PDGFR?/CD140b Extracellular Doma

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PDGFR?/CD140b Extracellular Domain (human, recombinant)

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Cat No: 33986

Proteins - Enzymes

PDGFRβ, also known as CD140b, is a type I transmembrane glycoprotein and receptor tyrosine kinase encoded by PDGFRB in humans.{54656} It is composed of five extracellular immunoglobulin-like (Ig-like) domains, a transmembrane domain, and an intracellu...

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Territorial Availability: Available through Bertin Technologies only in France

Correlated keywords:

CD-140b PDGF-R? PDGFR-? PDGFR1 auto-phosphorylation Leu-33

Product Overview:
PDGFRβ, also known as CD140b, is a type I transmembrane glycoprotein and receptor tyrosine kinase encoded by PDGFRB in humans.{54656} It is composed of five extracellular immunoglobulin-like (Ig-like) domains, a transmembrane domain, and an intracellular kinase domain. PDGFRβ is ubiquitously expressed and functions as a homodimer or a heterodimer with PDGFRα. Binding of the growth factor PDGF-BB or PDGF-DD to PDGFRβ promotes homodimerization, 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.{54656,54657,54658} Knockdown of Pdgfrb decreases the number of vascular smooth muscle cells, induces CNS-specific reduction in pericytes, and is postnatally lethal in mice. De novo mutations in PDGFRB have been found in patients with novel overgrowth syndrome.{54659} Cayman's PDGFRβ/CD140b Extracellular Domain (human, recombinant) protein can be used for binding assays. This protein consists of 510 amino acids, has a calculated molecular weight of 57.6 kDa, and a predicted N-terminus of Leu33 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 95 to 100 kDa due to glycosylation.

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	12352203

Technical File

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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.