Recombinant Human PDGF-AA, Animal-Free Protein Summary
Additional Information |
Intended for preclinical researchers who may transition to GMP PDGF-AA for their clinical work |
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 ED 50 for this effect is 50-200 ng/mL in a fluorometric assay using the redox sensitive dye, Resazurin (Catalog # AR002). |
Source |
E. coli-derived human PDGF-AA protein Ser87-Thr211, with and without an N-terminal Met Produced using non-animal reagents in an animal-free laboratory.
|
Accession # |
|
N-terminal Sequence |
Ser87 & Met |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Animal-Free Recombinant Proteins |
Gene |
PDGFA |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Purity Statement |
Antigen Affinity-purified |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
14 kDa (monomer). 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. |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. - 12 months from date of receipt, ≤ -20 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, ≤ -20 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. |
Purity |
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions |
Reconstitute at 0.2 mg/mL in sterile 4 mM HCl. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human PDGF-AA, Animal-Free Protein
Background
Platelet-derived growth factor (PDGF) was discovered as a major mitogenic factor present in serum but absent from plasma. It was found to be secreted from the alpha -granules of platelets activated during the coagulation of blood to form serum. Subsequent studies have demonstrated that PDGF is not one molecule but three, each a dimeric combination of two distinct but structurally related peptide chains designated A and B. The dimeric isoforms PDGF-AA, AB and BB are differentially expressed in various cell types and their effects are mediated through two distinct receptors, termed alpha and beta . Differences exist in isoform binding to each receptor. In general, PDGF isoforms are potent mitogens for connective tissue cells, including dermal fibroblasts, glial cells, arterial smooth muscle cells and some epithelial and endothelial cells. In addition to its activity as a mitogen, PDGF is chemotactic for fibroblasts, smooth muscle cells, neutrophils and mononuclear cells. Other reported activities for PDGF include stimulation of granule release by neutrophils and monocytes, facilitation of steroid synthesis by Leydig cells, stimulation of neutrophil phagocytosis, inhibition of natural killer (NK) cell activity, stimulation of collagen synthesis, modulation of thrombospondin expression and secretion, stimulation of collagenase activity and secretion, induction of contraction of rat aorta strips in vitro, and transient induction of T cell IL-2 secretion accompanied by a down-regulation of IL-4 and IFN-gamma production, temporary effects that may allow clonal expansion of antigen-activated B and T helper lymphocytes prior to differentiation. PDGF also appears to be ubiquitous in neurons throughout the CNS, where it is suggested to play an important role in neuron survival and regeneration, and in mediation of glial cell proliferation and differentiation.
Manufacturing Process
Animal-Free Manufacturing Conditions
Our dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.
Production
- All molecular biology procedures use animal-free media and dedicated labware.
- Dedicated fermentors are utilized in committed animal-free areas.
Purification
- Protein purification columns are animal-free.
- Bulk proteins are filtered using animal-free filters.
- Purified proteins are stored in animal-free containers in a dedicated cold storage room.
Quality Assurance
- Low Endotoxin Level.
- No impairment of biological activity.
- High quality product obtained under stringent conditions.
- For ex vivo research or bioproduction, additional documentation can be provided.
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