S1P1 Blocking Peptide

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S1P₁ Blocking Peptide

Cat No: 10006616

Antibodies - Blocking Peptides

To be used in conjunction with Cayman’s S1P1 Polyclonal Antibody (Item No. 10005228) to block protein-antibody complex formation during immunochemical analysis of S1P1. Sphingosine-1-phosphate (S1P) exerts its activity by binding to five distinct G-pro...

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Territorial Availability: Available through Bertin Technologies only in France

Correlated keywords:

antibodies western blotting blots signaling signalling WB IHC ICC immunohistochemistry formalin-fixed paraffin-embedded sections immunocytochemistry receptors controls peptides proteins sphingosine-1-phosphate receptors G-protein-coupled S1P1/EDG-1 S1P2/EDG-5 S1P3/EDG-3 S1P4/EDG-6 S1P5/EDG-8

Product Overview:
To be used in conjunction with Cayman’s S1P1 Polyclonal Antibody (Item No. 10005228) to block protein-antibody complex formation during immunochemical analysis of S1P1. 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} S1P1 primarily couples with pertussis toxin-sensitive Gi/o proteins to mediate S1P-induced cell proliferation, survival, migration, cytoskeletal organization, and morphogenesis.{11895,12477,10628} Expression of S1P1 is abundant in embryological vasculature and ubiquitous in adult cells, suggesting diverse physiological functions of this receptor.{12477} The human and murine S1P1 have 382 amino acids with an estimated molecular weight of 43 kDa. Glycosylation at the N-terminal extracellular domain may cause the protein to migrate at higher position in SDS-PAGE.{12476} Cayman’s S1P1 Polyclonal Antibody detects the receptor at 47 kDa in western blot. The antibody can also be used in immunostaining to study expression patterns of this protein.

Size	1 ea
Shipping	dry ice
Formulation	200 µg peptide lyophilized from water
Custom Code	3504.00
UNSPSC code	41105329

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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.