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Human Myostatin Recombinant

GDF8

accession:  O14793
   Size A     2ug   $ 70
   Size B      10ug  $160
   Size C      1mg  $ 4700
Domain  :  TGFB
Gene  :  GDF8
Catalog no. :  RKO14793
Source:
Optimized DNA sequence encoding Human Myostatin mature chain was expressed in Escherichia Coli.

 
Molecular weight:

Native human Myostatin, generated by the proteolytic removal of the signal peptide
and propeptide, molecule has a calculated molecular mass of approximately 13 kDa.

Recombinant human Myostatin is a disulfide-linked homodimeric protein consisting of two 110 amino acid residue subunits, and migrates as an approximately 25 kDa protein under non-reducing conditions and as a 13kDa protein under reducing conditions in SDS-PAGE.


 
Purity:
>97%, as determined by SDS-PAGE and HPLC

 
Biological Activity:
The ED(50) was determined by the dose-dependent proliferation inhibition of human MPC-11 cells was found to be in the range of 20.0-40.0 ng/ml.

 
Protein Sequence:
        10         20         30         40         50         60 
MQKLQLCVYI YLFMLIVAGP VDLNENSEQK ENVEKEGLCN ACTWRQNTKS SRIEAIKIQI 

        70         80         90        100        110        120 
LSKLRLETAP NISKDVIRQL LPKAPPLREL IDQYDVQRDD SSDGSLEDDD YHATTETIIT 

       130        140        150        160        170        180 
MPTESDFLMQ VDGKPKCCFF KFSSKIQYNK VVKAQLWIYL RPVETPTTVF VQILRLIKPM 

       190        200        210        220        230        240 
KDGTRYTGIR SLKLDMNPGT GIWQSIDVKT VLQNWLKQPE SNLGIEIKAL DENGHDLAVT 

       250        260        270        280        290        300 
FPGPGEDGLN PFLEVKVTDT PKRSRRDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA 

       310        320        330        340        350        360 
PKRYKANYCS GECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII 

       370 
YGKIPAMVVD RCGCS 
(*)Complete precursor sequence shown, expressed chain highlighted
 
Endotoxin:
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).

 
Presentation:
Recombinant Myostatin was lyophilized from a 0.2 μm filtered Tris solution pH 8.0.

 
Reconstitution:
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers

 
Storage:
The lyophilized protein is stable for at least 2 years from date of receipt at -20° C.
Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8° C for one month, or at -20° C for six months, with a carrier protein without detectable loss of activity.

Avoid repeated freeze/thaw cycles.

 
Usage:
This cytokine product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.

 

Myostatin

Growth differentiation Factor 8 (GDF-8), also known as myostatin, is a secreted protein that is expressed specifically in developing and adult skeletal muscle. It controls myoblast proliferation and is a potent negative regulator of skeletal muscle mass.GDF-8 belongs to the transforming growth factor β (TGF-β) superfamily, which includes the TGF-βs, bone morphogenetic proteins (BMPs), growth differentiation factors (GDFs), activins, inhibins, leftys, nodal, Mullerian inhibitory substance (MIS) and the glial cell line-derived neurotrophic factors (GDNFs).2 All TGF-β superfamily members are synthesized and secreted as a homodimeric prepropeptide that is cleaved by proprotein convertases such as furin to generate the dimeric N- terminal propeptide and the dimeric C-terminal mature active protein. The C- terminal mature protein contains the characteristic conserved cysteine residues involved in the formation of the cysteine knot domain. Mouse GDF-8 cDNA encodes a 376 amino acid residue (aa) preproprotein with a putative 24 aa signal peptide, a 243 aa propeptide and a 109 aa mature protein.1 As is the case with most TGF-β family proteins, GDF-8 is highly conserved across species. Mature human, mouse, rat, and cow GDF-8 share 100% aa sequence identity. Among TGF-β family members, GDF-8 is most closely related to GDF- 11/BMP-11. The two proteins share 65% overall aa sequence, within their mature regions, the two proteins differ only by 11 aa.residues. Similarly to TGF-β1, 2, and 3, the GDF-8 homodimeric propeptide and mature protein remained non- covalently linked after proteolytic cleavage, and is released as a biologically inactive latent complex that does bind its receptor.3 In serum, GDF-8 has also been found to exist in a large latent complex that also included FLGR (follistatin-related gene) and GASP-1 (growth and differentiation factor- associated serum protein-1) in addition to the propeptide.4 R&D Systems’ recombinant GDF-8 propeptide is capable of associating with the active GDF-8 with high- affinity to reconstitute the latent complex and is potent GDF-8 antagonist.

Related Publications:
relation between extent of Myostatin depletion and muscle growth in mature mice
Am J Physiol Endocrinol Metab, Oct 2009; 297: E935 - E940.
Myostatin inhibits igf-i induced myotube hypertrophy through akt
Am J Physiol Cell Physiol, Sep 2009; 10.1152/ajpcell.00043.2009.
Myostatin represses physiological hypertrophy of the heart and excitation-contraction couping
J. Physiol., Sep 2009; 10.1113/jphysiol.2009.172544.
Myostatin inhibition enhances the effects of exercise on performance and metabolic outcomes in aged mice
J Gerontol A Biol Sci Med Sci, Sep 2009; 64A: 940 - 948.
inhibition of Myostatin does not ameliorate disease features of severe spinal muscular atrophy mice
Hum. Mol. Genet., Sep 2009; 18: 3145 - 3152.




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