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|Growth Differentiation Factor 8|
Regulatory factors that determine actual cell size and number are relatively unknown. It has been suggested that tissues regulate their own size by synthesizing "inhibitors" that feedback on individual cells. When the collective concentration of tissue-specific inhibitor reaches a critical level, tissue-specific cells are frozen in size and number. It has also been proposed that cells outside the tissue of interest, clear or non-functionally bind circulating inhibitor. Thus, the proportion of cells secreting "inhibitor" relative to all cells making up the organism determines the availability of any limiting factor. The larger the quantity of tissue secreting inhibitor, the more inhibitor available to the secreting tissue after body-wide clearance.
One tissue that appears to support the theory of growth inhibition is skeletal muscle. Initial interest in myostatin (or GDF-8; growth/differentiation factor 8) as an inhibitor of skeletal muscle was based on the observation that the GDF-8 gene in double-muscled Belgian Blue and Piedmontese cattle was mutated, thus creating a non-functional protein.1,2 In Belgian Blue cattle, the gene for GDF-8 codes for a mature GDF-8 that is less than 10 amino acids (aa) long; in Piedmontese cattle, a critical cysteine is lost, resulting in a misfolded molecule.2 Recent studies in mice have confirmed the initial observations in cattle; a GDF-8 null mouse results in a super-muscular animal with abnormal muscle mass.3-5 Experiments have also shown that a functional GDF-8 inhibits the growth and proliferation of mouse C2C12 skeletal muscle cells.6,7 GDF-8 is a member of the TGF-beta superfamily (TGF-beta SF), demonstrating a characteristic cysteine knot configuration with extremely high aa conservation across species.2,4,8-11 Like all TGF-beta SF members, GDF-8 is synthesized as a pre-proprotein that undergoes intracellular proteolytic cleavage to create a 109 aa, 24-30 kDa mature, disulfide-linked dimer.4,6,10,12,13 Unlike most members of the TGF-beta SF, the mature GDF-8 dimer is secreted as a latent complex, retaining its pro-region in a non-covalent interaction that is analogous to that for TGF-beta 1. This pro-region confers latency on the mature GDF-8 dimer.
GDF-Series Microcomputer Excitation Controller only needs one button to start up, so it can realize full automatic excitation control and unattended operation.
GDF-5 excitation controller is the new version of high voltage excitation controller in 2014, which corrects many software and hardware problems in the old version. The new version of the controller adopts software synchronization, which is almost applicable to the controllable silicon control circuits of all kinds of connected excitation transformers, and relaxes the requirements for the connection of voltage transformers.
1) The gene encoding myostatin was discovered in 1997 by geneticists Se-Jin Lee and Alexandra McPherron who produced a strain of mutant mice that lack the gene. These myostatin "knockout" mice have approximately twice as much muscle as normal mice. These mice were subsequently named "mighty mice".
2) Naturally occurring deficiencies of myostatin have been identified in cattle by Ravi Kambadur, whippets, and humans; in each case the result is a dramatic increase in muscle mass. A mutation in the 3' UTR of the myostatin gene in Texel sheep creates target sites for the microRNAs miR-1 and miR-206. This is likely to cause the muscular phenotype of this breed of sheep.
3) Human myostatin consists of two identical subunits, each consisting of 109 (NCBI database claims human myostatin is 375 residues long) amino acid residues. Its total molecular weight is 25.0 kDa. The protein is inactive until a protease cleaves the NH2-terminal, or "pro-domain" portion of the molecule, resulting in the active COOH-terminal dimer. Myostatin binds to the activin type II receptor, resulting in a recruitment of either coreceptor Alk-3 or Alk-4. This coreceptor then initiates a cell signaling cascade in the muscle, which includes the activation of transcription factors in the SMAD family - SMAD2 and SMAD3. These factors then induce myostatin-specific gene regulation. When applied to myoblasts, myostatin inhibits their differentiation into mature muscle fibers.
Myostatin also inhibits Akt, a kinase that is sufficient to cause muscle hypertrophy, in part through the activation of protein synthesis. However, Akt is not responsible for all of the observed muscle hyperthrophic effects which are mediated by myostatin inhibition Thus myostatin acts in two ways: by inhibiting muscle differentiation, and by inhibiting Akt-induced protein synthesis.
|Description||white lyophilized powder||white lyophilized powder|
|Loss of drying||≤1.0%||0.5%|
|TLC||Only one spot||Only one spot|
|Conclusion||It complies with the USP 32.|
|HGH Frag176 191(HGH)||2mg|
|HGH Frag176 191(HGH)||5mg|
|CJC1295 With DAC||2mg/vial, 10vials/box|
|CJC1295 without DAC--MOD GRF(1-29)||2mg/vial, 10vials/box|
|PT141 (Bremelanotide)||10mg/vial, 10vials/box|
|MGF (Mechano growthfactor) (IGF- IEC)||2mg/vial, 10vials/box|
|PEG MGF||2mg/vial, 10vials/box|
|Triptorelin/Gnrh Triptoreli||2mg/vial, 10vials/box|
|IGF LR3-1||0.1mg/vial, 10vials/box|
|IGF LR3-1||1mg/vial, 10vials/box|
|IGF IDES||1mg/vial, 10vials/box|
|Follistatin 344||1mg/vial, 10vials/box|
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