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LCAT Blocking Peptide

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Cat No: 10009324
Cayman
€141.00
Price is excluding VAT and does not include packaging neither shipping

Amino acids: Human LCAT protein amino acids 132-143 · To be used in conjunction with Cayman’s LCAT Polyclonal Antibody (Item No. 10009323) to block protein-antibody complex formation during immunochemical analysis of LCAT
To be used in conjunction with...

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: 1 ea

This product can only be bought through Cayman Chemical. Please contact us.

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Territorial Availability: Available through Bertin Technologies only in Europe
Product Overview:
Amino acids: Human LCAT protein amino acids 132-143 · To be used in conjunction with Cayman’s LCAT Polyclonal Antibody (Item No. 10009323) to block protein-antibody complex formation during immunochemical analysis of LCAT
To be used in conjunction with Cayman’s LCAT Polyclonal Antibody (Item No. 10009323) to block protein-antibody complex formation during immunochemical analysis of LCAT. · Lecithin:cholesterol acyltransferase (LCAT) has both phospholipase and acyltransferase activities. LCAT catalyzes the fatty acid transfer from the sn-2 position of phosphatidylcholine (lecithin) to cholesterol and to a lesser degree to other acceptor molecules. This enzyme is critical to the process of reverse cholesterol transport or movement of cholesterol esters into high density lipoprotein (HDL) particles from cells. LCAT is abundant in blood-plasma, however it is present in other fluids and tissues such as ovary. This protein may be detected on immunoblot at 49.5 kDa as well as at 66 kDa when fully glycosylated. Plasma samples should be diluted prior to electrophoresis and immunoblotting to avoid the band-broadening effect caused by comigration with endogenous albumin.
Size: 1 ea
Shipping: wet ice
Stability: Store at -20 degrees; shelf life 365 days maximum after production
Formulation: 200 µg of peptide in 200 µl TBS containing 0.1% BSA and 0.02% sodium azide
Custom Code: 3504005000
UNSPSC code: 41105329

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.

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