Recombinant Human PDGF-BB Biotinylated Protein, CF Summary
|Details of Functionality
Measured in a cell proliferation assay using NR6R‑3T3 mouse fibroblast cells. Raines, E.W. et al. (1985) Methods Enzymol. 109:749. The ED50 for this effect is 1.5-6 ng/mL.
E. coli-derived human PDGF-BB protein
|Structure / Form
Disulfide-linked homodimer, biotinylated protein via amines
| Protein/Peptide Type
>95%, by SDS-PAGE with silver staining.
<1.0 EU per 1 μg of the protein by the LAL method.
12 kDa (monomer, unlabeled).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
12 kDa, reducing conditions
Packaging, Storage & Formulations
|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.
Lyophilized from a 0.2 μm filtered solution in HCl.
>95%, by SDS-PAGE with silver staining.
Reconstitute at 100 μg/mL in 4 mM HCl.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human PDGF-BB Biotinylated Protein, CF
Platelet-Derived Growth Factor (PDGF)-BB is synthesized as a 35 kDa, 241 amino acid (aa) prepro-precurser. It contains a signal peptide, an N-terminal prodomain, a mature region, and a C-terminal prodomain (1-4). The propercursor is initially dimerized and then intracellulary processed twice. The N-terminal prodomain is cleaved first, followed by cleavage of the C-terminal prodomain. The resulting mature region is 16-17 kDa in size (or 29-32 kDa as a homodimer) (4). Mature human PDGF-B shares 89% aa sequence identity with mouse mature PDGF-B. PDGF-BB is expressed by hepatocytes and nonresorbing osteoclasts, generating osteoblasts and bone formation (4, 5). It is also produced by platelets, macrophages, and mast cells. At sites of injury, it promotes neutrophil and macrophage infiltration for debridement, fibroblast secretion of new extracellular matrix, and IGF-I-mediated re-epithelialization (6, 7). The traditional receptor for PDGF is either a homodimer or heterodimer created from two type I transmembrane RTKs, PDGF R alpha and PDGF R beta (8, 9). PDGF-BB has been shown to bind the alpha alpha homodimer, alpha beta heterodimer, and the beta beta homodimer in vitro
, and act through the beta beta homodimer in vivo
- Rao, C.D. et al. (1986) Proc. Natl. Acad. Sci. USA 83:2392.
- Kaetzel, D.M. et al. (1996) Biochim. Biophys. Acta. 1298:250.
- Ostman, A. et al. (1992) J. Cell Biol. 118:509.
- Siegfried, G. et al. (2005) Oncogene 24:6925.
- Kreja, L. et al. (2010) J. Cell. Biochem. 109:347.
- van Steensel, L. et al. (2012) J. Clin. Endocrinol. Metab. 97:E400.
- Barrientos, S. et al. (2008) Wound Repair Regen. 16:585.
- Andrae, J. et al. (2008) Genes Dev. 22:1276.
- Heldin, C.H. and B. Westermark (1999) Physiol. Rev. 79:1283.
- Li, X. and U. Eriksson (2003) Cytokine Growth Factor Rev. 14:91.
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