- 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.
A minimum of 12 months when stored at ≤ -20 °C as supplied. Refer to lot specific COA for the Use by Date.
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).