loaded for western analysis with EV lysates extracted from the same protein mass of secreting cells, so that changes in band intensity on the blots with glutamine depletion reflected a net change in secretion of the marker on a per cell basis (see Fan et al., 2020 (link)). Protein preparations were ultimately dissolved in either reducing (containing 5% β‐mercaptoethanol) or non‐reducing (for CD63 and CD81 detection) sample buffer and were heated to 90°C–100°C for 10 min before loading with a pre‐stained protein ladder (Bio‐Rad). Proteins were wet‐transferred to polyvinylidene difluoride (PVDF) membranes at 100 V for 1 h using a Mini Trans‐Blot Cell (Bio‐Rad). Membranes were then blocked with either 5% milk (CD63 detection) or 5% BSA in TBS buffer with Tween‐20 (TBST) for 30 min and probed overnight at 4°C with primary antibody diluted in blocking buffer. The membranes were washed for 3 × 10 min with TBST, then probed with the relevant secondary antibodies for 1 h at 22°C, washed for 3 × 10 min again, and then the signals detected using the enhanced chemiluminescent detection reagent (Clarity, BioRad) and the Touch Imaging System (BioRad). Relative band intensities were quantified by ChemiDoc software (Bio‐Rad) or ImageJ. Signals were normalised to cell lysate protein (Fan et al., 2020 (link)).
Antibody suppliers, catalogue numbers and concentrations used were: rabbit anti‐CHMP1a (Proteintech #15761‐1‐AP, 1:500), rabbit anti‐CHMP1b (Proteintech #14639‐1‐AP, 1:500), rabbit anti‐IST1 (Biorad #VPA00314, 1:500), mouse anti‐CHMP5 (Santa Cruz #sc‐374338, 1:500), rabbit anti‐4E‐BP1 (Cell Signaling Technology #9644, rabbit anti‐p‐4E‐BP1‐Ser65 (Cell Signaling Technology #9456, 1:1000), rabbit anti‐S6 (Cell Signaling Technology #2217, 1:4000), rabbit anti‐p‐S6‐Ser240/244 S6 (Cell Signalling Technology #5364, 1:4000), rabbit anti‐Caveolin‐1 (Cell Signaling Technology #3238, 1:500), goat anti‐AREG (R&D Systems #AF262, 1:200), mouse anti‐Tubulin (Sigma #T8328, 1:4000), mouse anti‐CD81 (Santa Cruz #23962, 1:500), mouse anti‐CD63 (BD Biosciences # 556019, 1:500), rabbit anti‐Syntenin‐1 antibody (Abcam ab133267, 1:500), rabbit anti‐Tsg101 (Abcam ab125011, 1:500), mouse anti‐Rab11 (BD Biosciences #610657, 1:500), sheep anti‐TGN46 (BioRad; AHP500G, 1:1000), rabbit anti‐EEA1 (Cell Signalling Technology #3288, 1:1000) , anti‐mouse IgG (H+L) HRP conjugate (Promega #W4021, 1:10000), anti‐rabbit IgG (H+L) HRP conjugate (Promega #W4011, 1:10000), anti‐goat IgG (H+L) HRP conjugate (R&D Systems #HAF109, 1:100).
Publication 2023
2-Mercaptoethanol anti-IgG Antibodies Antibodies, Anti-Idiotypic AREG protein, human Buffers Caveolin 1 Cells Domestic Sheep EIF4EBP1 protein, human Gels Glutamine Goat Immunoglobulins Milk, Cow's Mus polyvinylidene fluoride Promega Proteins Proto-Oncogene Mas Rabbits Radioimmunoprecipitation Assay secretion Syntenin-1 Tissue, Membrane Touch TSG101 protein, human Tubulin Tween 20
Western blot was performed as previously described [71 (link)]. In brief, total proteins of cultured cells were lysed in lysis buffer (150 mM NaCl, 50 mM Tris- HCl, pH 7.5, 5 mM EDTA, 1% Triton X-100, 10 mM NaF, 1 mM Na3VO3, 0.1% SDS, and 1% Sodium deoxycholate) supplemented with protease inhibitor cocktail (4693116001, Roche, Basel, Switzerland). The supernatants collected from cultured epithelial Ishikawa cells with serum-free culture medium were dialyzed in 2 L distilled water for 2 h at room temperature with stirring and lyophilized in a vacuum lyophilizer (FreeZone Plus, LABCONCO, Kansas, MO, USA) for 8 h. The lyophilized powder was dissolved in lysis buffer. The BCA kit (23225, Thermo Scientific, Shanghai, China) were used to measure protein concentration. Protein lysates (5–10 μg) were electrophoresed in SDS-PAGE gels and transferred onto polyvinylidene fluoride (PVDF) membranes (IPVH00010, Millipore, Billerica, MA, USA). Membranes were blocked with 5% non-fat milk (A600669, Sangon, Shanghai, China) for 1 h at room temperature and then incubated with the specific primary antibody overnight at 4 °C. After the membranes were incubated with horseradish peroxidase (HRP)-conjugated secondary antibody (1:5000, Invitrogen, Carlsbad, CA, USA) for 1 h at room temperature, the signals were detected with an ECL Chemiluminescent Kit (WBKLS0100, Millipore, Burlington, MA, USA) on Tanon Imaging System (5200, Tanon, Shanghai, China). The primary antibodies used in this study included anti-Tubulin (#2144, 1:1000, Cell Signaling, Danvers, MA, USA), anti-GAPDH (#sc-32233, 1:1000, Santa Cruz, CA, USA), anti-ODC1 (#28728-1-AP, 1:1000, Proteintech, Rosemont, IL, USA), anti-IL4I1 (#ab222102, 1:1000, Abcam, Cambridge, UK), anti-Integrin β3 (#13166s, 1:1000, Cell Signaling Technology), anti-HOXA10 (#Sc-28620, 1:1000, Santa Cruz), anti-FOXO1 (#2880, 1:1000, Cell Signaling Technology), anti-AREG (#A1860, 1:500, Abclonal, Woburn, MA, USA), anti-Lamin A/C (#2032s, 1:1000, Cell Signaling Technology), anti-AHR (#NB100-2289SS, 1:1000, Novus Biologicals, Englewood, CO, USA).
Publication 2023
Antibodies AREG protein, human Biological Factors Buffers Cultured Cells Culture Media Deoxycholic Acid, Monosodium Salt Edetic Acid Epithelial Cells GAPDH protein, human Gels Horseradish Peroxidase Immunoglobulins Integrins LMNA protein, human Milk, Cow's Novus polyvinylidene fluoride Powder Protease Inhibitors Proteins SDS-PAGE Serum Sodium Chloride Tissue, Membrane Triton X-100 Tromethamine Tubulin Vacuum Western Blotting
RIPA buffer containing 50 mM tris (pH 7.4), 150 mM NaCl, 1% NP-40, 0.5% sodium deoxycholate and 0.1% SDS was used for cell lysis (Beyotime). Then, 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was to achieve protein separation. Polyvinylidene difluoride (PVDF) membrane (Millipore) was used for protein transfer. After blocking with a 5% blocking solution, the PVDF membrane was incubated with the primary antibody overnight at 4 °C. Following incubation with appropriate secondary antibodies, treatment with Luminata Crescendo Western HRP substrate (Millipore) was performed as well as exposure and digital imaging. The primary antibodies of TPM2 (1:1000, Proteintech, 28587-1-AP), PDLIM7 (1:1000, Proteintech, 10221-1-AP), YAP1 (1:1000, Proteintech, 13584-1-AP), p-YAP1(S127) (1:1000, Abcam, ab76252), NKX3.1 (1:1000, Abcam, ab196020), PSA (1:1000, Abcam, ab76113), c-Myc (1:1000, Cell Signaling Technology, 18583), AREG (1:1000, Proteintech, 16036-1-AP), PCAN (1:1000, Proteintech, 10205-2-AP), HA tag polyclonal antibody (1:1000, Proteintech, 51064-2-AP), GST tag polyclonal antibody (1:1000, Proteintech, 10000-0-AP), MYC tag polyclonal antibody (1:1000, Proteintech, 16286-1-AP) and GAPDH (1:2000, Proteintech, 10494-1-AP). The Beyotime cytoplasmic protein extraction kit was used to extract nuclear proteins based on the manufacturer’s instructions.
Publication 2023
Antibodies AREG protein, human Buffers Cells Cytoplasm Deoxycholic Acid, Monosodium Salt Fingers GAPDH protein, human Immunoglobulins Nonidet P-40 Nuclear Proteins Oncogenes, myc polyvinylidene fluoride Proteins Radioimmunoprecipitation Assay SDS-PAGE Sodium Chloride Tissue, Membrane Tromethamine YAP1 protein, human
Human UM cell line (MUM-2B) was obtained from the Fuheng Biology Inc., (Fuheng, Shanghai, China). For MUM-2B cell culture, DMEM (keyGEN bioTECH, China) with 10% fetal bovine serum (FBS) was used. Cells were transfected with the synthesized siRNAs (GenePharma, China) targeting AREG by the Lipofectamine3000 based on the manufacturer’s protocol. The siRNA-AREG sequences are provided in Supplementary Table S2.
Publication 2023
AREG protein, human Cell Culture Techniques Cell Lines Cells Fetal Bovine Serum Homo sapiens RNA, Small Interfering
The cell total RNA of was collected using RNA easy reagent (Vazyme, China) and cDNA was obtained using a PrimeScript RT Reagent Kit (Takara, Japan). Then, qRT-PCR was performed through a ChamQ SYBR qPCR Master Mix (Vazyme, China). The relative expression levels of m RNA were normalized to GAPDH. The primer sequences of AREG and GAPDH are shown in Supplementary Table S1.
Publication 2023
AREG protein, human DNA, Complementary GAPDH protein, human Oligonucleotide Primers Transcription, Genetic

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The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.
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The High-Capacity cDNA Reverse Transcription Kit is a laboratory tool used to convert RNA into complementary DNA (cDNA) molecules. It provides a reliable and efficient method for performing reverse transcription, a fundamental step in various molecular biology applications.
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TRIzol is a monophasic solution of phenol and guanidine isothiocyanate that is used for the isolation of total RNA from various biological samples. It is a reagent designed to facilitate the disruption of cells and the subsequent isolation of RNA.
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The IScript cDNA Synthesis Kit is a reagent kit used for the reverse transcription of RNA into complementary DNA (cDNA). The kit contains all the necessary components to perform this reaction, including a reverse transcriptase enzyme, reaction buffer, and oligo(dT) primers.
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The RNeasy kit is a laboratory equipment product that is designed for the extraction and purification of ribonucleic acid (RNA) from various biological samples. It utilizes a silica-membrane-based technology to efficiently capture and isolate RNA molecules.
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Recombinant AREG is a protein produced in a laboratory using recombinant DNA technology. It is the human Amphiregulin (AREG) protein.
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.

More about "AREG protein, human"

Amphiregulin (AREG) is a member of the epidermal growth factor (EGF) family of proteins, playing a crucial role in cell proliferation, differentiation, and survival.
It is involved in various physiological and pathological processes, such as tissue development, wound healing, and cancer progression.
AREG binds to and activates the EGF receptor (EGFR), triggering downstream signaling cascades that regulate gene expression and cellular behavior.
Researchers studying AREG protein and its functions can utilize PubCompare.ai, a powerful AI-driven comparison platform that helps identify the most effective protocols and procedures from literature, preprints, and patents.
This tool can enhance the reproducibility and accuracy of AREG protein experiments, allowing researchers to discover the best products and methodologies to advance their studies.
To extract and analyze AREG RNA and protein expression, researchers may employ techniques like the RNeasy Mini Kit, TRIzol reagent, and High-Capacity cDNA Reverse Transcription Kit.
These tools enable efficient RNA extraction, cDNA synthesis, and real-time PCR analysis using the StepOnePlus Real-Time PCR System and TaqMan Gene Expression Assays.
Moreover, researchers can investigate the functional aspects of AREG by working with recombinant AREG protein and utilizing transfection methods like Lipofectamine 2000 to introduce AREG-encoding plasmids into cell lines.
These approaches can help elucidate the signaling pathways and biological processes regulated by AREG.
In summary, the AREG protein is a versatile and influential member of the EGF family, with significant implications in various physiological and pathological contexts.
By leveraging PubCompare.ai and employing established molecular biology techniques, researchers can optimize their AREG protein research, enhance reproducibility, and drive their studies forward with greater efficiency and accuracy.