Click-IT™ Tetramethylrhodamine (TAMRA) Protein Analysis Detection Kit
Citations & References (5)
Invitrogen™
Click-IT™ Tetramethylrhodamine (TAMRA) Protein Analysis Detection Kit
The Click-iT™ Tetramethylrhodamine (TAMRA) Glycoprotein Detection Kit provides the second part of the simple and robust two-step technique to identifyRead more
Have Questions?
Catalog Number
Quantity
C33370
1 Kit
Catalog number C33370
Price (CLP)
556.690
Each
Add to cart
Quantity:
1 Kit
Price (CLP)
556.690
Each
Add to cart
The Click-iT™ Tetramethylrhodamine (TAMRA) Glycoprotein Detection Kit provides the second part of the simple and robust two-step technique to identify and characterize glycoproteins by one- or two-dimensional gel electrophoresis. In step two, after the incorporation of the azide handle 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. Gels with TAMRA labeled glycoproteins can be subsequently stained with the Multiplexed Proteomics™ technologies, SYPRO™ Ruby total protein stain and PRO-Q™ Emerald glycoprotein stain for the differential analysis of glycoprotein subclasses, total proteins and total glycoproteins in the same gel. Click-iT™ modified glycoproteins are also compatible with downstream LC-MS/MS and MALDI MS analysis for identification.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Detection MethodFluorescence
Green FeaturesLess hazardous
Labeling TargetProteins (Glycoproteins)
Label or DyeTAMRA™ Isomers, TMR (Tetramethylrhodamine)
Product TypeTAMRA Protein Analysis Detection Kit
Quantity1 Kit
Shipping ConditionRoom Temperature
Product LineClick-iT
Unit SizeEach
Contents & Storage
Store in freezer -5°C to -30°C.
Frequently asked questions (FAQs)
I am using Click-iT AHA (L-azidohomoalanine) kit to label nascent proteins in live cells, then detecting with TAMRA alkyne after fixation and permeabilization and a click reaction. But I'm seeing nucleolar labeling in the cells. It this expected?
Yes. All proteins synthesized during the time the AHA is present will be detected, and they may be all over the cell. Our imaging shows strong labeling in the nucleoli and cytoplasm, as well as nuclear labeling.
Protein synthesis in distal axons is not required for growth cone responses to guidance cues.
Authors:Roche FK, Marsick BM, Letourneau PC,
Journal:J Neurosci
PubMed ID:19158291
'Recent evidence suggests that growth cone responses to guidance cues require local protein synthesis. Using chick neurons, we investigated whether protein synthesis is required for growth cones of several types to respond to guidance cues. First, we found that global inhibition of protein synthesis stops axonal elongation after 2 h. ... More
Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins.
'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
The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase.
'Membrane-type 1 matrix metalloproteinase (MT1-MMP; MMP-14) drives fundamental physiological and pathological processes, due to its ability to process a broad spectrum of substrates. Because subtle changes in its activity can produce profound physiological effects, MT1-MMP is tightly regulated. Currently, many aspects of this regulation remain to be elucidated. It has ... More
A novel approach to tag and identify geranylgeranylated proteins.
Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.
Authors:Dias WB, Cheung WD, Wang Z, Hart GW,
Journal:J Biol Chem
PubMed ID:19506079
Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification. GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription. Here we show that calcium/calmodulin-dependent kinase IV (CaMKIV) is highly GlcNAcylated in vivo. ... More