Human Growth and Differentiation Factor-11 (AF)

Product code: 32-12086

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  •   20 µg

  •  100 µg

  • $430.00 

  • $823.00 

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Amount : 100 µg
Purification : Reducing and Non-Reducing SDS PAGE at >= 95%
Content : Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA)
Sterile 10 mM HCl at 0.1 mg/mL
Storage condition : Store at -20°C
AA sequence : NLGLDCDEHS SESRCCRYPL TVDFEAFGWD WIIAPKRYKA NYCSGQCEYM FMQKYPHTHL VQQANPRGSA GPCCTPTKMS PINMLYFNDK QQIIYGKIPG MVVDRCGCS
Gene : GDF11
Gene ID : 10220
Uniprot ID : O95390
Alternative Name : Bone morphogenetic protein 11, BMP11
Source: Genetically modified E.coli.
Predicted MW: Dimer, 12.5/24.9 kDa (109/218 aa)
Growth differentiation factor 11 (GDF-11), also known as bone morphogenetic protein 11 (BMP-11), is a regulator of cell growth and differentiation during muscular and neural development. GDF-11 binds the transforming growth factor-beta receptors ALK4, ALK5, and ALK7 to activate SMAD signaling. In adults, exogenous GDF-11 promotes cardiomyocyte regeneration to reverse age-related cardiac hypertrophy.

Endotoxin: Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Biological Activity was determined by Alkaline phosphatase activity in ATDC5 cells at <= 100 ng/mL; >= 1.0 x 10^4 units/mg (typical ED50 is < 10 ng/mL). Centrifuge vial before opening, Suspend the product by gently pipetting the above recommended solution down the sides of the vial. DO NOT VORTEX. Allow several minutes for complete reconstitution. For prolonged storage, dilute to working aliquots in a 0.1% BSA solution, store at -80°C and avoid repeat freeze thaws. Upon reconstitution, a small amount of visible precipitate can be expected. A 10% overfill has been added to the total material vialed to compensate for this loss.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

Subcellular location: Secreted
Post transnational modification: Synthesized as large precursor molecule that undergoes proteolytic cleavage. The mature C-terminal portion of the molecule is bound non-covalently to its N-terminal propeptide rendering it inactive. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase.
BioGrid: 115515. 20 interactions.
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