Myostatin Propeptide (HMP) 1mg

Myostatin Propeptide (HMP) 1mg

Myostatin Propeptide (HMP) 1mg

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Myostatin Propeptide is a 244 amino acid peptide developed as a segment analogue of a naturally occurring form of myostatin1. Myostatin, a member of the TGF-beta superfamily, is a negative regulator of myocyte action, thereby inhibiting the development of skeletal muscle2. When myostatin circulates through the mammalian blood stream it is found in an inactive state, bound to a deactivating propeptide3. Myostatin Propeptide imitates the action of this endogenous propeptide, binding free myostatin in the circulatory system. Through the deactivation of myostatin – i.e. being a myostatin blocker – Myostatin Propeptide allows the uninhibited action of myocytes to give rise to new muscle cells and to encourage the growth of a developed musculature4.

Description

Myostatin Propeptide is a 244 amino acid peptide developed as a segment analogue of a naturally occurring form of myostatin1. Myostatin, a member of the TGF-beta superfamily, is a negative regulator of myocyte action, thereby inhibiting the development of skeletal muscle2. When myostatin circulates through the mammalian blood stream it is found in an inactive state, bound to a deactivating propeptide3. Myostatin Propeptide imitates the action of this endogenous propeptide, binding free myostatin in the circulatory system. Through the deactivation of myostatin – i.e. being a myostatin blocker – Myostatin Propeptide allows the uninhibited action of myocytes to give rise to new muscle cells and to encourage the growth of a developed musculature4.

Myostatin Blocker and Hypertrophy Stimulator

Animal studies have demonstrated Myostatin Propeptide’s potent ability to encourage significant growth of skeletal muscle. By deregulating the activity of myocytes and myoblasts – muscle-producing cells – remarkable hypertrophy (growth of muscle cells) has been observed5. During this process of efficient muscle growth, myocytes turn to adipose tissue as a fuel source, leading to muscle gains and fat losses in animal test subjects6. The combined effects of Phospho DSIP make it an extremely attractive agent for the avoidance of musculature deterioration in muscle-wasting diseases like muscular dystrophy7.

Product Comparison

Myostatin Propeptide has similar effects in stimulating muscular hypertrophy as ACV2RB and Follistatin-344, though it achieves the deregulation of myocyte activity through a very different mechanism. ACV2RB acts as an exogenous stimulator of myocyte activity, doing very little to block myostatin, which is produced by the body to inhibit muscle-growing action8. Follistatin-344 acts to inhibit myostatin’s access to signalling receptors, thereby limiting its ability to regulate muscle growth and leading to significant hypertrophy9.

Myostatin Propeptide shows synergy with members of the GHRP (e.g. GHRP-2, GHRP-6, Ipamorelin), and GHRH (e.g. CJC 1295 with DAC, CJC 1295 no DAC, Fragment 176-191, AOD 9604, Hexarelin, Sermorelin) families, allowing the additional muscle cells produced as a result of Myostatin Propeptide administration to be met with a pulse of GH, assisting with their growth. IGF-1 LR3, IGF-1 DES, MGF, and PEG MGF are also recommended in a combination with Myostatin Propeptide for the achievement of significant muscle gains.

Synonyms: GDF-8 Inhibitor; MSTN; Growth Differentiation Factor 8; MSTN Muscle Hypertroph; Myostatin Inhibitor; HMP: Myopro; Myostatin MP; Myostatin HMP;

Peer-Reviewed Sources:

(1) Hill, J. J., Davies, M. V., Pearson, A. A., Wang, J. H., Hewick, R. M., Wolfman, N. M., & Qiu, Y. (2002). The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. Journal of Biological Chemistry, 277(43), 40735-40741.

(2) Miyazono, K. (2000). Positive and negative regulation of TGF-beta signaling. Journal of cell science, 113(7), 1101-1109.

(3) Lee, S. J., & McPherron, A. C. (2001). Regulation of myostatin activity and muscle growth. Proceedings of the National Academy of Sciences, 98(16), 9306-9311.

(4) Hill, J. J., Davies, M. V., Pearson, A. A., Wang, J. H., Hewick, R. M., Wolfman, N. M., & Qiu, Y. (2002). The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. Journal of Biological Chemistry, 277(43), 40735-40741.

(5) Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., & Lee, S. J. (2004). Myostatin mutation associated with gross muscle hypertrophy in a child. New England Journal of Medicine, 350(26), 2682-2688.

(6) Zhang, C., McFarlane, C., Lokireddy, S., Masuda, S., Ge, X., Gluckman, P. D., & Kambadur, R. (2012). Inhibition of myostatin protects against diet-induced obesity by enhancing fatty acid oxidation and promoting a brown adipose phenotype in mice. Diabetologia, 55(1), 183-193.

(7) Bogdanovich, S., Perkins, K. J., Krag, T. O., Whittemore, L. A., & Khurana, T. S. (2005). Myostatin propeptide-mediated amelioration of dystrophic pathophysiology. The FASEB Journal, 19(6), 543-549.

(8) Thompson, T. B., Woodruff, T. K., & Jardetzky, T. S. (2003). Structures of an ActRIIB: activin A complex reveal a novel binding mode for TGF‐β ligand: receptor interactions. The EMBO journal, 22(7), 1555-1566.

(9) Amthor, H., Nicholas, G., McKinnell, I., Kemp, C. F., Sharma, M., Kambadur, R., & Patel, K. (2004). Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis. Developmental biology, 270(1), 19-30.

More Information
Residue Sequence MG NENSEQKE NVEKEGLCNA CTWRQNTKSS RIEAIKIQIL SKLRLETAPN ISKDVIRQLL PKAPPLRELI DQYDVQRDDS SDGSLEDDDY HATTETIITM PTESDFLMQV DGKPKCCFFK FSSKIQYNKV VKAQLWIYLR PVETPTTVFV QILRLIKPMK DGTRYTGIRS LKLDMNPGTG IWQSIDVKTV LQNWLKQPES NLGIEIKALD ENGHDLAVTF PGPGEDGLNP FLEVKVTDTP KRSRRKLN
Molar Mass 27.8 kDa
Specificity Myostatin Propeptide is known to bind endogenous myostatin specifically, thereby blocking its myocyte inhibiting action.
Physical Appearance Fine White Lyophilized Powder
Solubility 100 μg/mL sterile diluent (distilled de-ionized water)
Stability Lyophilized protein is to be stored at -20°C. It is recommended to aliquot the reconstituted (dissolved) protein into several discrete vials in order to avoid repeated freezing and thawing. Reconstituted protein can be stored at 4°C.
Source Biosynthetic production
This product is prepared for LABORATORY RESEARCH USE ONLY and may not be used for other purposes.