Territorial Availability: Available through Bertin Technologies only in France
- Correlated keywords
- LECAM-1 CD-62L 62 Ly22 LAM-1 U-937 PSGL1 Gly-CAM-1 GlyCAM1 Trp-39 Ly-22 Ly22 lymph node homing receptor SELL
- Product Overview:
L-Selectin, also known as CD62L, is a glycoprotein and cell adhesion molecule that is encoded by the SELL gene in humans.{60879,60892} It is composed of an N-terminal calcium-dependent lectin domain that recognizes glycoproteins, an EGF-like domain, two consensus repeats, a transmembrane domain, and an intracellular C-terminal tail. L-selectin is expressed in leukocytes and localizes to the plasma membrane.{60893} It also exists as a soluble form that results from alternative splicing of SELL pre-mRNA or by ectodomain shedding via proteolytic cleavage.{60892} L-selectin facilitates leukocyte rolling on activated vascular endothelium and lymphocyte homing to high endothelial venules of lymph nodes.{60894} It binds to several glycoproteins containing the sulfated sialyl Lewis X (6-sulfo-sLeX) epitope, including P-selectin glycoprotein ligand-1 (PSGL-1) and glycosylation-dependent cell adhesion molecule-1 (GlyCAM-1).{60879} Sell-/- mice exhibit a reduction in the lymphocyte count in peripheral lymph nodes, as well as a decrease in neutrophil recruitment in a model of peritonitis induced by thioglycolate.{60894} Serum levels of soluble L-selectin are lower in patients with sepsis and associated with higher mortality.{60895} Cayman’s L-Selectin/CD62L Extracellular Domain (mouse, recombinant) protein can be used for cell-based assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of L-selectin (amino acids 1-332) fused to His-tagged human IgG1 at its C-terminus, consists of 542 amino acids, has a calculated molecular weight of 61 kDa, and a predicted N-terminus of Trp39 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 100-110 kDa by SDS-PAGE under reducing conditions.
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.