Identify and characterize myristylated proteins with Click-iT® myristic acid, azide using the powerful click chemistry, a simple and robust two-stepRead more
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Catalog Number
Quantity
C10268
1 mg
Catalog number C10268
Price (MXN)
-
Quantity:
1 mg
Identify and characterize myristylated proteins with Click-iT® myristic acid, azide using the powerful click chemistry, a simple and robust two-step labeling and detection technique. In step one, the azide-containing biomolecule is fed to cells or animals and actively incorporated into proteins. Unlike other labels such as biotin or a fluorescent dye, the azide-tag is small enough that the tagged molecule is an acceptable substrate for the enzymes that incorporate this building block into proteins. Detection utilizes the chemoselective ligation or “click" reaction between and azide and an alkyne where the modified protein is detected with the corresponding alkyne-containing dye or hapten using either the Click-iT® Cell Reaction Buffer Kit or the Click-iT® Protein Buffer Kit. With the Click-iT® Cell Reaction Buffer Kit, cells can be analyzed by fluorescence microscopy, flow cytometry or high-content imaging and analysis (HCS) together with other biomarkers of interest for content and context rich results. With the Click-iT® Protein Reaction Buffer Kit, achieve detection sensitivity in 1-D gels and western blots in the low femtomole range or perform LC-MS⁄MS and MALDI MS analysis.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
FormatSolid
Labeling MethodMetabolic Labeling
Product LineClick-iT, Molecular Probes
Product TypeMyristic Acid
Quantity1 mg
Shipping ConditionRoom Temperature
Labeling TargetProteins, Proteins
Label or DyeAzide
Unit SizeEach
Contents & Storage
Store at ≤-20°C, desiccated and protected from light.
Citations & References (4)
Citations & References
Abstract
Chemical probes for the rapid detection of Fatty-acylated proteins in Mammalian cells.
'New tools are needed to further our understanding of protein fatty acylation. Here we demonstrate that omega-azido fatty acids can be efficiently metabolized by mammalian cells and serve as selective probes to rapidly visualize N-myristoylation and S-acylation, respectively. In addition to the more sensitive detection of fatty-acylated proteins with these ... More
Dynamic monitoring of newly synthesized proteomes: up-regulation of myristoylated protein kinase A during butyric acid induced apoptosis.
Authors:Liu K, Yang PY, Na Z, Yao SQ,
Journal:Angew Chem Int Ed Engl
PubMed ID:21678537
Doubly charged: A double metabolic incorporation approach capable of proteome-wide profiling of post-translational modification dynamics on newly synthesized proteins has been developed (see scheme; blue box: methionine surrogate, orange diamond: PTM probe). This strategy reveals for the first time that up-regulation of myristoylated PKA protein is necessary for the occurrence ... More
Lipid raft-dependent endocytosis of close homolog of adhesion molecule L1 (CHL1) promotes neuritogenesis.
Authors:Tian N, Leshchyns'ka I, Welch JH, Diakowski W, Yang H, Schachner M, Sytnyk V,
Journal:J Biol Chem
PubMed ID:23144456
CHL1 plays a dual role by either promoting or inhibiting neuritogenesis. We report here that neuritogenesis-promoting ligand-dependent cell surface clustering of CHL1 induces palmitoylation and lipid raft-dependent endocytosis of CHL1. We identify ßII spectrin as a binding partner of CHL1, and we show that partial disruption of the complex between ... More
Robust fluorescent detection of protein fatty-acylation with chemical reporters.
Authors:Charron G, Zhang MM, Yount JS, Wilson J, Raghavan AS, Shamir E, Hang HC,
Journal:J Am Chem Soc
PubMed ID:19281244
Fatty-acylation of proteins in eukaryotes is associated with many fundamental cellular processes but has been challenging to study due to limited tools for rapid and robust detection of protein fatty-acylation in cells. The development of azido-fatty acids enabled the nonradioactive detection of fatty-acylated proteins in mammalian cells using the Staudinger ... More