Recombinant Human GDF-5 (BMP-14/CDMP-1)
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. Recombinant Human GDF-5 is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains.
Above 98% as determined by SDS-PAGE Analysis.
The ED50 was determined by its ability to induce alkaline phosphatase production by ATDC-5 chondrogenic cells is 1.0-2.0 µg/ml.
APLATRQGK RPSKNLKAR CSRKALHVN FKDMGWDDW IIAPLEYEA FHCEGLCEF PLRSHLEPT NHAVIQTLM NSMDPESTP PTCCVPTRL SPISILFID SANNVVYKQ YEDMVVESC GCR
|Research Interest:||Stem Cell Research|
|Cell Type:||Stem Cells|
|Protein Cross Reactivity:||Mouse|