Technical Data
Platelet Derived Growth Factor AA, Recombinant, Human (PDGF-AA)
Molecular Biology Storage: -20CShipping: RT
PDGFs are disulfide-linked dimers consisting of two 12.0-13.5kD polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs. (PDGF-AA, PDGF-BB and PDGF-AB) are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet alpha-granules and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB. PDGF is released when platelets adhere to traumatized tissues. Connective tissue cells near the traumatized region respond by initiating the process of replication.The synthesis of PDGF can be induced by Interleukin-1, Interleukin-6, TNF-alpha, TGF-beta and EGF.

Recombinant Human Platelet Derived Growth Factor-AA is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 125 amino acids and having a total molecular mass of 28511 Dalton.

The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ser-Ile-Glu-Glu.

Dimers and Aggregates:
1% as determined by silver-stained SDS-PAGE gel analysis.

Biological Activity:
PDGF-AA is fully biologically active when compared to standard. The ED50, calculated by the dose-dependent proliferation of murine BALB/c 3T3 indicator cells (measured by 3H-thymidine uptake) is < 1ng/ml, corresponding to a Specific Activity of 1MIU/mg.

0.1ng/ug (IEU/ug) of PDGF-AA.

Protein Content:
Protein quantitation was carried out by two independent methods:
1. UV spectroscopy at 280nm using the absorbency value of 0.55 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
2. Analysis by RP-HPLC, using a standard solution of PDGF-AA as a Reference Standard.

Reconstitute the lyophilized PDGF-AA in sterile 18M-cm H2O not less than 100ug/ml, which can then be further diluted to other aqueous solutions.

Storage and Stability:
Lyophilized powder may be stored at 4C for short-term only. Reconstitute to nominal volume by adding sterile dH2O and store at -20C. Reconstituted product is stable for 12 months at -20C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer.

Also Available:
P4258: Platelet Derived Growth Factor AA, Recombinant, Human (PDGF-AA)
P4258-01: Platelet Derived Growth Factor AA, Recombinant, Human (PDGF-AA)
P4258-01A: Platelet Derived Growth Factor AA, Recombinant, Human (PDGF-AA)
P4258-03: Platelet Derived Growth Factor AA, Recombinant, Human (PDGF-AA) Mab Mo xHu
P4258-04: Platelet Derived Growth Factor AA (PDGF-AA) Pab Rb xHu
P4258-04A: Platelet Derived Growth Factor AA (PDGF-AA) (Biotin) Pab Rb xHu
P4258-14: Platelet Derived Growth Factor AA (PDGF-AA) (Biotin) Pab Rb xHu
P4258-16A: Platelet Derived Growth Factor AA (PDGF-AA) Pab Rb xHu
P4258-19: Platelet Derived Growth Factor AA,AB,BB Neutralizing (PDGF-AA,AB,BB) Pab Gt xHu
Source: E. coli
Purity: 95% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified.
Concentration: ~0.1mg/ml
Form: Supplied as a lyophilized powder. No additives.

Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
1. IL-13 and IL-1beta promote lung fibroblast growth through coordinated up-regulation of PDGF-AA and PDGF-Ralpha. Ingram JL, Rice AB, Madtes DK, FASEB J 2004 Jul;18(10):1132-4 2. Influence of hormones and growth factors on lens protein composition: the effect of dexamethasone and PDGF-AA. Vinader LM, van Genesen ST, Lubsen NH, Mol Vis 2003 Dec 18;9:723-9 3. Role for TGF-beta1, FGF-2 and PDGF-AA in a myelination of CNS aggregate cultures enriched with macrophages. Diemel LT, Jackson SJ, J Neurosci Res 2003 Dec 15;74(6):858-67 4. Different mechanisms influencing permeation of PDGF-AA and PDGF-BB across the blood-brain barrier. Kastin AJ, Akerstrom V, Pan W, J Neurochem 2003 Oct;87(1):7-12 5. Expression of TGF-beta and PDGF-AA antigens and corresponding mRNAs in cytomegalovirus-infected rat kidney allografts. Inkinen K, Holma K, Krogerus L, Lautenschlager I, Transplant Proc 2003 Mar;35(2):804-5 6. A2B5+ and O4+ Cycling progenitors in the adult forebrain white matter respond differentially to PDGF-AA, FGF-2, and IGF-1. Mason JL, Goldman JE, Mol Cell Neurosci 2002 May;20(1):30-42.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.