S1P3 Polyclonal Antibody

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S1P₃ Polyclonal Antibody

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Cat No: 10006373

Sphingosine-1-phosphate (S1P) exerts its activity by binding to five distinct G-protein-coupled receptors, S1P1/EDG-1, S1P2/EDG-5, S1P3/EDG-3, S1P4/EDG-6, and S1P5/EDG-8.{11895,12477} S1P3 couples to Gi/o-ERK, Gq-PLC, and G12/13-Rho axes to mediate S1...

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Territorial Availability: Available through Bertin Technologies only in France

Correlated keywords:

antisera antiserum immunocytochemistry FACS flow cytometry sphingosine-1-phosphates GPCRs G-protein-coupled receptors S1P1 S1P2 S1P4 S1P5 edg-1 edg-5 edg-6 edg-8 couples coupling Gi/o-ERK G12/13-Rho axes mediates proliferation survival migration singalling events expressed tissues physiological functions receptors murine glycosylation N-terminal extracellular domains proteins migrates SDS-PAGE cerbral cortex liver heart immunoblotting

Product Overview:
Sphingosine-1-phosphate (S1P) exerts its activity by binding to five distinct G-protein-coupled receptors, S1P1/EDG-1, S1P2/EDG-5, S1P3/EDG-3, S1P4/EDG-6, and S1P5/EDG-8.{11895,12477} S1P3 couples to Gi/o-ERK, Gq-PLC, and G12/13-Rho axes to mediate S1P-induced cell proliferation, survival, migration, and related signaling events.{11895,12477,10628} S1P3 is widely expressed in various tissues, suggesting diverse physiological functions of this receptor.{10623} The human and mouse S1P3 have 378 amino acids with an estimated molecular weight of 42 kDa. Glycosylation at the N-terminal extracellular domain may cause the protein to migrate at different positions in SDS-PAGE. Cayman’s S1P3 Polyclonal Antibody can be used for immunocytochemistry and Western blot applications. The antibody recognizes S1P3 at 47 kDa from human, mouse, and rat samples. Liver and heart tissues display 2-3 bands between 40-50 kDa, possibly due to different degree of glycosylation.

Size	1 ea
Shipping	dry ice
Host	Rabbit
Antigen	Synthetic peptide from the N-terminal region of human S1P3
Application(s)	ICC and WB
Formulation	Peptide affinity-purified antibody lyophilized from 500 µl
Custom Code	3822.19
UNSPSC code	12352203

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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.