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Recombinant human GDF-5 is a non-glycosylated homodimer containing two 120 amino acids chains. To enable bacterial expression the N-terminal sequence of Ala-Pro-Leu-Thr was replaced with a Lys.
Reconstitute using sterile water at 0.1 mg/mL and centrifuge prior to opening vial. Gently pipet solution down the sides of the vial. DO NOT VORTEX sample. Store reconstituted material at -20°C and add 0.1% BSA for additional stability.
GDF-5 is expressed in long bones during embryonic development and postnatally in articular cartilage. Mutations in the GDF-5 gene have been implicated in Hunter-Thompson type dwarfism and in Grebe Syndrome, which is characterized by short stature, extra digits, and short and deformed extremities. The mature and functional form of GDF-5 is a homodimer of two 120 amino-acid polypeptide chain (monomers) linked by a single disulfide bond. Each GDF-5 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 27 amino acid signal peptide and a 354 amino acid propeptide. This precursor undergoes intracellular dimerization, and upon secretion it is processed by a furin-type protease.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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