Recombinant Equine PDGF-BB Protein Summary
Product Specifications
Ser51-Thr159
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
8585-BB
Formulation | Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in 4 mM HCl. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
8585-BB/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in HCl. |
Reconstitution | Reconstitute at 100 μg/mL in 4 mM HCl. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: PDGF-BB
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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