Log In Sign up
The largest database of trusted experimental protocols
> Chemicals & Drugs > Amino Acid > Activins

Activins

Activins are a family of dimeric protein growth and differentiation factors.
They are members of the transforming growth factor-beta superfamily and play important roles in cell proliferation, differentiation, and apoptosis.
Activins exhert their effects through binding to specific cell-surface receptors and activating intracellular signaling pathways.
They are involved in a variety of physiological and pathological processes, including embryonic development, hormone regulation, immune function, and disease states such as cancer and fibrosis.
Researchers can optimize Activin-related studies using PubCompare.ai, an AI-driven platform that helps locate high-quality protocols, products, and methods from the scientific literature, preprints, and patents to enhance reproducibility and accuracy.

Most cited protocols related to «Activins»

1
CellChatDB: Comprehensive Ligand-Receptor Interactions
Cited 44 times
To construct a database of ligand-receptor interactions that comprehensively represents the current state of knowledge, we manually reviewed other publicly available signaling pathway databases, as well as peer-reviewed literature and developed CellChatDB. CellChatDB is a database of literature-supported ligand-receptor interactions in both mouse and human. The majority of ligand–receptor interactions in CellChatDB were manually curated on the basis of KEGG (Kyoto Encyclopedia of Genes and Genomes) signaling pathway database (https://www.genome.jp/kegg/pathway.html). Additional signaling molecular interactions were gathered from recent peer-reviewed experimental studies. We took into account not only the structural composition of ligand-receptor interactions, that often involve multimeric receptors, but also cofactor molecules, including soluble agonists and antagonists, as well as co-stimulatory and co-inhibitory membrane-bound receptors that can prominently modulate ligand-receptor mediated signaling events. The detailed steps for how CellChatDB was built and how to update CellChatDB by adding user-defined ligand-receptor pairs were provided in Supplementary Note 1. To further analyze cell–cell communication in a more biologically meaningful way, we grouped all of the interactions into 229 signaling pathway families, such as WNT, ncWNT, TGFβ, BMP, Nodal, Activin, EGF, NRG, TGFα, FGF, PDGF, VEGF, IGF, chemokine and cytokine signaling pathways (CCL, CXCL, CX3C, XC, IL, IFN), Notch and TNF. The supportive evidences for each signaling interaction is included within the database.
Jin S., Guerrero-Juarez C.F., Zhang L., Chang I., Ramos R., Kuan C.H., Myung P., Plikus M.V, & Nie Q. (2021). Inference and analysis of cell-cell communication using CellChat. Nature Communications, 12, 1088.
Full text: Click here
Publication 2021
Activins agonists antagonists Cell Communication Chemokine Cytokine Genes Genome Homo sapiens Ligands Mus Platelet-Derived Growth Factor Psychological Inhibition Signal Transduction Pathways TGFA protein, human Tissue, Membrane Transforming Growth Factor beta Vascular Endothelial Growth Factors
2
Monolayer Differentiation of hPSCs to Paraxial and Lateral Mesoderm
Cited 25 times

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2016
accutase Activins Becaplermin BMP4 protein, human Cartilage Fibroblast Growth Factor 2 Fibroblasts LDN 193189 Mesoderm Paraxial Mesoderm PD-0325901 Serum Somites thiazovivin transforming growth factor beta1.2 vismodegib XAV939
3
Pluripotent Stem Cell Differentiation to Hepatic and Pancreatic Endoderm
Cited 9 times
hESCs (H9 from WiCell, Maddison, WI, USA) and hIPSCs (BBHX8, A1ATD-1, JRO1D; University of Cambridge, Cambridge, UK) [16 (link)] were passaged weekly using collagenase IV and maintained in chemically defined medium (CDM) supplemented with activin A (10 ng/ml) and FGF2 (12 ng/ml), as described previously [17 (link)]. Differentiation was carried out as described in Fig. 1 and is explained in detail in the electronic supplementary material (ESM) Methods.

Protocols to generate hepatic and pancreatic endoderm from hESCs and hIPSCs. Successive culture conditions driving differentiation of pluripotent stem cells towards pancreatic endoderm and hepatic endoderm. A, activin; ADV, advanced DMEM; B, BMP; CMRL, Connaught Medical Research Laboratories medium; CYCP, cytochrome P450; DAPT, N-(N-[3,5-diflurophenylacetyl]-l-alanyl)-S-phenylglycine t-butyl ester; F, FGF; HGF, hepatocyte growth factor; Ly, LY294002; Nog, noggin; OSM, oncostatin M

Cho C.H., Hannan N.R., Docherty F.M., Docherty H.M., Joåo Lima M., Trotter M.W., Docherty K, & Vallier L. (2012). Inhibition of activin/nodal signalling is necessary for pancreatic differentiation of human pluripotent stem cells. Diabetologia, 55(12), 3284-3295.
Publication 2012
1,2-dilinolenoyl-3-(4-aminobutyryl)propane-1,2,3-triol activin A Activins alpha 1-Antitrypsin Deficiency Collagenase Cytochrome P450 Endoderm Esters Fibroblast Growth Factor 2 Hepatocyte Growth Factor Human Embryonic Stem Cells Human Induced Pluripotent Stem Cells LY 294002 noggin protein OSM protein, human Pancreas Pluripotent Stem Cells
4
Actin Cytoskeleton Analysis of Xenopus Explants
Cited 8 times
For the animal cap explants, MARCKS mRNA or Mo was coinjected with 0.5 pg activin mRNA into the animal pole of two-cell embryos. The animal cap was dissected from stage-9 embryos. For DMZ explants, mRNA or a Mo was injected into the two dorsal blastomeres of four-cell embryos. Explants were isolated at stage 10+. These explants were cultured in 1× Steinberg's solution until sibling embryos reached stage 17. To dissociate cells from the explants, the explants were incubated in the Ca2+-Mg2+–free medium for 2 h. For the cytological observation, explants and dissociated cells were cultured in 1× Steinberg's solution on an FN-coated dish (4000–030; Iwakil), or on a cover glass coated with FN (∼1 μg/cm2, F1141; Sigma-Aldrich). To stain F-actin, cells were fixed in 4% PFA and stained with PBS 0.5% Triton X-100 containing a 40-fold dilution of BODIPY 581/589 phalloidin (B-3416; Molecular Probes) or Alexa Fluor 488 phalloidin (A-12379; Molecular Probes). For confocal microscopy, images were captured using 510 software (Carl Zeiss MicroImaging, Inc.). All images were prepared for publication using Adobe Photoshop software.
Iioka H., Ueno N, & Kinoshita N. (2004). Essential role of MARCKS in cortical actin dynamics during gastrulation movements. The Journal of Cell Biology, 164(2), 169-174.
Publication 2004
Activins alexa fluor 488 Animals Blastomeres BODIPY Cells Embryo F-Actin Hyperostosis, Diffuse Idiopathic Skeletal MARCKS protein, human Microscopy, Confocal Molecular Probes Phalloidine Polar Bodies RNA, Messenger Technique, Dilution Triton X-100
5
Cardiomyocyte Differentiation from Human Embryonic Stem Cells
Cited 7 times
Detailed methods are provided in the Online Data Supplement. In brief, cardiomyocytes were generated from H7 hESCs using our recently reported directed differentiation protocol, which involves serum-free monolayer culture and serial treatment with activin A and bone morphogenetic protein-4 (BMP4)1 (link). Where indicated, this differentiation protocol was modified by supplementation with ErbB agonists or antagonists. At two weeks following induction of differentiation with activin, cultures were enzymatically dispersed to single cells and re-plated on glass coverslips at low density. Unless otherwise stated, phenotyping studies were performed on days 20–25 post-induction, using cell preparations comprised of ~60% cardiomyocytes (Online Figure I).
For selected experiments, hESC-CM cultures were transduced with a lentiviral vector in which the proximal promoter-enhancer region of the chicken GATA6 (cGATA6) gene drives expression of enhanced green fluorescent protein (EGFP)29 (link), 30 (link). Parallel control experiments indicated ~50% transduction efficiency. Transduced cells were employed in electrophysiological or immunocytochemical studies at 3–4 days post-transduction, which corresponds to 22–25 days post-induction with activin.
Zhu W.Z., Xie Y., Moyes K.W., Gold J.D., Askari B, & Laflamme M.A. (2010). Neuregulin/ErbB Signaling Regulates Cardiac Subtype Specification in Differentiating Human Embryonic Stem Cells. Circulation research, 107(6), 776-786.
Publication 2010
activin A Activins agonists antagonists Bone Morphogenetic Protein 4 Cells Chickens Cloning Vectors Dietary Supplements enhanced green fluorescent protein Genes Genes, erbB Human Embryonic Stem Cells Myocytes, Cardiac Serum

Most recents protocols related to «Activins»

1
Renal Cortical Tissue Protein Analysis

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2023
Activins Antibodies BAMBI protein, human bicinchoninic acid Biological Assay Bone Morphogenetic Proteins Buffers cadherin 5 Densitometry GAPDH protein, human Glyceraldehyde-3-Phosphate Dehydrogenases Horseradish Peroxidase Immunoglobulins Immunoprecipitation Kidney Cortex polyvinylidene fluoride Proteins Saline Solution SDS-PAGE Tissue, Membrane Tissues Tween 20
2
Combination Therapy for Prostate Cancer
Vehicle and enzalutamide (30 mg/kg body weight), SRC inhibitor eCF506 (20 mg/kg body weight) was given via daily oral gavage; L-Clod/PBS (1 mg/mouse, twice a week) were administered by i.v. injection; DT or control Glu52-DT (25 μg/kg body weight, every other day), anti-Ly-6G depleting Abs (200 μg/mouse, every other day), activin-A receptor inhibitor SB-505124 (5 mg/kg body weight, every other day) were delivered by i.p. injection. In some experiments, mice continuously received doxycycline diet (625 mg/kg). Enzalutamide was synthesized by chemical core at Memorial Sloan Kettering Cancer Center; eCF506 was kindly provided by A. Unciti-Broceta; L-Clod/PBS was from Liposoma; anti-Ly-6G Abs (clone #1A8) were from BioxCell; activin-A receptor inhibitor SB-505124 was from Selleckchem; and DT/Glu52-DT was from Sigma-Aldrich.
Li X.F., Selli C., Zhou H.L., Cao J., Wu S., Ma R.Y., Lu Y., Zhang C.B., Xun B., Lam A.D., Pang X.C., Fernando A., Zhang Z., Unciti-Broceta A., Carragher N.O., Ramachandran P., Henderson N.C., Sun L.L., Hu H.Y., Li G.B., Sawyers C, & Qian B.Z. (2023). Macrophages promote anti-androgen resistance in prostate cancer bone disease. The Journal of Experimental Medicine, 220(4), e20221007.
Full text: Click here
Publication 2023
Activins Body Weight Clone Cells Diet Doxycycline enzalutamide Malignant Neoplasms Mice, House SB-505124 Tube Feeding
3
Serum Myostatin Levels in Liver Disease
Within the first 72 h after admission, blood samples were taken at 8.00 a.m. in fasting conditions and were immediately frozen at −20 °C. Serum myostatin levels were determined by quantitative sandwich enzyme immunoassay technique (R&D Systems, Abingdon Science Park, Abingdon, UK). Each serum sample needed a pretreatment with acid hydrolysis and posterior adjustment to PH 7.4 with HEPES buffer to cleave the active peptide (myostatin) of the original propeptide. We have strictly followed the recommendations of the ELISA manufacturer (R&D Systems, Abingdon Science Park, Abingdon, UK). The yellow final complex was measured at 450 nm in a microplate spectrophotometer reader (Spectra MAX-190, Molecular Devices, Sunnyvale, CA 94089, USA). The calibration curve was prepared with authentic myostatin standards. The coefficient of correlation of the standard curve was 0.997. The detection limit of this assay was established at 2.25 pg/mL; the intra and interassay CV were 3.23% and 4.23%, respectively. The antibody used to coat wells of the plate in this ELISA kit is a human specific monoclonal one. This assay recognizes natural and recombinant mature myostatin. No significant cross-reactivity or interference was observed with other peptides as activin RIIA, activin RIIB, decorin, GASP-2, GDF-11, and GDF-15. The molecules listed previously were prepared at 50 ng/mL in calibrator diluent and assayed for cross-reactivity.
Routine laboratory testing was done for all patients and controls. We recorded prothrombin activity, bilirubin, and albumin, and further calculated the Child–Pugh score. Mean corpuscular volume (MCV) and gamma glutamyl transferase (GGT) were considered “markers” of ethanol consumption.
Martín-González C., Pérez-Hernández O., García-Rodríguez A., Abreu-González P., Ortega-Toledo P., Fernández-Rodríguez C.M., Alvisa-Negrín J.C., Martínez-Riera A, & González-Reimers E. (2023). Serum Myostatin among Excessive Drinkers. International Journal of Molecular Sciences, 24(3), 2981.
Full text: Click here
Publication 2023
Acids Activins Albumins Bilirubin BLOOD Buffers Child Cross Reactions Decorin Enzyme-Linked Immunosorbent Assay Enzyme Immunoassay Erythrocyte Volume, Mean Cell Freezing gamma-Glutamyl Transpeptidase GDF8 protein, human GDF11 protein, human Growth Differentiation Factor 15 HEPES Homo sapiens Hydrolysis Immunoglobulins Medical Devices Patients Peptides Prothrombin Serum
4
Stimulation Assays for hiPSC Cultures
Stimulation assays were performed on confluent hiPSC cultures maintained in mTeSR1 medium. HiPSCs were seeded at 1.5 × 105 cells/cm² on Matrigel-coated coverslips in mTeSR1 medium supplemented with Ri. The next day, medium was replaced by fresh mTeSR1 medium. The day after hiPSCs cultures were stimulated for 1 h with BMP4 (R&D, ref. 314-BP, 50 ng/mL) or ACTIVIN A (100 ng/mL), and 6 h with WNT3A (R&D, ref. 5036-WNT, ranging from 5 ng/mL to 50 ng/mL) in mTeSR1 medium. Cells were then fixed and signaling pathways activation was assessed through immunocytochemical analyses. Medium replacement protocols are summarized in Supplementary Table 5.
For experiments of rescue and chemical induction of epithelial integrity, hiPSCs were seeded on Matrigel-coated coverslips at a density of 0.75 × 105 cells/cm² in mTeSR1 medium supplemented with Ri. The next day, medium was replaced by fresh mTeSR1 medium. The day after, medium was replaced for 1 day by mTeSR1 medium supplemented with 5 µM of LPA or 10 µM of Blebbistatin. Finally, confluent cultures were stimulated for 1 h with BMP4 (50 ng/mL) in mTeSR1 medium, and then fixed and analyzed by immunocytochemistry.
For long-term stimulation experiments of BMP and ACTIVIN pathways, hiPSCs were seeded on Matrigel-coated coverslips at a density of  1.1 × 105 cells/cm² in mTeSR1 medium supplemented with Ri. The next day, medium was replaced by fresh mTeSR1 medium. The day after, hiPSCs cultures were stimulated with BMP4 (50 ng/mL) or ACTIVIN A (100 ng/mL) in mTeSR1 medium. hiPSCs cultures were then fixed and analyzed by immunocytochemistry at 0, 2, 6, 9, 12, and 18 h following stimulation.
Legier T., Rattier D., Llewellyn J., Vannier T., Sorre B., Maina F, & Dono R. (2023). Epithelial disruption drives mesendoderm differentiation in human pluripotent stem cells by enabling TGF-β protein sensing. Nature Communications, 14, 349.
Full text: Click here
Publication 2023
activin A Activins Biological Assay blebbistatin BMP4 protein, human Cells Human Induced Pluripotent Stem Cells Immunocytochemistry matrigel Signal Transduction Pathways
5
Activin A ELISA Assay in Lung Cancer
AMs from orthotopic vehicle-control or lung cancer model mice were isolated by FACS and incubated in 96-well plate overnight. Activin A protein levels in cell culture supernatants were determined using the Activin A ELISA kit (#OKBB00124, Aviva Systems Biology, San Diego, CA) according to the manufacturer’s instructions.
Taniguchi S., Matsui T., Kimura K., Funaki S., Miyamoto Y., Uchida Y., Sudo T., Kikuta J., Hara T., Motooka D., Liu Y.C., Okuzaki D., Morii E., Emoto N., Shintani Y, & Ishii M. (2023). In vivo induction of activin A-producing alveolar macrophages supports the progression of lung cell carcinoma. Nature Communications, 14, 143.
Full text: Click here
Publication 2023
activin A Activins Cell Culture Techniques Enzyme-Linked Immunosorbent Assay Lung Cancer Mus Proteins Staphylococcal Protein A

Top products related to «Activins»

1
Activin a by R&D Systems
Sourced in United States, United Kingdom, Germany
Activin A is a secreted dimeric protein that belongs to the transforming growth factor beta (TGF-β) superfamily. It plays a role in a variety of cellular processes, including cell growth, differentiation, and apoptosis.
2
Lipofectamine 2000 by Thermo Fisher Scientific
Sourced in United States, China, Germany, United Kingdom, Canada, Japan, France, Italy, Switzerland, Australia, Spain, Belgium, Denmark, Singapore, India, Netherlands, Sweden, New Zealand, Portugal, Poland, Israel, Lithuania, Hong Kong, Argentina, Ireland, Austria, Czechia, Cameroon, Taiwan, Province of China, Morocco
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.
3
Trizol by Thermo Fisher Scientific
Sourced in United States, Germany, China, Japan, United Kingdom, Canada, France, Italy, Australia, Spain, Switzerland, Belgium, Denmark, Netherlands, India, Ireland, Lithuania, Singapore, Sweden, Norway, Austria, Brazil, Argentina, Hungary, Sao Tome and Principe, New Zealand, Hong Kong, Cameroon, Philippines
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.
4
Rneasy mini kit by Qiagen
Sourced in Germany, United States, United Kingdom, Netherlands, Spain, Japan, Canada, France, China, Australia, Italy, Switzerland, Sweden, Belgium, Denmark, India, Jamaica, Singapore, Poland, Lithuania, Brazil, New Zealand, Austria, Hong Kong, Portugal, Romania, Cameroon, Norway
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.
5
Dmem f12 by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, China, France, Japan, Canada, Australia, Italy, Switzerland, Belgium, New Zealand, Spain, Denmark, Israel, Macao, Ireland, Netherlands, Austria, Hungary, Holy See (Vatican City State), Sweden, Brazil, Argentina, India, Poland, Morocco, Czechia
DMEM/F12 is a cell culture medium developed by Thermo Fisher Scientific. It is a balanced salt solution that provides nutrients and growth factors essential for the cultivation of a variety of cell types, including adherent and suspension cells. The medium is formulated to support the proliferation and maintenance of cells in vitro.
6
Matrigel by BD
Sourced in United States, United Kingdom, Germany, China, Canada, Japan, Italy, France, Belgium, Australia, Uruguay, Switzerland, Israel, India, Spain, Denmark, Morocco, Austria, Brazil, Ireland, Netherlands, Montenegro, Poland
Matrigel is a solubilized basement membrane preparation extracted from the Engelbreth-Holm-Swarm (EHS) mouse sarcoma, a tumor rich in extracellular matrix proteins. It is widely used as a substrate for the in vitro cultivation of cells, particularly those that require a more physiologically relevant microenvironment for growth and differentiation.
7
Sb431542 by Bio-Techne
Sourced in United Kingdom, United States, Canada, China
SB431542 is a potent and selective inhibitor of the transforming growth factor-beta (TGF-β) type I receptor activin receptor-like kinase (ALK) 4, ALK5, and ALK7. It blocks TGF-β signaling by inhibiting the phosphorylation and activation of Smad2 and Smad3.
8
Penicillin streptomycin by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom, China, Canada, France, Japan, Australia, Switzerland, Israel, Italy, Belgium, Austria, Spain, Gabon, Ireland, New Zealand, Sweden, Netherlands, Denmark, Brazil, Macao, India, Singapore, Poland, Argentina, Cameroon, Uruguay, Morocco, Panama, Colombia, Holy See (Vatican City State), Hungary, Norway, Portugal, Mexico, Thailand, Palestine, State of, Finland, Moldova, Republic of, Jamaica, Czechia
Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.
9
Follistatin by R&D Systems
Sourced in United States, Germany
Follistatin is a glycoprotein that binds to and neutralizes the activity of activin, a member of the transforming growth factor-beta (TGF-β) superfamily. It plays a role in the regulation of follicle-stimulating hormone (FSH) secretion and inhibits the differentiation of various cell types.
10
Rhactivina by R&D Systems
Sourced in Germany, United States
RhActivinA is a recombinant human Activin A protein. Activin A is a member of the transforming growth factor beta (TGF-β) superfamily and plays a role in regulating cell growth and differentiation.

More about "Activins"

Activins are a family of potent protein growth and differentiation factors that belong to the transforming growth factor-beta (TGF-β) superfamily.
These dimeric proteins play pivotal roles in a wide range of physiological and pathological processes, including embryonic development, hormone regulation, immune function, and various disease states such as cancer and fibrosis.
Activin A is a specific member of the Activin family and is known to exert its effects by binding to specialized cell-surface receptors and activating intracellular signaling pathways.
This process ultimately leads to the regulation of cell proliferation, differentiation, and apoptosis (programmed cell death).
Researchers investigating Activin-related mechanisms and applications can utilize various tools and techniques to enhance their studies.
For example, Lipofectamine 2000 is a commonly used transfection reagent that can be employed to introduce Activin-encoding plasmids or siRNAs into cell lines.
The TRIzol or RNeasy Mini Kit methods can be employed to isolate high-quality RNA for gene expression analysis, while DMEM/F12 media and Matrigel can provide a suitable environment for cell culture and differentiation experiments.
Additionally, the small-molecule inhibitor SB431542 can be used to specifically block the Activin signaling pathway, allowing researchers to dissect its precise role in various biological processes.
Penicillin and streptomycin antibiotics are often included in cell culture media to prevent microbial contamination, while Follistatin, a natural Activin antagonist, can be used to modulate Activin activity.
By leveraging these tools and techniques, along with the power of data-driven research optimization platforms like PubCompare.ai, scientists can enhance the reproducibility, accuracy, and impact of their Activin-related studies.
PubCompare.ai helps researchers locate high-quality protocols, products, and methods from the scientific literature, preprints, and patents, ensuring that they can make the most of their Activin research endeavors.