Myostatin Propeptide Human E. coli Tag free

Cat. No.	Size	Price 1 - 4 pcs / 5 - 9 pcs / 10+ pcs
RD172058100	0.1 mg	$421 / $370 / On request

Technical Data

Type

Recombinant protein

Description

Total 248 AA. MW: 28 kDa (calculated). UniProtKB acc.no. O14793. 243 AA of recombinant human Myostatin Propeptide and 5 extra AA (2 AA N-terminal, 3 AA C-terminal).

Amino Acid Sequence

MGNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRKLN

Source

E. coli

Purity

˃ 90 % by SDS-PAGE

SDS-PAGE Gel

12% SDS-PAGE separation of Human Myostatin Propeptide
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and heated sample, 7μg/lane
3. non-reduced and non-heated sample, 7μg/lane

Endotoxin

< 1.0 EU/µg

Formulation

Filtered (0,4 μm) and lyophilized in 0.5 mg/mL in 20mM TRIS, 50mM NaCl, pH 8.0

Reconstitution

Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely.

Applications

Western blotting, ELISA

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at -80 °C. Lyophilized protein remains stable until the expiry date when stored at -80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.
SDS PAGE to determine purity of the protein. Endotoxin level determination.

Note

This product is intended for research use only.

Summary

Research topic

Cardiovascular disease, Energy metabolism and body weight regulation, Muscle growth and physiology regulation, Pulmonary diseases

Summary

Myostatin (GDF 8) is expressed uniquely in human skeletal muscle as a 12 kDa mature glycoprotein consisting of 109 amino acid residues and secreted into plasma. Myostatin is a member of the transforming growth factor β superfamily of secreted growth and differentiation factors that is essential for proper regulation of skeletal muscle mass. Studies have shown that myostatin could play an important role in cardiac development and physiology. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority (>70%) of myostatin in serum bound to its propeptide. The myostatin propeptide is negative regulator of myostatin in vivo.

Product References (1)

References

Diel P, Schiffer T, Geisler S, Hertrampf T, Mosler S, Schulz S, Wintgens KF, Adler M. Analysis of the effects of androgens and training on myostatin propeptide and follistatin concentrations in blood and skeletal muscle using highly sensitive immuno PCR. Mol Cell Endocrinol. 2010 Dec 15;330(1-2):1-9. doi: 10.1016/j.mce.2010.08.015. Epub 2010 Aug 27. PubMed PMID: 20801187. See more on PubMed

Summary References (9)

References to Myostatin

Artaza JN, Bhasin S, Magee TR, Reisz-Porszasz S, Shen R, Groome NP, Meerasahib MF, Gonzalez-Cadavid NF. Myostatin inhibits myogenesis and promotes adipogenesis in C3H 10T(1/2) mesenchymal multipotent cells. Endocrinology. 2005 Aug;146 (8):3547-57
Gonzalez-Cadavid NF, Taylor WE, Yarasheski K, Sinha-Hikim I, Ma K, Ezzat S, Shen R, Lalani R, Asa S, Mamita M, Nair G, Arver S, Bhasin S. Organization of the human myostatin gene and expression in healthy men and HIV-infected men with muscle wasting. Proc Natl Acad Sci U S A. 1998 Dec 8;95 (25):14938-43
Hill JJ, Davies MV, Pearson AA, Wang JH, Hewick RM, Wolfman NM, Qiu Y. The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. J Biol Chem. 2002 Oct 25;277 (43):40735-41
Jiang MS, Liang LF, Wang S, Ratovitski T, Holmstrom J, Barker C, Stotish R. Characterization and identification of the inhibitory domain of GDF-8 propeptide. Biochem Biophys Res Commun. 2004 Mar 12;315 (3):525-31
Lee SJ, McPherron AC. Regulation of myostatin activity and muscle growth. Proc Natl Acad Sci U S A. 2001 Jul 31;98 (16):9306-11
McPherron AC, Lee SJ. Double muscling in cattle due to mutations in the myostatin gene. Proc Natl Acad Sci U S A. 1997 Nov 11;94 (23):12457-61
Sharma M, Kambadur R, Matthews KG, Somers WG, Devlin GP, Conaglen JV, Fowke PJ, Bass JJ. Myostatin, a transforming growth factor-beta superfamily member, is expressed in heart muscle and is upregulated in cardiomyocytes after infarct. J Cell Physiol. 1999 Jul;180 (1):1-9
Taylor WE, Bhasin S, Artaza J, Byhower F, Azam M, Willard DH Jr, Kull FC Jr, Gonzalez-Cadavid N. Myostatin inhibits cell proliferation and protein synthesis in C2C12 muscle cells. Am J Physiol Endocrinol Metab. 2001 Feb;280 (2):E221-8
Thies RS, Chen T, Davies MV, Tomkinson KN, Pearson AA, Shakey QA, Wolfman NM. GDF-8 propeptide binds to GDF-8 and antagonizes biological activity by inhibiting GDF-8 receptor binding. Growth Factors. 2001;18 (4):251-9

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