ACVR2B Recombinant Protein Cat

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ACVR2B Recombinant Protein Cat. No.: 96-009 ACVR2B Recombinant Protein Specifications SPECIES: Human SOURCE SPECIES: HEK293 cells SEQUENCE: Ser 19 - Thr 137 FUSION TAG: C-His Tag TESTED APPLICATIONS: WB APPLICATIONS: This recombinant protein can be used for WB. For research use only. PREDICTED MOLECULAR 14.5 kDa WEIGHT: Properties PURITY: >97% as determined by SDS-PAGE. PHYSICAL STATE: Lyophilized BUFFER: PBS, pH7.4 Lyophilized Protein should be stored at -20˚C or lower for long term storage. Upon STORAGE CONDITIONS: reconstitution, working aliquots should be stored at -20˚C or -70˚C. Avoid repeated freeze-thaw cycles. September 27, 2021 1 https://www.prosci-inc.com/acvr2b-recombinant-protein-96-009.html Additional Info OFFICIAL SYMBOL: ACVR2B ALTERNATE NAMES: ACVR2B, ACTRIIB, MGC116908 ACCESSION NO.: NP_001097 GENE ID: 93 Background and References Activin receptor type-2B (ACVR2B) is also known as ActR-IIB and MGC116908, ACVR2B is an activin type 2 receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a BACKGROUND: cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases. This gene encodes activin A type IIB receptor, which displays a 3- to 4-fold higher affinity for the ligand than activin A type II receptor. Defects in ACVR2B are the cause of visceral heterotaxy autosomal type 4 (HTX4). REFERENCES: 1) Attisano, L. et al., 1996, Mol. Cell. Biol. 16: 1066-1073. 2) Woodruff, T.K., 1998, Biochem. Pharmacology 55:953. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 27, 2021 2 https://www.prosci-inc.com/acvr2b-recombinant-protein-96-009.html.

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Lack of Tgfbr1 and Acvr1b Synergistically Stimulates Myofibre Hypertrophy And
bioRxiv preprint doi: https://doi.org/10.1101/2021.03.03.433740; this version posted March 6, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Lack of Tgfbr1 and Acvr1b synergistically stimulates myofibre hypertrophy and accelerates muscle regeneration *M.M.G. Hillege1, *A. Shi1,2 ,3, R.C. Galli Caro1, G. Wu4, P. Bertolino5, W.M.H. Hoogaars1,6, R.T. Jaspers1 1. Laboratory for Myology, Department of Human Movement Sciences, Faculty of Behavioural and Movement Sciences, Vrije Universiteit Amsterdam, Amsterdam Movement Sciences, Amsterdam, The Netherlands 2. Department of Oral and Maxillofacial Surgery/Pathology, Amsterdam UMC and Academic Center for Dentistry Amsterdam (ACTA), Vrije Universiteit Amsterdam (VU), Amsterdam Movement Sciences (AMS), Amsterdam, the Netherlands 3. Key Laboratory of Oral Medicine, Guangzhou Institute of Oral Disease, Affiliated Stomatology Hospital of Guangzhou Medical University, Guangzhou Medical University, Guangzhou, China 4. Department of Oral Implantology and Prosthetic Dentistry, Academic Centre for Dentistry Amsterdam (ACTA), University of Amsterdam (UvA) and Vrije Universiteit Amsterdam (VU), The Netherlands 5. Centre de Recherche en Cancérologie de Lyon, UMR INSERM U1052/CNRS 5286, Université de Lyon, Centre Léon Bérard, Lyon, France 6. European Research Institute for the Biology of Ageing (ERIBA), University Medical Center Groningen (UMCG), University of Groningen, Groningen, The Netherlands *Contributed equally to this manuscript **Correspondence: [email protected]; Tel.: +31 (0) 205988463 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.03.03.433740; this version posted March 6, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder.
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