Recombinant Human/Mouse/Rat GDF-8 Protein

Beta LifeScience SKU/CAT #: BL-2256NP
BL-2256NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-2256NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human/Mouse/Rat GDF-8 Protein

Beta LifeScience SKU/CAT #: BL-2256NP
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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
Associated Diseases Muscle hypertrophy (MSLHP)

Gene Functions References

  1. Mstn deficiency-induced apoptosis took place along with generation of reactive oxygen species and elevated fatty acid oxidation, which may play a role in triggering mitochondrial membrane depolarization, the release of cytochrome c, and caspase activation. PMID: 30241032
  2. the maturation and secretion of myostatin precursor MstnPP and its metabolites in a human muscle cell line, was investigated. PMID: 29546591
  3. Acute high-intensity interval exercise decreased irisin levels and increased myostatin levels. PMID: 29558345
  4. 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
  5. Tolloid cleavage activates latent GDF8 by destabilizing specific prodomain-growth factor interfaces and primes the growth factor for release from the prodomain. PMID: 29343545
  6. Myostatin pathway is down-regulated in the neuromuscular diseases. PMID: 29192144
  7. 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
  8. 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
  9. 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
  10. 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
  11. Myostatin (and Smad2) were significantly up-regulated in the failing heart of female patients, but not male patients. PMID: 28465115
  12. The Growth Differentiation Factor 11 (GDF11) and Myostatin (MSTN) in tissue specific aging. PMID: 28472635
  13. MSTN 153Arg(R) polymorphism is associated with long distance running success. PMID: 28007336
  14. GDF8 promotes ovarian cancer cell migration via ALK4/5-SMAD2/3-E-cadherin signaling. PMID: 27481097
  15. 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
  16. 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
  17. Serum myostatin levels were significantly decreased in heart failure patients and associated with lower extremity muscle wasting. PMID: 27390974
  18. 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
  19. MSTN, but not GDF11, declines in healthy men throughout aging. PMID: 27304512
  20. 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
  21. 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
  22. data indicated that serum myostatin concentration did not correlate with muscle and bone mass in postmenopausal women PMID: 27144806
  23. 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
  24. Low expression of serum MSTN is associated with Cachexia Prevention in Patients with Medullary Thyroid Cancer. PMID: 27165248
  25. Myostatin was differentially expressed in the muscle and adipose tissue in relation to physical activity and dysglycaemia PMID: 26572800
  26. Our results suggest that serum levels of myostatin and irisin are related in patients with type 2 diabetes PMID: 26438394
  27. 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
  28. A synthetic peptide corresponding to this decorin region dose-dependently inhibited the response to myostatin in cardiomyocytes PMID: 27559042
  29. Findings suggest that GDF8 and CTGF may play critical roles in the regulation of proliferative events in human granulosa cells. PMID: 26577677
  30. 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
  31. 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
  32. Plasma myostatin levels are increased in chronic obstructive pulmonary disease patients who have cor pulmonale. PMID: 26998756
  33. 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
  34. 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
  35. Plasma MSTN level was elevated in an early stage of CKD, which could be involved in the progression of sarcopenia. PMID: 26502079
  36. 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
  37. 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
  38. There is a significant decrease in levels of circulating myostatin in postsurgical acute phase reaction. PMID: 25749570
  39. Myostatin myocardial expression increases in the presence of structural cardiomyopathy either of hypertensive or other origin. PMID: 25915890
  40. 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
  41. 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
  42. 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
  43. Adenomyotic tissues express high levels of myostatin, follistatin, and activin type II receptors. PMID: 26086422
  44. 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
  45. 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
  46. 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
  47. MyoD acts to promote SC proliferation and transition of cells into differentiation, while myogenin is known to drive terminal differentiation PMID: 25108351
  48. role of myostatin in cardiovascular disease and cachexia PMID: 24680839
  49. Myostatin localization was positively identified in extravillous trophoblast. Myostatin positively affected proliferation and migration of extravillous trophoblast. PMID: 25093622
  50. 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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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