Recombinant human activin A protein (Qk001)

Product: Qk001 Category: Stem cells

Price range: £250.00 through £3,190.00

Recombinant human activin A protein (Qk001) - Image 4

Activin A is a TGF-β family growth factor regulating embryonic development, cell proliferation, differentiation, and immune responses. Activin A is frequently used to maintain pluripotency in induced pluripotent and embryonic stem cell cultures. It is also used in many stem cell differentiation protocols, including endoderm lineage differentiation and further maturation into hepatocyte and pancreatic cells.

Recombinant human activin A protein is a high-purity mature bioactive dimer of 26 kDa. It is animal origin-free (AOF), carrier protein-free, and tag-free to ensure its purity with exceptional lot-to-lot consistency. This protein has been rigorously benchmarked against other commercial sources and extensively validated for highly reproducible stem cell culture. Qkine founder Marko Hyvönen developed the protocol for making high-purity activin A, and this protein is used at the Cambridge Stem Cell Institute.

High purity mature bioactive dimer rigorously benchmarked against other commercial sources.

Qkine activin A is also available as cell therapy grade with extended quality testing and documentation – Qk001-CTG

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Price range: £250.00 through £3,190.00

1000 µg will be dispatched as 2 x 500 µg.

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Summary:

Bioactive mature domain of recombinant human activin A protein, residues 311-426 (Uniprot: P08476)

26 kDa (dimer)
>98%, by SDS-PAGE quantitative densitometry
Expressed in E. coli
Animal origin-free (AOF) and carrier protein-free
Manufactured in our Cambridge, UK laboratories
Lyophilized from acetonitrile, TFA
Resuspend in 10 mM HCl (Reconstitution solution A) at >50 µg/ml, add carrier protein if desired, prepare single-use aliquots and store frozen at -20 °C (short-term) or -80 °C (long-term)

Handling and storage FAQ

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Featured applications:

Induced pluripotent and embryonic stem cell differentiation and maintenance
iPSC-derived mesoderm differentiation
Differentiation of iPSC into endoderm
Chemically defined media for organoid culture

Alternative protein names

Species reactivity

Frequently used together

Related discovery kits

Alternative proteins

Activin A activity was determined using the activin-responsive firefly luciferase reporter assay in transiently transfected HEK293T cells. Cells were treated in triplicate with a serial dilution of activin A. Firefly luciferase activity was measured and normalized. EC50 = 11.9 pM (309.4 pg/ml). Data from Qk001 lot #104276.

Activin A migrates as a single band at 24 kDa in non-reducing (NR) and 13 kDa as a single monomeric species upon reduction (R). No contaminating protein bands are visible. Purified recombinant protein (7 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptothanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250. Data from Qk001 lot #011.

Further quality assays

Mass spectrometry: single species with expected mass
Recovery from stock vial: >95%
Endotoxin: <0.05 EU/μg protein

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MSDS file

We are a company founded and run by scientists to provide a service and support innovation in stem cell biology and regenerative medicine. All our products are exceptionally high purity, with complete characterisation and bioactivity analysis on every lot.

Qkine activin A was as bioactive as activin A protein from an alternative supplier. Activin A activity was determined using the activin-responsive firefly luciferase reporter assay in transiently transfected HEK293T cells. Cells were treated in triplicate with a serial dilution of Qkine activin A (Qk001, green) or alternative activin A (Supplier B, black). Firefly luciferase activity was measured and normalized. Data from Qk001 lot #204536 EC50 = 16 pM, Supplier B EC50 = 12 pM.

Technote | Activin A

Qkine activin A had consistent bioactivity over 3 independently manufactured lots. Activin A activity was determined using the activin-responsive firefly luciferase reporter assay in transiently transfected HEK293T cells. Cells were treated in triplicate with a serial dilution of 3 independent lots of Qkine activin A. Firefly luciferase activity was measured and normalized. Lot #204536 EC50 = 0.26 ng/ml, lot #204545 EC50 = 0.29 ng/ml, lot #204564 EC50 = 0.27 ng/ml.

Technote | Activin A

Protein background

Activin A is a member of the belongs to the transforming growth factor beta (TGF-β) superfamily TGF-β family of growth factors [1–4]. It was first identified for its ability to stimulate the release of follicle-stimulating hormone (FSH) from the pituitary gland. It was later recognized as a multifunctional protein with diverse cellular effects [5, 6]. It plays crucial physiological roles in regulating embryonic development, cell proliferation, and differentiation [6, 7]. It promotes the patterning and differentiation of various organs, including the development of the mesoderm, neural, and reproductive systems. It is also involved in maintaining homeostasis, regulating immune responses, and wound healing [8]. Impaired activin A signaling has been associated with various pathological conditions, including cancer, inflammation, and fibrosis [9, 10]. As activin A can contribute to disease progression and severity, it is a growing area of research for promising therapeutic targets.

Activins are disulfide-linked homo- and heterodimers of four inhibin β chains [6]. The best-characterized are activin A and activin B, homodimers of inhibin βA and inhibin βB, respectively. Like all other members of the TGF-β family, activins are synthesized as significant precursors consisting of an N-terminal signal peptide, a pro-domain of 250–350 residues, and a highly conserved mature domain. The pro-domain, which is cleaved off in the mature protein, has essential roles in the biosynthesis, stabilization, transportation and signaling of the growth factors in the body [11]. Activin A binds to activin type I (ALK4 or ALK7) and type II (ActRIIA or ActRIIB) receptors [6, 12]. The type II receptor phosphorylates the type I receptor upon ligand binding, initiating downstream signaling cascades, mainly through the SMAD family of proteins. Activated SMAD complexes translocate into the nucleus, regulating the transcription of target genes involved in various cellular processes. In vivo, the high-affinity inhibitor follistatin and inhibins tightly regulate activin A activity in a feedback loop [13, 14]. Follistatin is secreted into the media during stem cell culture. However, the impact on the efficiency of stem cell differentiation and cellular homogeneity has not been studied closely (see this discussion for more information).

Activin A is frequently used for the maintenance of pluripotency of human induced pluripotent stem cells and human embryonic stem cell lines along with fibroblast growth factor 2 (FGF-2) [2, 4]. Activin A is also used in various stem cell differentiation protocols. It directs the differentiation into definitive endoderm, precursor to different cell types such as pancreatic and liver cells [15–18]. Activin A also promotes neural precursor cells and drives astrocytic differentiation with Ciliary neurotrophic factor (CNTF) and Glial cell line-derived neurotrophic factor (GDNF) [19]. Moreover, activin A is also involved in mesodermal differentiation to derive muscle, bone, and blood cells. Finally, activin A is often used for the development and maintenance of organoids [18, 20, 21]. Qkine recombinant activin A protein has been extensively validated and benchmarked with other suppliers’ proteins in stem cell culture and assays. You can view the results of this analysis and a commentary by Qkine’s founder, Marko Hyvönen.

Background references

[1] Piek, E., Heldin C. H., and Ten Dijke, P. Specificity, diversity, and regulation in TGF-beta superfamily signaling. FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol. (1999) PMID: 10593858
[2] Pauklin, S. and Vallier, L. Activin/Nodal signalling in stem cells, Development (2015) doi: 10.1242/dev.091769.
[3] Lee, J. J. and Rosenberg, H. F. Eds. Chapter 12 - Eosinophil-Mediated Tissue Remodeling and Fibrosis, in Eosinophils in Health and Disease, Boston: Academic Press (2013) doi: 10.1016/B978-0-12-394385-9.00012-2.
[4] Vallier, L., Alexander, M. and Pedersen, R. A. Activin/Nodal and FGF pathways cooperate to maintain pluripotency of human embryonic stem cells. J. Cell Sci. (2005) doi: 10.1242/jcs.02553.
[5] Carroll, R. S., Kowash, P. M., Lofgren, J. A., Schwall, R. H. and Chin, W. W. In vivo regulation of FSH synthesis by inhibin and activin. Endocrinology (1991) doi: 10.1210/endo-129-6-3299.
[6] Xia, Y. and Schneyer, A. L. The Biology Of Activin: Recent Advances In Structure, Regulation And Function. J. Endocrinol.(2009) doi: 10.1677/JOE-08-0549.
[7] Sulzbacher, S., Schroeder, I. S., Truong, T. T. and Wobus, A. M. Activin A-Induced Differentiation of Embryonic Stem Cells into Endoderm and Pancreatic Progenitors—The Influence of Differentiation Factors and Culture Conditions. Stem Cell Rev. Rep. (2009) doi: 10.1007/s12015-009-9061-5.
[8] Hübner, G., Hu, Q., Smola, H. and Werner, S. Strong Induction of Activin Expression after Injury Suggests an Important Role of Activin in Wound Repair. Dev. Biol. (1996) doi: 10.1006/dbio.1996.0042.
[9] Loomans, H. A. and Andl, C. D. Intertwining of Activin A and TGFβ Signaling: Dual Roles in Cancer Progression and Cancer Cell Invasion. Cancers (2015) doi: 10.3390/cancers7010070.
[10] Jones, K. L., de Kretser, D. M., Patella, S. and Phillips, D. J. Activin A and follistatin in systemic inflammation. Mol. Cell. Endocrinol. (2004) doi: 10.1016/j.mce.2004.07.010.
[11] Wang, X., Fischer, G. and Hyvönen, M. Structure and activation of pro-activin A. Nat. Commun. (2016) doi: 10.1038/ncomms12052.
[12] Mathews, L. S. Activin Receptors and Cellular Signaling by the Receptor Serine Kinase Family. Endocr. Rev. (1994) doi: 10.1210/edrv-15-3-310.
[13] Harrington, A E., Morris-Triggs, S. A., Ruotolo, B. T., Robinson, C. V., Ohnuma, S. and Hyvönen, M. Structural basis for the inhibition of activin signalling by follistatin. EMBO J. (2006) doi: 10.1038/sj.emboj.7601000.
[14] Welt, C., Sidis, Y., Keutmann, H. and Schneyer, A. Activins, inhibins, and follistatins: from endocrinology to signaling. A paradigm for the new millennium’, Exp. Biol. Med. Maywood NJ (2002) doi: 10.1177/153537020222700905.
[15] D’Amour, K. A., Agulnick, A. D., Eliazer, S., Kelly, O. G., Kroon, E. and Baetge, E. E. Efficient differentiation of human embryonic stem cells to definitive endoderm. Nat. Biotechnol.(2005) doi: 10.1038/nbt1163.
[16] Andreasson, L., Evenbratt, H., Mobini, R. and Simonsson, S. Differentiation of induced pluripotent stem cells into definitive endoderm on Activin A-functionalized gradient surfaces. J. Biotechnol. (2021) doi: 10.1016/j.jbiotec.2020.10.030.
[17] Ghorbani-Dalini, S. et al. Optimization of activin-A: a breakthrough in differentiation of human induced pluripotent stem cell into definitive endoderm. Biotech (2020) doi: 10.1007/s13205-020-02215-3.
[18] Qiu, S. et al. An Efficient Method for the Differentiation of Human iPSC-Derived Endoderm toward Enterocytes and Hepatocytes. Cells (2021) doi: 10.3390/cells10040812.
[19] Arber, C. et al. Activin A directs striatal projection neuron differentiation of human pluripotent stem cells. Development (2015) doi: 10.1242/dev.117093.
[20] Miranda, C. C., Fernandes, T. G., Diogo, M. M. and Cabral, J. M. S. Towards Multi-Organoid Systems for Drug Screening Applications. Bioengineering (2018) doi: 10.3390/bioengineering5030049.
[21] Shariati, L., Esmaeili, Y., Haghjooy Javanmard, S., Bidram, E. and Amini, A. Organoid Technology: Current Standing and Future Perspectives. Stem Cells (2021) doi: 10.1002/stem.3379.

Additional resources

Publications using Recombinant human activin A protein (Qk001)

Differentiation of induced pluripotent stem cells into definitive endoderm on Activin A-functionalized gradient surfaces
Andreasson L, Evenbratt H, Mobini R and Simonsson S et al.
DOI: doi: 10.1016/j.jbiotec.2020.10.030
Validation of Current Good Manufacturing Practice Compliant Human Pluripotent Stem Cell-Derived Hepatocytes for Cell-Based Therapy
Blackford SJI et al.
DOI: doi.org/10.1002/sctm.18-0084
Distinct Molecular Trajectories Converge to Induce Naive Pluripotency
Stuart HT et al.
DOI: doi: 10.1016/j.stem.2019.07.009
IGF1-mediated human embryonic stem cell self-renewal recapitulates the embryonic niche
Wamaitha SE, Grybel KJ, Alanis-Lobato G et al.
DOI: doi: 10.1038/s41467-020-14629-x
A transient modified mRNA encoding Myc and Cyclin T1 induces cardiac regeneration and improves cardiac function after myocardial injury
Boikova A, Quaife-Ryan GA, Batho CAP et al.
DOI: https://doi.org/10.1101/2023.08.02.551469
Differentiating functional human islet-like aggregates from pluripotent stem cells
Barsby T, Ibrahim H, Lithovius V et al.
DOI: doi: 10.1016/j.xpro.2022.101711.
Distinct pathways drive anterior hypoblast specification in the implanting human embryo
Weatherbee BAT, Weberling A, Gantner CW et al.
DOI: doi: 10.1038/s41556-024-01367-1
Dysregulated RNA polyadenylation contributes to metabolic impairment in non-alcoholic fatty liver disease
Jobbins AM, Haberman N, Artigas N et al.
DOI: doi: 10.1093/nar/gkac165
Esrrb guides naive pluripotent cells through the formative transcriptional programme
Carbognin E, Carlini V, Panariello F et al.
DOI: doi: 10.1038/s41556-023-01131-x
Exploring the link between dioxin exposure and diabetes risk: contributions of the islet aryl hydrocarbon receptor
Gang N
DOI: Thesis
Extracellular matrices modulate differentiation of human embryonic stem cell-derived hepatocyte-like cells with spatial hepatic features
Farhan F, Trivedi M, Di Wu P et al.
DOI: doi: 10.1186/s13287-023-03542-x
Feeder-free culture of naive human pluripotent stem cells retaining embryonic, extraembryonic and blastoid generation potential
Rossignoli G, Oberhuemer M, Brun IS et al.
DOI: https://doi.org/10.1101/2025.01.17.633522
Generation of human iPSC-derived pancreatic organoids to study pancreas development and disease
Darrigrand J-F, Isaacson A and Spagnoli FM
DOI: doi: 10.12688/f1000research
Genetic and functional correction of argininosuccinate lyase deficiency using CRISPR adenine base editors
Jalil S, Keskinen T, Juutila J et al.
DOI: doi: 10.1016/j.ajhg.2024.03.004
Hydrostatic pressure promotes chondrogenic differentiation and microvesicle release from human embryonic and bone marrow stem cells
Luo L, Foster NC, Man KL et al.
DOI: doi: 10.1002/biot.202100401
Pancreas agenesis mutations distrupt a lead enhancer controlling a developmental enhancer cluster
Miguel-Escalada I, Maestro MÁ, Balboa D et al.
DOI: doi: 10.1016/j.devcel.2022.07.014
Pluripotent stem cell-derived model of the post-implantation human embryo
Weatherbee BAT, Gantner CW, Iwamoto-Stohl LK et al.
DOI: doi: 10.1038/s41586-023-06368-y
Protocol for generating a 3D culture of epiblast stem cells
Rosa VS, Sato N and Shahbazi MN et al.
DOI: doi: 10.1016/j.xpro.2024.103347
RBL2-E2F-GCN5 guide cell fate decisions during tissue specification by regulating cell-cycle-dependent fluctuations of non-cell-autonomous signaling
Militi S, Nibhani R, Jalali M and Pauklin S.
DOI: doi: 10.1016/j.celrep.2023.113146
Refined and benchmarked homemade media for cost-effective, weekend-free human pluripotent stem cell culture
Truszkowski L, Bottini S, Bianchi S et al.
DOI: doi.org/10.12688/openreseurope.18245.2
Role of mechanotransduction in pancreatic endocrine cell fate acquisition in SC-islets
Farbergshagen, AC (Thesis)
DOI: Thesis
Self-renewing human naïve pluripotent stem cells dedifferentiate in 3D culture and form blastoids spontaneously
Guo M, Wu J, Chen C et al.
DOI: doi: 10.1038/s41467-024-44969-x
Single Cell Transcriptional Perturbome in Pluripotent Stem Cell Models
Balmas E, Ratto ML, Snijders KE et al.
DOI: http://dx.doi.org/10.2139/ssrn.4854180
STAT3 signalling enhances tissue expansion during postimplantation mouse development
Azami T, Theeuwes B, Ton M-LN et al.
DOI: doi: 10.1016/j.celrep.2025.115506
Stem cell-derived porcine macrophages as a new platform for studying host-pathogen interactions
Meek S, Watson T, Eory L et al.
DOI: doi: 10.1186/s12915-021-01217-8
Stem cell-derived synthetic embryos self-assemble by exploiting cadherin codes and cortical tension
Bao M, Cornwall-Scoones J, Sanchez-Vasquez E et al.
DOI: doi: 10.1038/s41556-023-01157-1
The HASTER lncRNA promoter is a cis-acting transcriptional stabilizer of HNF1A
Beucher A, Miguel-Escalada I, Balboa D et al.
DOI: doi: 10.1038/s41556-022-00996-8
The transcriptional regulator ZNF398 mediates pluripotency and epithelial character downstream of TGF-beta in human PSCs
Zorzan I, Pellegrini M, Arboit M et al.
DOI: doi: 10.1038/s41467-020-16205-9
Modelling Cholestasis in vitro Using Hepatocytes Derived from Human Induced Pluripotent Stem Cells
Garitta E
DOI: https://qmro.qmul.ac.uk/xmlui/handle/123456789/105833
HNF1A and A1CF coordinate a beta cell transcription-splicing axis that is disrupted in type 2 diabetes
Bernardo, Edgar et al.
DOI: 10.1016/j.cmet.2025.07.007
Signaling reprogramming via Stat3 activation unravels high-fidelity human post-implantation embryo modeling
Chen C, Wu J, Wang X et al.
DOI: DOI: 10.1016/j.stem.2025.08.011
Opposing CTCF and GATA4 activities set the pace of chromatin topology remodeling during cardiomyogenesis
Becca S, Bianchi S, Hahn EM et al.
DOI: doi.org/10.1101/2025.10.07.680441
Simplified In Vitro Generation of Human Gastruloids for Modelling Early Development
Azami T, Patton EE and Nichols J.
DOI: doi.org/10.1101/2025.10.15.682610
Expanding the apelin receptor pharmacological toolbox using novel fluorescent ligands
Williams TL, Macrae RGC, Kuc RE, Brown AJH, Maguire JJ, Davenport AP.
DOI: doi: 10.3389/fendo.2023.1139121
Genetic Correction of the Most Common Mutation Causing Primary Hyperoxaluria Restores Enzyme Localization and Oxalate Metabolism
Keskinen T, Jalil S, Gümüşoğlu I et al.
DOI: doi: 10.1002/jimd.70122
Age-Driven Lipid Remodeling Activates Lysosome-Mediated Plasma Membrane Repair
Skowronska-Krawczyk et al.
DOI: doi.org/10.21203/rs.3.rs-8607320/v1
Gene Expression at the Pluripotency Stage Predicts Pancreatic Endocrine Differentiation in iPSC Clones
Zamarian V, Monaco L, Marras M et al.
DOI: doi.org/10.1007/s12015-026-11091-y
Animal proteins from stem cells as an alternative to reduce the ecological and climate impact of animal farming
Bottini S (Thesis)
DOI: Thesis
Serum coating enables feeder-free culture of naive human pluripotent stem cells preserving developmental potential
Rossignoli G, Oberhuemer M, Brun IS et al.
DOI: https://doi.org/10.1038/s44318-026-00714-2
Intramuscular Transplantation of Human Pluripotent Stem Cell-derived Pancreatic Endocrine Cells in Mice
Hernanz M, Matas D, Mirasierra M et al.
DOI: DOI: 10.3791/69562

FAQ

What is the function of the activin A protein?

Activin A is a multifunctional protein. It is involved in regulating embryonic development, cell proliferation, and differentiation. It promotes the patterning and differentiation of various organs, including the development of the mesoderm, neural, and reproductive systems. It is also involved in maintaining homeostasis, regulating immune responses, and wound healing. Finally, it stimulates the release of follicle-stimulating hormone from the pituitary gland.

What does activin A do in cell culture?

Activin A is a critical factor in stem cell culture, commonly used to maintain the pluripotency of induced pluripotent stem cells (iPSCs) and embryonic stem cells (ESCs). It is integral to various stem cell differentiation protocols, guiding the differentiation of the definitive endoderm, neural and mesodermal lineages. Activin A is also commonly utilized in the development and maintenance of organoids.

What are activin A and inhibin A?

Activin A and inhibin A are closely related proteins in the TGF-β superfamily. They share structural similarities but have distinct functions and roles in regulating various physiological processes. Activin A has broader functions beyond reproduction, which include handling embryonic development, stem cell maintenance, and the immune system. Inhibin A, conversely, is more specifically associated with the feedback control of follicle-stimulating hormones in the context of reproductive physiology.

What does activin A bind to?

Activin A binds to activin type I (ALK4 or ALK7) and type II (ActRIIA or ActRIIB) receptors to activate downstream SMAD signalling.

Does activin increase LH?

Yes, activin is involved in a feedback loop that regulates the secretion of follicle-stimulating hormone (FSH) and luteinising hormone (LH).

What does the activin gene do?

The activin gene family includes several genes that encode different activin subunits, forming various activin isoforms such as Inhibin Beta Subunits (INHBA / INHBB / INHBC / INHBD).

What inhibits activin A?

Follistatin and inhibins tightly regulate activin A activity in a feedback loop.

Special guidance for reconstitution of TGF beta family including activins, BMPs and GDF-15

TGF beta family proteins and other growth factors can be very poorly soluble in physiological solutions. Please follow the handling guidance for lyophilized cytokines below to minimize loss of protein due to precipitation or adsorption to plastic. We advise storing the recombinant protein at very low pH before dilution in cell culture media or final working solutions. Low pH will also assist in maintaining the correct disulfide structure of the protein by minimizing disulfide bond exchange reactions.

Resuspension in physiological buffers may cause precipitation of stock solutions, hence we recommend dissolving our lyophilized cytokines in 10 mM HCl (1:1000 dilution of concentrated HCl) while keeping the protein concentration at 50 µg/ml or above, in order to avoid loss by adsorption to plasticware.
To ensure you recover all of the protein, let the sample sit for a few minutes with the solubilization buffer at room temperature and pipette gently up and down (avoid foaming).
Rinse the tube with some more 10 mM HCl and pool with the rest.
The protein is tolerant of some freeze and thaw cycles, but as always with proteins, it is better to aliquot and store frozen.
Our proteins are supplied carrier-protein free. If compatible with your work, add carrier protein of your choice such as BSA, HSA or gelatin to further minimize loss by adsorption.
Store in -80°C for long term storage. -20°C for short-term.

Every effort is made to ensure samples are sterile; however, we recommend sterile filtering after dilution in media or the final working solution.

Our products are for research use only and not for diagnostic or therapeutic use. Products are not for resale.

For use in manufacturing of cellular or gene therapy products. Not intended for in vivo applications.

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Recombinant human activin A protein (Qk001)

Summary:

Featured applications:

Further quality assays

Protein background

Additional resources

Publications using Recombinant human activin A protein (Qk001)

Differentiation of induced pluripotent stem cells into definitive endoderm on Activin A-functionalized gradient surfaces

Validation of Current Good Manufacturing Practice Compliant Human Pluripotent Stem Cell-Derived Hepatocytes for Cell-Based Therapy

Distinct Molecular Trajectories Converge to Induce Naive Pluripotency

IGF1-mediated human embryonic stem cell self-renewal recapitulates the embryonic niche

A transient modified mRNA encoding Myc and Cyclin T1 induces cardiac regeneration and improves cardiac function after myocardial injury

Differentiating functional human islet-like aggregates from pluripotent stem cells

Distinct pathways drive anterior hypoblast specification in the implanting human embryo

Dysregulated RNA polyadenylation contributes to metabolic impairment in non-alcoholic fatty liver disease

Esrrb guides naive pluripotent cells through the formative transcriptional programme

Exploring the link between dioxin exposure and diabetes risk: contributions of the islet aryl hydrocarbon receptor

Extracellular matrices modulate differentiation of human embryonic stem cell-derived hepatocyte-like cells with spatial hepatic features

Feeder-free culture of naive human pluripotent stem cells retaining embryonic, extraembryonic and blastoid generation potential

Generation of human iPSC-derived pancreatic organoids to study pancreas development and disease

Genetic and functional correction of argininosuccinate lyase deficiency using CRISPR adenine base editors

Hydrostatic pressure promotes chondrogenic differentiation and microvesicle release from human embryonic and bone marrow stem cells

Pancreas agenesis mutations distrupt a lead enhancer controlling a developmental enhancer cluster

Pluripotent stem cell-derived model of the post-implantation human embryo

Protocol for generating a 3D culture of epiblast stem cells

RBL2-E2F-GCN5 guide cell fate decisions during tissue specification by regulating cell-cycle-dependent fluctuations of non-cell-autonomous signaling

Refined and benchmarked homemade media for cost-effective, weekend-free human pluripotent stem cell culture

Role of mechanotransduction in pancreatic endocrine cell fate acquisition in SC-islets

Self-renewing human naïve pluripotent stem cells dedifferentiate in 3D culture and form blastoids spontaneously

Single Cell Transcriptional Perturbome in Pluripotent Stem Cell Models

STAT3 signalling enhances tissue expansion during postimplantation mouse development

Stem cell-derived porcine macrophages as a new platform for studying host-pathogen interactions

Stem cell-derived synthetic embryos self-assemble by exploiting cadherin codes and cortical tension

The HASTER lncRNA promoter is a cis-acting transcriptional stabilizer of HNF1A

The transcriptional regulator ZNF398 mediates pluripotency and epithelial character downstream of TGF-beta in human PSCs

Modelling Cholestasis in vitro Using Hepatocytes Derived from Human Induced Pluripotent Stem Cells

HNF1A and A1CF coordinate a beta cell transcription-splicing axis that is disrupted in type 2 diabetes

Signaling reprogramming via Stat3 activation unravels high-fidelity human post-implantation embryo modeling

Opposing CTCF and GATA4 activities set the pace of chromatin topology remodeling during cardiomyogenesis

Simplified In Vitro Generation of Human Gastruloids for Modelling Early Development

Expanding the apelin receptor pharmacological toolbox using novel fluorescent ligands

Genetic Correction of the Most Common Mutation Causing Primary Hyperoxaluria Restores Enzyme Localization and Oxalate Metabolism

Age-Driven Lipid Remodeling Activates Lysosome-Mediated Plasma Membrane Repair

Gene Expression at the Pluripotency Stage Predicts Pancreatic Endocrine Differentiation in iPSC Clones

Animal proteins from stem cells as an alternative to reduce the ecological and climate impact of animal farming

Serum coating enables feeder-free culture of naive human pluripotent stem cells preserving developmental potential

Intramuscular Transplantation of Human Pluripotent Stem Cell-derived Pancreatic Endocrine Cells in Mice

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