# | Product Name | Applications | Reactivity | |
---|---|---|---|---|
42028 | Human PDGF-AA Recombinant Protein |
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Product Information
MW (kDa) | 18 |
Purity | >98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hPDGF-AA. All lots are greater than 98% pure. |
Endotoxin | Less than 0.01 ng endotoxin/1 μg hPDGF-AA. |
Activity | The bioactivity of recombinant hPDGF-AA was determined in a NIH/3T3 proliferation assay. The ED50 of each lot is between 4-12 ng/ml. |
Molecular Formula | Recombinant hPDGF-AA does not have a Met on the amino terminus and has a calculated MW of 14,305. DTT-reduced protein migrates as an 18 kDa polypeptide and the non-reduced cystine-linked homodimer migrates as a 34 kDa protein. The expected amino-terminal SIEEA of recombinant hPDGF-AA was verified by amino acid sequencing. |
Recombinant human PDGF-AA (hPDGF-AA) Ser87-Thr211 (Accession #NP_002598) was produced in E. coli at Cell Signaling Technology.
PDGF-AA is integrally involved in embryonic development, angiogenesis and organogenesis and induces fibroblast proliferation and migration (1,2). PDGF-AA is produced by epithelial, muscle, osteosarcoma and neuronal progenitor cells (1,3). Active PDGF-AA is formed through intracellular proteolytic cleavage of a large precursor. PDGF-AA is also concentrated in the extracellular matrix through alternative splicing that generates an extended carboxy-terminal that binds components of the extracellular matrix. The carboxy-terminal stretch is removed extracellularly to generate mature PDGF-AA (1,2). PDGF-AA binding to the PDGFR-α activates the receptor tyrosine kinase (1). PDGF-AA-induced signaling is through the Ras-MAPK, PI3K/AKT and PLCγ pathways (1). Dysregulation of PDGF-AA expression and/or signaling is often associated with cancer and fibrotic disorders (1).
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