Recombinant Human/Mouse/Rat GDF-8 Protein

Name: Recombinant Human/Mouse/Rat GDF-8 Protein
Brand: Beta LifeScience
SKU: BL-2256NP
Availability: InStock

BL-2256NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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Product Overview

Description	Recombinant Human/Mouse/Rat Growth Differentiation Factor 8 is produced by our Mammalian expression system and the target gene encoding Lys262-Ser375 is expressed.
Accession	O14793
Synonym	Growth/differentiation factor 8; GDF-8; Myostatin; Mstn; Gdf8
Gene Background	Growth/differentiation factor 8(Mstn, GDF-8) is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. It is expressed specifically in developing and adult skeletal muscle. It exists as a homodimer, and interacts with WFIKKN2, leading to inhibit its activity. This protein can act specifically as a negative regulator of skeletal muscle growth. It regulates cell growth and differentiation in both embryonic and adult tissues.
Molecular Mass	13.1 KDa
Apmol Mass	12-15 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Acts specifically as a negative regulator of skeletal muscle growth.
Subcellular Location	Secreted.
Protein Families	TGF-beta family
Database References	HGNC: 4223 OMIM: 601788 KEGG: hsa:2660 STRING: 9606.ENSP00000260950 UniGene: PMID: 30241032 the maturation and secretion of myostatin precursor MstnPP and its metabolites in a human muscle cell line, was investigated. PMID: 29546591 Acute high-intensity interval exercise decreased irisin levels and increased myostatin levels. PMID: 29558345 Autosomal Dominant Polycystic Kidney Disease patients with moderately preserved renal function have higher levels of FasL, myostatin and urine TGF-beta1 than controls PMID: 29794429 Tolloid cleavage activates latent GDF8 by destabilizing specific prodomain-growth factor interfaces and primes the growth factor for release from the prodomain. PMID: 29343545 Myostatin pathway is down-regulated in the neuromuscular diseases. PMID: 29192144 the prodomain:GDF8 complex can exist in a fully latent state and an activated or "triggered" state where the prodomain remains in complex with the mature domain PMID: 29348202 Higher serum myostatin levels correlated with muscle mass loss, hyperammonemia, and impaired protein synthesis, as reflected by lower serum albumin levels and lower branched-chain amino acid to tyrosine ratio levels. High serum myostatin levels were also associated with a reduced OS rate in LC patients. PMID: 28627027 Study showed the expression of myostatin in healthy endometrium and a higher expression in endometriosis and endometrial cancer, suggesting myostatin involvement in human endometrial physiology and related pathologies. PMID: 28345488 Studied levels of myostatin in both serum and synovial fluid in patients with knee osteoarthritis and found both correlated with severity of knee osteoarthritis. PMID: 27878995 Myostatin (and Smad2) were significantly up-regulated in the failing heart of female patients, but not male patients. PMID: 28465115 The Growth Differentiation Factor 11 (GDF11) and Myostatin (MSTN) in tissue specific aging. PMID: 28472635 MSTN 153Arg(R) polymorphism is associated with long distance running success. PMID: 28007336 GDF8 promotes ovarian cancer cell migration via ALK4/5-SMAD2/3-E-cadherin signaling. PMID: 27481097 Results demonstrat that GDF8 stimulates the expression and secretion of CTGF in human granulosa cells and provide evidence that both proteins may play critical roles in the regulation of extracellular matrix formation in these cells. PMID: 27392496 These studies identify distinctive structural features of GDF11 that enhance its potency, relative to GDF8; however, the biological consequences of these differences remain to be determined. PMID: 28257634 Serum myostatin levels were significantly decreased in heart failure patients and associated with lower extremity muscle wasting. PMID: 27390974 our data showed a virtual absence of the variant (K) allele in MSTN rs1805086 in Japanese population, and no differences in allele/genotype frequencies in ACTN3 rs1815739 among centenarians and healthy controls of this country. PMID: 27861536 MSTN, but not GDF11, declines in healthy men throughout aging. PMID: 27304512 Multivariate regression analysis revealed that myostatin levels correlated significantly with tricuspid annular plane systolic excursion values and right ventricle myocardial performance index among the study patients PMID: 27323660 Study measured circulating myostatin levels in seven inherited muscle diseases using an immunoaffinity LC-MS/MS approach, found significantly lower serum myostatin concentrations in numerous muscle disease patient populations and the associations with clinical measurements suggests the potential utility of myostatin as a biomarker of genetic muscle disease progression PMID: 28074267 data indicated that serum myostatin concentration did not correlate with muscle and bone mass in postmenopausal women PMID: 27144806 Myostatin mRNA expression in skeletal muscle was significantly reduced compared with pre-exercise values at all time points with no difference between exercise intensity. PMID: 27467217 Low expression of serum MSTN is associated with Cachexia Prevention in Patients with Medullary Thyroid Cancer. PMID: 27165248 Myostatin was differentially expressed in the muscle and adipose tissue in relation to physical activity and dysglycaemia PMID: 26572800 Our results suggest that serum levels of myostatin and irisin are related in patients with type 2 diabetes PMID: 26438394 Matrix metalloproteinase 14 was highly expressed in uterine leiomyoma and correlated with myostatin and activin A mRNA expression. Moreover, MMP14 and myostatin mRNA expression correlated significantly and directly with the intensity of dysmenorrhea. PMID: 26138721 A synthetic peptide corresponding to this decorin region dose-dependently inhibited the response to myostatin in cardiomyocytes PMID: 27559042 Findings suggest that GDF8 and CTGF may play critical roles in the regulation of proliferative events in human granulosa cells. PMID: 26577677 Myostatin concentrations in plasma and protein expression in placental tissue are significantly higher in women with preeclampsia. Cytokine production by first-trimester placental tissues was altered following myostatin treatment. PMID: 25736326 Myostatin is a well-described negative regulator of postnatal skeletal and cardiac muscle mass and modulates metabolic processes. It functions in the heart, skeletal muscle, and brain. Review. PMID: 27034275 Plasma myostatin levels are increased in chronic obstructive pulmonary disease patients who have cor pulmonale. PMID: 26998756 In human granulosa cells, GDF8 may play an important role in the modulation of cellular responsiveness to gonadotropins and in the regulation of ovarian steroid production, most likely as a luteinization inhibitor. PMID: 26607022 Plasma myostatin might be suitable in predicting weight regain after marked weight loss, but no association with weight loss was observed in patients undergoing a non-surgical weight loss program. PMID: 26393401 Plasma MSTN level was elevated in an early stage of CKD, which could be involved in the progression of sarcopenia. PMID: 26502079 it is becoming clearer that besides its conventional role in muscle, myostatin plays a critical role in metabolism. Hence, molecular mechanisms by which myostatin regulates several key metabolic processes need to be further explored. PMID: 26305594 The aim of this study was to investigate MSTN polymorphisms in an elderly sarcopenic population in Turkey and determine how they relate to sarcopenia. PMID: 26046327 There is a significant decrease in levels of circulating myostatin in postsurgical acute phase reaction. PMID: 25749570 Myostatin myocardial expression increases in the presence of structural cardiomyopathy either of hypertensive or other origin. PMID: 25915890 In contrast to elite endurance and power track and field athletes, the MSTN 153RR genotype was not found in short distance-swimmers, and among the long distance-swimmers it was not associated with top level swimming performance. PMID: 25936293 Lower serum myostatin independently associated with MetS, central obesity, low HDL-C, and high triglycerides after adjustment. Higher serum myostatin is associated with favorable metabolic profiles. PMID: 25254550 Results indicate that GDF8 down-regulates PTX3 expression via SMAD-dependent signaling in human granulosa cells suggesting a potential role for GDF8 in the regulation of follicular function. PMID: 25641196 Adenomyotic tissues express high levels of myostatin, follistatin, and activin type II receptors. PMID: 26086422 This is the first demonstration of a spatial asymmetry in the expression pattern of Mstn/IGF-I in healthy hearts, which is likely to play a role in the different growth regulation of left vs. right ventricle PMID: 25591711 Myostatin expression in placental tissue is altered under stress conditions (e.g. obesity and abnormal glucose metabolism) found in pregnancies complicated with gestational diabetes mellitus. PMID: 25443639 we show that the K153R mutation significantly increases the rate of proteolysis of promyostatin by furin, but has no effect on the activity of the latent complex or the cleavage of the latent complex by bone morphogenetic protein 1 (BMP-1). PMID: 25543063 MyoD acts to promote SC proliferation and transition of cells into differentiation, while myogenin is known to drive terminal differentiation PMID: 25108351 role of myostatin in cardiovascular disease and cachexia PMID: 24680839 Myostatin localization was positively identified in extravillous trophoblast. Myostatin positively affected proliferation and migration of extravillous trophoblast. PMID: 25093622 The present study demonstrated that the variant alleles of MSTN A55T and K153R polymorphisms could significantly enhance muscle hypertrophy in response to strength training among Han Chinese men. PMID: 24479661

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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