{"id":70729,"date":"2026-05-12T10:06:21","date_gmt":"2026-05-12T10:06:21","guid":{"rendered":"https:\/\/medsbase.com\/?post_type=product&#038;p=70729"},"modified":"2026-05-21T07:14:10","modified_gmt":"2026-05-21T07:14:10","slug":"gdf-8","status":"publish","type":"product","link":"https:\/\/medsbase.com\/nl\/gdf-8\/","title":{"rendered":"GDF-8 (Myostatine)"},"content":{"rendered":"<p><!-- medsbase-tldr-answer --><\/p>\n<div style=\"background: #fff8e1; border-left: 4px solid #f5a623; padding: 18px 22px; margin: 18px 0; border-radius: 4px;\">\n<h3 style=\"margin: 0 0 8px 0; font-size: 16px; color: #1a4a6b;\">Quick Answer \u2014 What is GDF-8 (Myostatin)?<\/h3>\n<p style=\"margin: 0;\"><strong>GDF-8<\/strong> (Growth\/Differentiation Factor 8), also called <strong>myostatin<\/strong>, is a recombinant TGF-\u03b2 superfamily protein and the principal endogenous negative regulator of skeletal muscle mass. Loss-of-function mutations cause the well-known &#8220;double-muscling&#8221; phenotype in mice, cattle, dogs, and one documented human case. In published research, recombinant GDF-8 is used as a pathway-stimulus tool: inducing atrophy phenotypes, validating myostatin antagonists such as <a href=\"https:\/\/medsbase.com\/nl\/follistatin-344\/\">follistatin 344<\/a>, and characterising Smad2\/Smad3 downstream signalling. Supplied in 1\u00a0mg lyophilized vials for laboratory research use only.<\/p>\n<\/div>\n<div class=\"medsbase-trust-strip\" style=\"background: #f4f8fb; border: 1px solid #d8e3eb; padding: 12px 16px; margin: 16px 0; border-radius: 4px; font-size: 14px;\"><strong>Wat u krijgt bij MedsBase:<\/strong> Research-grade lyophilized recombinant protein \u00b7 HPLC \u226595% purity (COA on request) \u00b7 Discreet temperature-stable packaging \u00b7 Worldwide peptide courier \u00b7 1,400+ verified <a href=\"https:\/\/medsbase.com\/nl\/reviews\/\">klantbeoordelingen<\/a><\/div>\n<p class=\"medsbase-reship-line\" style=\"font-size: 14px; color: #444; margin: 8px 0 18px;\">\ud83d\udce6 Elke bestelling is gedekt door onze <a href=\"https:\/\/medsbase.com\/nl\/medsbase-re-shipment-assurance-policy\/\"><strong>Reshipment Assurance Policy<\/strong><\/a> \u2014 als uw pakket niet binnen 20 werkdagen arriveert, sturen wij het opnieuw.<\/p>\n<table class=\"medsbase-spec-table\" style=\"width: 100%; border-collapse: collapse; margin: 18px 0; font-size: 14px;\">\n<thead>\n<tr style=\"background: #2c7cb0; color: #fff;\">\n<th style=\"padding: 8px 12px; text-align: left; width: 30%;\">Specificatie<\/th>\n<th style=\"padding: 8px 12px; text-align: left;\">Detail<\/th>\n<\/tr>\n<\/thead>\n<tbody>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>CAS-nummer<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Not formally registered for the mature dimer (recombinant protein). Encoded by the MSTN gene; UniProt O14793<\/td>\n<\/tr>\n<tr style=\"background: #fff;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Type<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Recombinant protein (TGF-\u03b2 superfamily ligand; mature 109-amino-acid C-terminal disulfide-linked homodimer cleaved from a 375-aa preproprotein precursor)<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Moleculair gewicht<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">~25.8\u00a0kDa (mature homodimer; ~12.9\u00a0kDa per monomer chain)<\/td>\n<\/tr>\n<tr style=\"background: #fff;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Structure<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Mature 109-aa monomer with the canonical TGF-\u03b2 superfamily cystine-knot fold; two monomers covalently linked by an intermolecular disulfide bond to form the biologically active homodimer; receptor-binding surfaces engage ActRIIB<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Form<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Lyophilized recombinant protein (white to off-white)<\/td>\n<\/tr>\n<tr style=\"background: #fff;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Zuiverheid<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">\u226595% (HPLC verified, COA on request)<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Opslag<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Lyophilized: 2\u20138\u00a0\u00b0C (refrigerator) for working stock; \u221220\u00a0\u00b0C for long-term storage of unopened vials. Reconstituted: 2\u20138\u00a0\u00b0C, use within ~30 days. Protect from light. Do not freeze\u2013thaw the reconstituted solution \u2014 recombinant proteins are particularly sensitive to freeze-thaw denaturation.<\/td>\n<\/tr>\n<tr style=\"background: #fff;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Oplosbaarheid<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Bacteriostatic water (recommended) or sterile water for shorter use windows. Carrier protein (BSA, 0.1%) optional for working dilutions to minimise adsorption losses.<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0; width: 30%;\"><strong>Onderzoeksgebruik<\/strong><\/td>\n<td style=\"padding: 8px 12px; border-bottom: 1px solid #e0e0e0;\">Alleen voor laboratoriumonderzoek. Niet voor humaan of veterinair diagnostisch of therapeutisch gebruik.<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<p><!-- \/medsbase-tldr-answer --><\/p>\n<h2>What Is GDF-8 (Myostatin)?<\/h2>\n<p><strong>GDF-8<\/strong> (Growth\/Differentiation Factor 8), commonly known as <strong>myostatin<\/strong>, is a member of the transforming growth factor beta (TGF-\u03b2) superfamily and the principal physiological negative regulator of skeletal muscle mass. It was first characterised by McPherron, Lawler, and Lee (Nature 1997) as a secreted protein whose targeted disruption in mice produced animals with two- to three-fold greater skeletal muscle mass than wild-type controls. The same gene was rapidly identified as the cause of the &#8220;double-muscling&#8221; phenotype in Belgian Blue and Piedmontese cattle, the Bully Whippet phenotype in racing greyhounds, and one documented human case of striking infant hypermuscularity (Schuelke et al., NEJM 2004) \u2014 all carrying loss-of-function MSTN mutations.<\/p>\n<p>Mature myostatin is generated by post-translational processing of a 375-amino-acid preproprotein: the signal peptide is removed during secretion, then the prodomain (~243 aa) is cleaved off by furin proteases, releasing the active 109-amino-acid C-terminal mature myostatin. The active form is a homodimer of two mature monomer chains covalently linked by an intermolecular disulfide bond, with apparent mass approximately 25.8\u00a0kDa on non-reducing SDS-PAGE. The protein adopts the canonical TGF-\u03b2 cystine-knot fold and binds the activin type IIB receptor (ActRIIB) with high affinity to initiate Smad-mediated signalling. Recombinant GDF-8 is supplied as a high-purity lyophilized powder for reconstitution with bacteriostatic water. Myostatin is <strong>niet goedgekeurd<\/strong> by the FDA, EMA, MHRA, or any other major regulator for human therapeutic use. The research-grade GDF-8 sold here is supplied <strong>uitsluitend voor laboratoriumonderzoek<\/strong> and is not intended for human or veterinary administration.<\/p>\n<h2>Mechanism of Action \u2014 ActRIIB Signalling and the Smad2\/Smad3 Axis<\/h2>\n<p>What makes GDF-8 mechanistically distinctive among TGF-\u03b2 superfamily ligands is its <strong>dominant role as a tonic brake on muscle growth<\/strong> through a well-characterised three-step signalling cascade documented in published research:<\/p>\n<ul>\n<li><strong>ActRIIB receptor binding and type I receptor recruitment<\/strong> \u2014 Mature myostatin homodimer binds activin type IIB receptor (ActRIIB) on the surface of skeletal muscle fibres and other cell types. ActRIIB is a constitutively-active serine\/threonine kinase that, once myostatin-bound, recruits and trans-phosphorylates the type I receptors ALK4 (ActRIB) and ALK5 (T\u03b2RI). The ligand-receptor stoichiometry is a 2:2:2 heterotetramer in the active complex. ActRIIB knockout produces a phenotype similar to myostatin knockout, confirming the receptor identity.<\/li>\n<li><strong>Smad2\/Smad3 phosphorylation and nuclear translocation<\/strong> \u2014 The phosphorylated ALK4\/ALK5 type I receptors phosphorylate the receptor-regulated Smads \u2014 specifically Smad2 and Smad3 in the myostatin pathway. Phospho-Smad2\/Smad3 form a heteromeric complex with Smad4 (common Smad) and translocate to the nucleus, where they bind Smad-binding elements in target-gene promoters and recruit transcriptional cofactors. The Smad pathway is the dominant signalling output for myostatin in skeletal muscle.<\/li>\n<li><strong>Downstream transcriptional effects \u2014 atrogin-1\/MuRF1 upregulation and protein synthesis suppression<\/strong> \u2014 The nuclear Smad complex coordinates a transcriptional programme that promotes muscle atrophy through three converging mechanisms: induction of the ubiquitin-ligase atrogenes (atrogin-1 \/ Fbxo32 and MuRF1 \/ Trim63) to accelerate protein degradation; inhibition of Akt\/mTOR-mediated protein synthesis through cross-talk with the IGF\/insulin axis; and suppression of myogenic regulatory factors (MyoD, myogenin) to slow satellite-cell-driven repair. The net effect is reduced muscle protein accretion and, at high doses or chronic exposure, frank atrophy.<\/li>\n<\/ul>\n<p>Importantly for research design, GDF-8 acts as a tonic inhibitor under physiological conditions \u2014 muscle mass is regulated by the balance between myostatin tone (atrophic) and IGF\/Akt\/mTOR signalling (anabolic). This is why <a href=\"https:\/\/medsbase.com\/nl\/follistatin-344\/\">Follistatin 344<\/a> (a myostatin\/activin antagonist) and recombinant GDF-8 (the agonist itself) are both used in muscle research \u2014 the antagonist removes the brake, while the recombinant ligand is the experimental tool that quantifies how strong the brake is and validates antagonist activity in receptor-binding and reporter-cell assays.<\/p>\n<h2>Gepubliceerde onderzoeksapplicaties<\/h2>\n<p>Recombinant GDF-8 is used in laboratory research contexts that investigate:<\/p>\n<ul>\n<li><strong>Muscle atrophy and wasting research<\/strong> \u2014 in-vitro myotube atrophy assays, ex-vivo muscle preparations, in-vivo administration to induce reproducible atrophy phenotypes for studying intervention strategies (McPherron et al., Nature 1997; Lee, Annu Rev Cell Dev Biol 2004)<\/li>\n<li><strong>Myostatin antagonist validation<\/strong> \u2014 binding-affinity assays, neutralising-antibody potency assays, receptor-occupancy assays for drug discovery programmes targeting the myostatin pathway; canonical research tool for validating <a href=\"https:\/\/medsbase.com\/nl\/follistatin-344\/\">follistatin 344<\/a>, soluble ActRIIB-Fc fusion proteins, and anti-myostatin antibodies<\/li>\n<li><strong>Smad2\/Smad3 signalling pathway research<\/strong> \u2014 Smad phosphorylation kinetics, nuclear translocation imaging, Smad-binding-element reporter assays, cross-talk with other TGF-\u03b2 pathway members<\/li>\n<li><strong>Atrogene transcription research<\/strong> \u2014 atrogin-1 (Fbxo32) and MuRF1 (Trim63) promoter analysis, ubiquitin-proteasome activity, autophagy-axis cross-talk<\/li>\n<li><strong>Cachexia and sarcopenia models<\/strong> \u2014 tumour-bearing rodent cachexia models, aged-mouse sarcopenia, denervation-induced atrophy \u2014 recombinant GDF-8 used to amplify or recapitulate the wasting phenotype<\/li>\n<li><strong>Cardiac and other tissue research<\/strong> \u2014 myostatin is expressed at lower levels in heart, adipose, and other tissues; published research investigates GDF-8 effects in cardiomyocyte hypertrophy models and adipose-tissue biology<\/li>\n<li><strong>Comparative TGF-\u03b2 superfamily research<\/strong> \u2014 benchmarking against the closely-related GDF-11 (90% sequence identity in mature domain) and activin A (binds the same receptor system); mechanistic dissection of receptor selectivity<\/li>\n<li><strong>Inverse-pharmacology pairing with Follistatin 344<\/strong> \u2014 co-administration with <a href=\"https:\/\/medsbase.com\/nl\/follistatin-344\/\">Follistatin 344<\/a> as the antagonist arm allows direct quantification of myostatin\/antagonist binding stoichiometry and rescue of GDF-8-induced atrophy in research models.<\/li>\n<\/ul>\n<p>For broader context on where GDF-8 fits within the anabolic \/ muscle-research landscape, see <a href=\"https:\/\/medsbase.com\/nl\/follistatin-344\/\">Follistatin 344<\/a> as the canonical myostatin antagonist, <a href=\"https:\/\/medsbase.com\/nl\/igf-1-lr3\/\">IGF-1 LR3<\/a> for the opposite-pathway anabolic arm (direct IGF-1R agonism), and <a href=\"https:\/\/medsbase.com\/nl\/tb-500\/\">TB-500<\/a> for systemic muscle and tissue recovery research. Browse the full <a href=\"https:\/\/medsbase.com\/nl\/peptides\/\">onderzoekspeptiden catalogus<\/a> voor gerelateerde verbindingen.<\/p>\n<h2>Beschikbare sterktes en concentraties<\/h2>\n<p>MedsBase stocks recombinant GDF-8 (Myostatin) in 1\u00a0mg lyophilized vials. The vial is available in 10-vial or 20-vial pack formats with full reconstitution guidance:<\/p>\n<table style=\"width: 100%; border-collapse: collapse; margin: 16px 0;\">\n<thead>\n<tr style=\"background: #2c7cb0; color: #fff;\">\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">Vulsterkte<\/th>\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">Typisch Onderzoeksgebruik<\/th>\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">Verpakkingsgroottes<\/th>\n<\/tr>\n<\/thead>\n<tbody>\n<tr>\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>1\u00a0mg<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Standard research strength \u2014 binding assays, atrophy-induction protocols, antagonist validation<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">10 of 20 flesjes<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<p>GDF-8 is a ~25.8\u00a0kDa recombinant homodimeric protein supplied at \u226595% HPLC purity. The 1\u00a0mg vial format covers the typical research dose range: nanomolar working concentrations for in-vitro binding and reporter-cell assays consume small fractions of a vial; in-vivo administration in rodent models uses microgram-per-injection doses that consume more vial per protocol.<\/p>\n<h2>How It Compares \u2014 GDF-8 (Myostatin) vs Follistatin 344<\/h2>\n<p>Recombinant GDF-8 and <a href=\"https:\/\/medsbase.com\/nl\/follistatin-344\/\">Follistatin 344<\/a> are an inverse-pharmacology pair: GDF-8 is the ligand and Follistatin 344 is the high-affinity binding protein that sequesters it. They are routinely paired in research because the antagonist&#8217;s function can only be quantified against the ligand. The relationship parallels other well-known inverse pairs in pharmacology (e.g., agonist + antagonist of the same receptor) but at the ligand-binding-protein level rather than the receptor level.<\/p>\n<table style=\"width: 100%; border-collapse: collapse; margin: 16px 0;\">\n<thead>\n<tr style=\"background: #2c7cb0; color: #fff;\">\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">Criterium<\/th>\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">GDF-8 (Myostatine)<\/th>\n<th style=\"padding: 10px; border: 1px solid #ddd; text-align: left;\">Follistatin 344<\/th>\n<\/tr>\n<\/thead>\n<tbody>\n<tr>\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Role in muscle biology<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Atrophic ligand (the brake)<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Antagonist binding protein (brake remover)<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Active form<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">109-aa homodimer (~25.8 kDa)<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">344-aa glycoprotein monomer (~37 kDa)<\/td>\n<\/tr>\n<tr>\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Receptor or target<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">ActRIIB (activin type IIB receptor)<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Sequesters myostatin \/ activin (no receptor; direct ligand binding)<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Downstream signalling<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Activates Smad2\/Smad3, atrogenes<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Blocks Smad activation by removing ligand<\/td>\n<\/tr>\n<tr>\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Primary research role<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Tool to induce \/ probe atrophy phenotype<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Tool to reverse \/ prevent atrophy<\/td>\n<\/tr>\n<tr style=\"background: #f9f9f9;\">\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Typische onderzoeksdosis<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">10\u2013100\u00a0ng\/mL in vitro; 0.1\u201310\u00a0mcg in vivo<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">10\u2013100\u00a0mcg in vivo per dose<\/td>\n<\/tr>\n<tr>\n<td style=\"padding: 10px; border: 1px solid #ddd;\"><strong>Pairing<\/strong><\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Co-used with follistatin 344 for binding stoichiometry<\/td>\n<td style=\"padding: 10px; border: 1px solid #ddd;\">Co-used with GDF-8 to validate antagonist activity<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<p>For muscle-research design, the pair is used together in three principal ways: (1) binding-affinity measurement (surface plasmon resonance, ELISA, isothermal titration calorimetry) of follistatin\u2013myostatin interaction; (2) cell-based atrophy\/rescue assays where GDF-8 induces myotube atrophy and follistatin co-treatment is tested for rescue; and (3) in-vivo validation where GDF-8 amplifies a wasting phenotype that follistatin co-administration attenuates. The two proteins are mechanistically complementary and rarely studied in isolation.<\/p>\n<h2>Opslag en Reconstituering<\/h2>\n<p><strong>Voor reconstituering:<\/strong> store lyophilized vials refrigerated at 2\u20138\u00a0\u00b0C in original packaging for short-term working stock. For unopened long-term storage, freeze at \u221220\u00a0\u00b0C. Lyophilized GDF-8 is stable under refrigeration for up to 12 months and at \u221220\u00a0\u00b0C for up to 24 months \u2014 somewhat shorter than small synthetic peptides because the larger recombinant disulfide-linked dimer is more susceptible to misfolding and aggregation over time. Avoid freeze-thaw cycles on the lyophilized powder.<\/p>\n<p><strong>Reconstitueringsprocedure:<\/strong> inject bacteriostatic water down the side wall of the vial (not directly onto the lyophilized cake). For a 1\u00a0mg vial, 1.0\u00a0mL of bacteriostatic water yields a 1\u00a0mg\/mL working concentration. Swirl gently \u2014 do <strong>niet<\/strong> shake \u2014 and allow 5\u201310 minutes for full dissolution. Recombinant proteins dissolve more slowly than small peptides; vigorous agitation can disrupt the intermolecular disulfide and degrade activity. A correctly reconstituted solution should be clear and colourless with no visible particles. For working dilutions below 100\u00a0mcg\/mL, the addition of carrier protein (BSA at 0.1% final concentration) minimises adsorption losses to plastic and glass surfaces.<\/p>\n<p><strong>Na reconstitutie:<\/strong> store refrigerated at 2\u20138\u00a0\u00b0C and use within 30 days for optimal stability. Do not freeze the reconstituted solution \u2014 recombinant dimeric proteins are particularly sensitive to freeze-thaw denaturation, which produces aggregation and loss of receptor-binding activity. Discard any vial showing cloudiness, precipitate, or discolouration. For binding-affinity assays requiring tight dose-response calibration, use freshly-reconstituted solution within 7 days for the most reproducible results.<\/p>\n<h2 id=\"faqs\">Veelgestelde vragen<\/h2>\n<h3>What is GDF-8 (Myostatin) used for in research?<\/h3>\n<p>Recombinant GDF-8 is used in laboratory research as the canonical agonist of the myostatin pathway \u2014 it is the experimental tool for inducing reproducible muscle atrophy phenotypes, characterising Smad2\/Smad3 signalling, validating myostatin antagonists (including <a href=\"https:\/\/medsbase.com\/nl\/follistatin-344\/\">Follistatin 344<\/a> and ActRIIB-Fc fusion proteins), and quantifying binding stoichiometry in pharmacology assays. It is not used to &#8220;improve&#8221; anything in research models \u2014 it is the negative regulator that researchers want to understand and ultimately inhibit. The research-grade GDF-8 sold here is <strong>niet<\/strong> FDA-goedgekeurd en wordt strikt geleverd voor laboratoriumonderzoek alleen.<\/p>\n<h3>How is GDF-8 different from Follistatin 344?<\/h3>\n<p>The two are an inverse-pharmacology pair. GDF-8 is the active myostatin ligand \u2014 the brake on muscle growth that drives atrophy via Smad2\/Smad3 signalling. Follistatin 344 is a high-affinity binding protein that sequesters GDF-8 and activin, removing them from receptor availability. In research models, GDF-8 induces or amplifies the atrophy phenotype and follistatin 344 rescues it. The two are routinely paired in binding-affinity assays, cell-based rescue assays, and in-vivo validation studies of myostatin-pathway antagonists.<\/p>\n<h3>How is GDF-8 different from GDF-11?<\/h3>\n<p>GDF-8 (myostatin) and GDF-11 share approximately 90% amino-acid identity in the mature domain and bind the same ActRIIB receptor with comparable affinity. The functional roles are partially overlapping but distinct in tissue distribution: GDF-8 is predominantly expressed in skeletal muscle and is the dominant regulator of muscle mass; GDF-11 is more broadly expressed and is studied in cardiac, neural, and hematopoietic contexts. The close sequence similarity makes selective antagonist development a major focus of current research.<\/p>\n<h3>What is the typical GDF-8 research dose?<\/h3>\n<p>Published preclinical protocols typically use 10\u2013100\u00a0ng\/mL working concentrations for in-vitro cell culture experiments (myotube atrophy assays, reporter-cell assays, binding studies), and 0.1\u201310\u00a0mcg per administration for in-vivo rodent atrophy-induction protocols. A 1\u00a0mg vial reconstituted with 1.0\u00a0mL bacteriostatic water yields 1\u00a0mg\/mL \u2014 dilution into PBS or culture medium gives nanomolar working solutions for in-vitro use.<\/p>\n<h3>Is GDF-8 FDA approved?<\/h3>\n<p>No. GDF-8 \/ myostatin is not approved by the FDA, EMA, MHRA, or any other major regulator for human therapeutic use. Myostatin pathway research has produced clinical-stage antagonists (anti-myostatin antibodies, soluble ActRIIB-Fc, follistatin gene therapy), some of which have reached late-stage trials for muscular dystrophy and sarcopenia, but recombinant GDF-8 itself is not a therapeutic. All GDF-8 sold by research-use-only suppliers is for laboratory investigation and should not be administered to humans.<\/p>\n<h3>How should GDF-8 be stored?<\/h3>\n<p>Lyophilized vials: refrigerated at 2\u20138\u00a0\u00b0C for short-term working stock, or \u221220\u00a0\u00b0C for long-term storage of unopened vials. Reconstituted solution: refrigerated at 2\u20138\u00a0\u00b0C, use within 30 days for general protocols or within 7 days for binding-affinity assays requiring tight calibration. Do not freeze reconstituted solution \u2014 recombinant dimeric proteins are particularly sensitive to freeze-thaw denaturation. Protect from direct light at all times. Carrier protein (BSA at 0.1%) is recommended for working dilutions below 100\u00a0mcg\/mL.<\/p>\n<h3>How do I reconstitute GDF-8?<\/h3>\n<p>Follow the reconstitution procedure above. Add bacteriostatic water down the side wall of the vial (not onto the lyophilized cake), swirl gently, and allow 5\u201310 minutes for full dissolution. Do <strong>niet<\/strong> shake the vial \u2014 vigorous agitation can disrupt the intermolecular disulfide bond and degrade activity. A correctly reconstituted solution is clear and colourless with no visible particles. For a 1\u00a0mg vial + 1.0\u00a0mL diluent, the working concentration is 1\u00a0mg\/mL.<\/p>\n<h3>Why is the purity specification 95% rather than 99%?<\/h3>\n<p>Recombinant proteins like GDF-8 cannot achieve the \u226599% HPLC purity standard typical of small synthetic peptides because of inherent heterogeneity in any recombinant expression system \u2014 different folding intermediates and disulfide-isomer forms appear as related peaks on HPLC that are not impurities but isoforms of the target protein. \u226595% HPLC purity is the standard research-grade specification for GDF-8 and similar recombinant disulfide-linked dimer proteins. SDS-PAGE typically shows the expected ~25.8\u00a0kDa band under non-reducing conditions and ~12.9\u00a0kDa monomer under reducing conditions.<\/p>\n<h3>Welke sterktes heeft MedsBase op voorraad?<\/h3>\n<p>MedsBase carries recombinant GDF-8 (Myostatin) in 1\u00a0mg lyophilized vials. The vial is available in 10-vial or 20-vial pack sizes. All vials are supplied at \u226595% HPLC purity with a certificate of analysis available on request.<\/p>\n<h3>Can GDF-8 and Follistatin 344 be paired in research?<\/h3>\n<p>Yes \u2014 this is the canonical use case. The two are routinely paired in three principal ways: (1) binding-affinity measurement via SPR, ELISA, or ITC of the follistatin\u2013myostatin interaction; (2) cell-based atrophy\/rescue assays where GDF-8 induces myotube atrophy and follistatin co-treatment rescues; and (3) in-vivo studies where GDF-8 amplifies a wasting phenotype that follistatin co-administration attenuates. The inverse-pharmacology pairing is foundational to myostatin-axis research design.<\/p>\n<h3>Does GDF-8 cause side effects in research?<\/h3>\n<p>The principal on-target effect of recombinant GDF-8 in research models is muscle atrophy \u2014 this is the intended pharmacological action, not a side effect. Off-target findings include modest effects on cardiac and adipose tissues consistent with the lower-level expression of ActRIIB in those compartments. At very high doses, broader TGF-\u03b2-superfamily-related effects on fibrosis and inflammation can be observed, attributable to receptor cross-talk with activin and GDF-11 pathways.<\/p>\n<h3>What is the half-life of GDF-8?<\/h3>\n<p>In preclinical research, recombinant mature GDF-8 has a plasma half-life of approximately 2\u20134 hours following intravenous administration. Endogenously, mature myostatin circulates bound to its own prodomain (latent complex) and to follistatin \/ other binding proteins, which dramatically extends the effective tissue half-life. For research protocols, the recombinant active dimer is administered without the prodomain to deliver &#8220;free&#8221; myostatin to the ActRIIB receptor.<\/p>\n<h3>Why was GDF-8 originally discovered?<\/h3>\n<p>GDF-8 was identified by McPherron, Lawler, and Lee at Johns Hopkins (Nature 1997) using a degenerate-PCR screening strategy designed to find novel TGF-\u03b2-superfamily members. Targeted disruption in mice produced animals with two- to three-fold larger skeletal muscle mass than wild-type controls \u2014 an arrestingly clear phenotype that immediately established myostatin as the dominant physiological negative regulator of muscle growth. The connection to naturally occurring &#8220;double-muscling&#8221; phenotypes in Belgian Blue cattle and Whippet dogs was established within months, and a human MSTN-mutation case was published in NEJM in 2004.<\/p>\n<h3>How long does GDF-8 take to show effects in preclinical research?<\/h3>\n<p>In-vitro effects on Smad2\/Smad3 phosphorylation are detectable within minutes of cell exposure. Myotube atrophy in cell-based assays is measurable within 24\u201372 hours. In-vivo atrophy phenotypes in rodent models develop over 1\u20134 weeks of regular administration, with the kinetics depending on dose, route, and the underlying muscle-mass baseline of the model organism.<\/p>\n<h3>Can I order GDF-8 for international shipping?<\/h3>\n<p>Yes. MedsBase ships GDF-8 worldwide from our dedicated peptide shipping network. Peptide-only orders qualify for our standalone peptide shipping service. All orders ship in temperature-controlled packaging with full tracking and are covered by our <a href=\"https:\/\/medsbase.com\/nl\/medsbase-re-shipment-assurance-policy\/\">Reshipment Assurance Policy<\/a>.<\/p>\n<p><!-- medsbase-related-alts-v1 --><\/p>\n<h2>Other Peptides for Anabolic, Muscle, and Growth-Axis Research<\/h2>\n<ul>\n<li><a href=\"\/nl\/follistatin-344\/\"><strong>Follistatin 344<\/strong><\/a> \u2014 Myostatin \/ activin antagonist binding protein \u2014 the inverse-pharmacology pair to GDF-8<\/li>\n<li><a href=\"\/nl\/igf-1-lr3\/\"><strong>IGF-1 LR3<\/strong><\/a> \u2014 Long-arginine recombinant IGF-1 analog \u2014 opposite-pathway anabolic stimulus via IGF-1R<\/li>\n<li><a href=\"\/nl\/tb-500\/\"><strong>TB-500 (Thymosin Beta-4)<\/strong><\/a> \u2014 Systemic healing fragment \u2014 muscle and cardiac recovery research<\/li>\n<li><a href=\"\/nl\/cjc-1295-with-dac\/\"><strong>CJC-1295 met DAC<\/strong><\/a> \u2014 Long-acting GHRH analog \u2014 growth hormone axis research<\/li>\n<li><a href=\"\/nl\/sermorelin\/\"><strong>Sermorelin<\/strong><\/a> \u2014 Shorter-acting GHRH(1-29) analog \u2014 natural GH-pulse research<\/li>\n<\/ul>\n<p><!-- medsbase-peptide-guide-cta --><\/p>\n<h2>Verder lezen<\/h2>\n<div style=\"background: #f4f8fb; border-left: 4px solid #2c7cb0; padding: 18px 22px; margin: 18px 0; border-radius: 4px;\">\n<p style=\"margin: 0 0 8px 0;\"><strong>\ud83d\udcd6 Explore the myostatin pathway<\/strong><\/p>\n<p style=\"margin: 0;\">Bekijk het volledige <a href=\"https:\/\/medsbase.com\/nl\/peptides\/\"><strong>onderzoekspeptiden catalogus<\/strong><\/a>, with the inverse-pharmacology pair <a href=\"https:\/\/medsbase.com\/nl\/follistatin-344\/\">Follistatin 344<\/a> as the myostatin antagonist for pathway-rescue research, <a href=\"https:\/\/medsbase.com\/nl\/igf-1-lr3\/\">IGF-1 LR3<\/a> for direct IGF-receptor anabolic research, and <a href=\"https:\/\/medsbase.com\/nl\/tb-500\/\">TB-500<\/a> for systemic muscle and tissue recovery research.<\/p>\n<\/div>\n<p><!-- pep-seo-v1 --><\/p>","protected":false},"excerpt":{"rendered":"<p>\u2705 Recombinant 25.8 kDa active myostatin homodimer<br \/>\n\u2705 Canonical TGF-\u03b2 superfamily atrophic ligand<br \/>\n\u2705 Inverse-pharmacology pair to Follistatin 344<br \/>\n\u2705 ActRIIB \/ Smad2\/Smad3 pathway agonist<br \/>\n\u2705 \u226595% HPLC purity, COA on request<\/p>\n<p><strong>GDF-8 (Myostatine)<\/strong> is a recombinant protein.<\/p>","protected":false},"featured_media":70950,"comment_status":"open","ping_status":"closed","template":"","meta":[],"product_brand":[],"product_cat":[5426],"product_tag":[6279,6278,5441],"class_list":{"0":"post-70729","1":"product","2":"type-product","3":"status-publish","4":"has-post-thumbnail","6":"product_cat-peptides","7":"product_tag-gdf-8","8":"product_tag-myostatin","9":"product_tag-peptide","11":"first","12":"instock","13":"shipping-taxable","14":"purchasable","15":"product-type-variable","16":"has-default-attributes"},"acf":[],"_links":{"self":[{"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/product\/70729","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/product"}],"about":[{"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/types\/product"}],"replies":[{"embeddable":true,"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/comments?post=70729"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/media\/70950"}],"wp:attachment":[{"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/media?parent=70729"}],"wp:term":[{"taxonomy":"product_brand","embeddable":true,"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/product_brand?post=70729"},{"taxonomy":"product_cat","embeddable":true,"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/product_cat?post=70729"},{"taxonomy":"product_tag","embeddable":true,"href":"https:\/\/medsbase.com\/nl\/wp-json\/wp\/v2\/product_tag?post=70729"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}