Recombinant Human Platelet-derived Growth Factor-BB GMP

Source Escherichia coli.

Molecular Weight Approximately 24.8 kDa, a disulfide-linked homodimeric protein containing two 110 amino acid residues polypeptide (B chain).

AA Sequence MSLGSLTIAE PAMIAECKTR TEVFEISRRL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRPTQVQLRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETVAAARPVT

Purity > 98 % by SDS-PAGE and HPLC analyses.

Biological Activity Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 3 ng/ml, corresponding to a specific activity of > 3.3 × 105 IU/mg.

Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.

Endotoxin Less than 0.01 EU/μg of rHuPDGF-BB GMP as determined by LAL method.

Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.

12 months from date of receipt, -20 to -70 °C as supplied.

1 month, 2 to 8 °C under sterile conditions after reconstitution.

3 months, -20 to -70 °C under sterile conditions after reconstitution.

Usage This GMP product can be for research use or further manufacturing use.

Quality statement The manufacture and testing of this product is in compliance with ICH Q7a guidelines.

Reference 1. Hart CE, Bailey M, Curtis DA, et al. 1990. Biochemistry, 29: 166-72.

2. Heidaran MA, Yu JC, Jensen RA, et al. 1992. J Biol Chem, 267: 2884-7.

3. Haber M, Cao Z, Panjwani N, et al. 2003. Vet Ophthalmol, 6: 211-7.

4. Matei D, Kelich S, Cao L, et al. 2007. Cancer Biol Ther, 6: 1951-9.

5. Chung R, Foster BK, Zannettino AC, et al. 2009. Bone, 44: 878-85.

6. Sufen G, Xianghong Y, Yongxia C, et al. 2011. Cell Biol Int, 35: 545-51.

Background Platelet-derived growth factor (PDGF) presenting in serum but absent from plasma was first discovered in animal study by Lynch and co-workers in the late 1980s. It is a disulfide-linked dimer consisting of two peptides-chain A and chain B. PDGF has three subforms: PDGF-AA, PDGF-BB, PDGF-AB. It is involved in a number of biological processes, including hyperplasia, embryonic neuron development, chemotaxis, and respiratory tubule epithelial cell development. The function of PDGF is mediated by two receptors (PDGFR-α and PDGFR-β).