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protein

Human Myostatin Recombinant

MBS553028

0.01 mg

220 USD

MBS553028

Recombinant Protein

Human Myostatin Recombinant

Myostatin

MSTN; myostatin; gdf8

growth/differentiation factor 8; Growth/differentiation factor 8; Myostatin

GDF8

MSTN; GDF8; GDF-8

GDF8_HUMAN

E Coli

375

MQKLQLCVYI YLFMLIVAGP VDLNENSEQK ENVEKEGLCN ACTWRQNTKS SRIEAIKIQI LSKLRLETAP NISKDVIRQL LPKAPPLREL IDQYDVQRDD SSDGSLEDDD YHATTETIIT MPTESDFLMQ VDGKPKCCFF KFSSKIQYNK VVKAQLWIYL RPVETPTTVF VQILRLIKPM KDGTRYTGIR SLKLDMNPGT GIWQSIDVKT VLQNWLKQPE SNLGIEIKAL DENGHDLAVT FPGPGEDGLN PFLEVKVTDT PKRSRRDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA PKRYKANYCS GECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII YGKIPAMVVD RCGCS

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

Recombinant Myostatin was lyophilized from a 0.2 um filtered Tris solution pH 8.0.

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

Domain: TGFB. Host Note: Optimized DNA sequence encoding Human Myostatin mature chain was expressed in Escherichia Coli.

Endotoxin: Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/ug (1EU/ug). 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. Molecular Weight Note: 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.

Cytokines

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 (TGF- ) superfamily, which includes the TGF- s, 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- 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- family proteins, GDF-8 is highly conserved across species. Mature human, mouse, rat, and cow GDF-8 share 100% aa sequence identity. Among TGF- 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- 1, 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.

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.

4885259

NP_005250.1

NM_005259.2

O14793

42,750 Da

Hypertrophy Model Pathway 198828

Function: Acts specifically as a negative regulator of skeletal muscle growth. Subunit structure: Homodimer; disulfide-linked . By similarity. Interacts with WFIKKN2, leading to inhibit its activity. Interacts with FST3. Ref.5 Ref.7. Subcellular location: Secreted. Involvement in disease: Muscle hypertrophy (MSLHP) [MIM:614160]: A condition characterized by increased muscle bulk and strength. Affected individuals are exceptionally strong.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6. Sequence similarities: Belongs to the TGF-beta family.

0.01 mg

220 USD