Click-IT™ Biotin Protein Analysis Detection Kit
Click-IT™ Biotin Protein Analysis Detection Kit
Invitrogen™

Click-IT™ Biotin Protein Analysis Detection Kit

Green features
The Click-iT™ Biotin Glycoprotein Detection Kit provides the second part of a simple and robust technique to identify and characterizeRead more
Have Questions?
Catalog NumberQuantity
C333721 Kit
Catalog number C33372
Price (MXN)
-
Quantity:
1 Kit
The Click-iT™ Biotin Glycoprotein Detection Kit provides the second part of a simple and robust technique to identify and characterize glycoproteins by Western blot. In step two, after the incorporation of an azide moiety into protein glycan structures with either a Click-iT™ metabolic labeling reagent or the Click-iT™ Enzymatic Labeling system, the azide-modified glycoproteins are detected via the chemoselective ligation or click reaction between an azide and an alkyne. With this technique, detection sensitivity is in the low femptomole range and biotin-labeled samples can be detected before or after probing the Western with a primary antibody.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Detection MethodBiotin-based, Fluorescence
Green FeaturesLess hazardous
Product LineClick-iT
Product TypeBiotin Protein Analysis Detection Kit
Quantity1 Kit
Shipping ConditionRoom Temperature
Labeling TargetProteins
Label or DyeBiotin
Unit SizeEach
Contents & Storage
Store in freezer -5°C to -30°C.

Citations & References (6)

Citations & References
Abstract
Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins.
Authors:Clark PM, Dweck JF, Mason DE, Hart CR, Buck SB, Peters EC, Agnew BJ, Hsieh-Wilson LC,
Journal:J Am Chem Soc
PubMed ID:18683930
'We report an advanced chemoenzymatic labeling strategy for direct fluorescence detection of O-GlcNAc proteins in gels that facilitates proteomic studies and greatly extend the reach of existing technologies. These new tools also enable the expression and dynamics of O-GlcNAc modifications to be monitored by imaging in cells and tissues. ... More
Comparative methods for analysis of protein covalent modification by electrophilic quinoids formed from xenobiotics.
Authors:Yu B, Qin Z, Wijewickrama GT, Edirisinghe P, Bolton JL, Thatcher GR,
Journal:Bioconjug Chem
PubMed ID:19301905
'Conjugation of biotin and fluorophore tags is useful for assaying covalent protein modification. Oxidative bioactivation of selective estrogen receptor modulators (SERMs) yields reactive quinoid electrophiles that covalently modify proteins, and bioactivation is associated with carcinogenic and chemopreventive effects. Identification of the protein targets of electrophilic metabolites is of general importance ... More
Rapid temporal dynamics of transcription, protein synthesis, and secretion during macrophage activation.
Authors:Eichelbaum K, Krijgsveld J,
Journal:
PubMed ID:24396086
Macrophages provide the first line of host defense with their capacity to react to an array of cytokines and bacterial components requiring tight regulation of protein expression and secretion to invoke a properly tuned innate immune response. To capture the dynamics of this system, we introduce a novel method combining ... More
A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly.
Authors:Ohn T, Kedersha N, Hickman T, Tisdale S, Anderson P,
Journal:Nat Cell Biol
PubMed ID:18794846
Stress granules (SGs) and processing bodies (PBs) are microscopically visible ribonucleoprotein granules that cooperatively regulate the translation and decay of messenger RNA. Using an RNA-mediated interference-based screen, we identify 101 human genes required for SG assembly, 39 genes required for PB assembly, and 31 genes required for coordinate SG and ... More
Identification of structural and functional O-linked N-acetylglucosamine-bearing proteins in Xenopus laevis oocyte.
Authors:Dehennaut V, Slomianny MC, Page A, Vercoutter-Edouart AS, Jessus C, Michalski JC, Vilain JP, Bodart JF, Lefebvre T,
Journal:Mol Cell Proteomics
PubMed ID:18617508
O-Linked N-acetylglucosaminylation (O-GlcNAcylation) (or O-linked N-acetylglucosamine (O-GlcNAc)) is an abundant and reversible glycosylation type found within the cytosolic and the nuclear compartments. We have described previously the sudden O-GlcNAcylation increase occurring during the Xenopus laevis oocyte G(2)/M transition, and we have demonstrated that the inhibition of O-GlcNAc-transferase (OGT) blocked this ... More