PDGFR?/CD140a (human, recombinan

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PDGFR?/CD140a (human, recombinant)

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Cat No: 31843

Proteins - Enzymes

PDGFRα, also known as CD140a, is a type I transmembrane glycoprotein and receptor tyrosine kinase.{54656,60401} It is composed of five extracellular immunoglobulin-like (Ig-like) domains, a transmembrane domain, and an intracellular kinase domain. PDG...

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Territorial Availability: Available through Bertin Technologies only in France

Correlated keywords:

PDGFR-? CD140-a PDGFAA PDGFCC PDGFBB PDGFAB FIP1L-1 FIP-1L1 di-sulfide IgG-1

Product Overview:
PDGFRα, also known as CD140a, is a type I transmembrane glycoprotein and receptor tyrosine kinase.{54656,60401} It is composed of five extracellular immunoglobulin-like (Ig-like) domains, a transmembrane domain, and an intracellular kinase domain. PDGFRα is widely expressed and functions as a homodimer or a heterodimer with PDGFRβ.{60401} Binding of the growth factor PDGF-AA or PDGF-CC induces homodimerization, while binding of PDGF-BB or PDGF-AB can induce either homodimerization or heterodimerization with PDGFRβ.{54656} In each case, binding of the ligands induces receptor autophosphorylation and a conformational change that facilitates access to the intracellular kinase domain and intracellular signaling through multiple pathways, including ERK/MAPK, PI3K/AKT/mTOR, PLC/PKC, and JAK/STAT.{54656,60401} Activating point mutations in PDGFRA, the gene encoding PDGFRα, are associated with gastrointestinal stromal tumors.{60401} PDGFRα can also fuse with FIP1L1, and the fusion protein has been found in patients with idiopathic hypereosinophilia. Cayman’s PDGFRα/CD140a (human, recombinant) protein can be used for binding activity assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of PDGFRα (amino acids 24-524) fused to human IgG1 Fc at its C-terminus, consists of 739 amino acids and has a calculated molecular weight of 82.9 kDa. As a result of glycosylation, the monomer migrates at approximately 120-130 kDa by SDS-PAGE under reducing conditions.

Size	100 µg
Shipping	dry ice
Formulation	Lyophilized from sterile PBS, pH 7.4
Purity	≥90% estimated by SDS-PAGE
Custom Code	3504.00
UNSPSC code	12352204

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Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.