Platelet Derived Growth Factor-AA Recombinant Protein | PDGFAA recombinant protein

Human Platelet Derived Growth Factor-AA Recombinant

Cat. Num. AAA553119

• Purity: >98%, as determined by SDS-PAGE and HPLC
• Synonyms: Platelet Derived Growth Factor-AA; Human Platelet Derived Growth Factor-AA Recombinant; Human PDGFAA Recombinant; pdgf-aa; platelet derived growth factor; PDGFAA recombinant protein

• Host: E Coli
• Purity/Purification: >98%, as determined by SDS-PAGE and HPLC
• Form/Format: Recombinant PDGF-AA was lyophilized from a 0.2 um filtered PBS solution pH 7.0.
• Sequence: MRTLACLLLL GCGYLAHVLA EEAEIPREVI ERLARSQIHS IRDLQRLLEI DSVGSEDSLD TSLRAHGVHA TKHVPEKRPL PIRRKRSIEE AVPAVCKTRT VIYEIPRSQV DPTSANFLIW PPCVEVKRCT GCCNTSSVKC QPSRVHHRSV KVAKVEYVRK KPKLKEVQVR LEEHLECACA TTSLNPDYRE EDTGRPRESG KKRKRKRLKP T
• Sequence Length: 211

• Domain: Cystine knot growth factor
• Host Note: Optimized DNA sequence encoding Human PDGF-AA mature chain was expressed in Escherichia Coli.
• Endotoxin: Endotoxin content was assayed using a LAL gel clot method.; Endotoxin level was found to be less than 0.1 ng/ug (1EU/ug).
• Reconstitution: A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
• Molecular Weight Note: Human PDGF-AA, is generated by the proteolytic removal of the signal peptide; and propeptide. The molecule has a calculated molecular mass of approximately 28 kDa.; ; Recombinant PDGF-AA is a disulfide-linked homodimeric protein consisting of two 126 amino acid residue subunits, migrates as an approximately 28 kDa protein under non-reducing and as 14kDa under reducing conditions in SDS-PAGE.
• Preparation and Storage: The lyophilized protein is stable for at least 2 years from date of receipt at -20 degree C.; Upon reconstitution, this cytokine can be stored in working aliquots at 2 degree - 8 degree C for one month, or at -20 degree C for six months, with a carrier protein without detectable loss of activity. ; ; Avoid repeated freeze/thaw cycles.

Related Product Information for PDGFAA recombinant protein

PDGF is synthesized mainly by megakaryocytes. It is stored in the alpha granules of platelets from which it is released after cell activation of platelets. Platelets synthesize a mixture of the three possible isoforms (BB,AB,AA) while fibroblasts stimulated with EGF synthesize AA homodimers. PDGF receptors are expressed in fibroblasts, osteoblasts, chondroblasts, smooth muscle cells, glial cells, and endothelial cells.Two related receptors, are PDGFRalpha (CD140a) or PDGFRbeta (CD140b).In contrast to many other cytokines PDGF is not released into the circulation. PDGF binds to several plasma proteins and also to proteins of the extracellular matrix which facilitates local concentration of the factor. The factor functions as a local autocrine and paracrine growth factor. In the adult organism PDGF is involved in wound healing processes. The aberrant expression of PDGF is observed with vascular proliferative diseases such as atherosclerosis. PDGF regulates the synthesis of its own receptor and also influences the expression of membrane receptors for IL1, EGF, 5-Hydroxytryptamine, LDL, transferrin, and muscarinergic receptor.

Product Categories/Family for PDGFAA recombinant protein

Cytokines

References

• pdgf receptor-β modulates metanephric mesenchyme chemotaxis induced by pdgf aa .Am J Physiol Renal Physiol, Feb 2009; 296: F406 - F417.
• persistent cytomegalovirus infection is associated with increased expression of tgf-ß1, PDGF-AA and icam-1 and arterial intimal thickening in kidney allografts .Nephrol. Dial. Transplant., Apr 2005; 20: 790 - 796.
• il-13 and il-1β promote lung fibroblast growth through coordinated up-regulation of PDGF-AA and pdgf-ralpha .FASEB J, May 2004; 10.1096/fj.03-1492fje.
• pdgf (alpha) -receptor is unresponsive to PDGF-AA in aortic smooth muscle cells from the ng2 knockout mouse .J. Cell Sci., Mar 1999; 112: 905 - 915.
• pdgf aa as mediator in nicotine-dependent carcinogenesis .Carcinogenesis, Sep 1996; 17: 1813 - 1818.