Recombinant Equine PDGF-BB Protein 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 5-30 ng/mL. |
Source |
E. coli-derived equine PDGF-BB protein Ser51-Thr159 |
Accession # |
|
N-terminal Sequence |
Ser51 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE with silver staining |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
12 kDa. 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. |
SDS-PAGE |
12 kDa, reducing conditions |
Packaging, Storage & Formulations
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.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein. |
Purity |
>95%, by SDS-PAGE with silver staining |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in 4 mM HCl. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Equine PDGF-BB Protein
Background
Platelet-Derived Growth Factor (PDGF)-BB is synthesized as a prepro-precurser that contains a signal peptide, an N-terminal prodomain, a mature region, and a
C-terminal prodomain (1-4). The proprecursor is initially dimerized and then intracellulary processed twice. The N-terminal prodomain is cleaved first, followed by cleavage of the C-terminal prodomain prior to the formation of a disulfide-linked homodimer. Mature equine PDGF-B shares 95%, 88%, 89%, 83%, 79%, and 79% amino acid sequence identity with human, mouse, rat, sheep, cow, and goat PDGF-B, respectively. 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 (8, 10). Equine PDGF-BB has been shown to stimulate contraction of fibroblast-populated collagen matrix, a model of equine wound contraction, in a Rho kinase- and p38-dependent manner (12). PDGF-BB is present in platelet-rich plasma (PRP), which has been used to treat soft tissue injuries in horses (13, 14). The levels of equine PDGF-BB in PRP is dependent on breed, gender, and age (15).
- 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.
- Watts, E.J. and M.T. Rose (2010) Domest. Anim. Endocrinol. 38:253.
- Boswell, S.G. et al. (2014) Am. J. Sports Med. 42:42.
- Halper, J. (2014) Adv. Exp. Med. Biol. 802:59.
- Giraldo, C.E. et al. (2013) BMC Vet. Res. 9:29.
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