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引用資料與參考文獻 (18)
Invitrogen™
Multiplexed Proteomics™ Phosphoprotein Gel Stain Kits (with Pro-Q™ Diamond and SYPRO™ Ruby Gel Stains)
Our new Pro-Q Diamond Phosphoprotein Gel Stain provides a convenient method for selectively staining phosphoproteins in acrylamide gels, without the need for blotting or phosphoprotein-specific antibodies and western blot analysis.
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變更視圖
| 產品號碼 | Quantity |
|---|---|
| M33306 | 1 Set, 200 mL per Dye |
| M33305 | 1 Set, 1 L per Dye |
產品號碼 M33306
價格 (TWD)
8,820.00
Online offer
Ends: 31-Mar-2026
12,600.00您節省 3,780.00 (30%)
Each
Quantity:
1 Set, 200 mL per Dye
價格 (TWD)
8,820.00
Online offer
Ends: 31-Mar-2026
12,600.00您節省 3,780.00 (30%)
Each
Our new Pro-Q Diamond Phosphoprotein Gel Stain provides a convenient method for selectively staining phosphoproteins in acrylamide gels, without the need for blotting or phosphoprotein-specific antibodies and western blot analysis. This reagent, when combined with our total protein stain, SYPRO Ruby Protein Gel Stain, becomes a powerful combination for quantitative proteome analysis.
Our new Pro-Q Diamond Phosphoprotein Gel Stain provides a convenient method for selectively staining phosphoproteins in acrylamide gels, without the need for blotting or phosphoprotein-specific antibodies and western blot analysis. This reagent, when combined with our total protein stain, SYPRO Ruby Protein Gel Stain, becomes a powerful combination for quantitative proteome analysis. This convenient Pro-Q Diamond Phosphoprotein Gel Stain and SYPRO Ruby Protein Gel Stain Pack provides each stain in 1-liter amounts (Cat. No. M-33305) or in 200-mL amounts (Cat. No. M-33306).
Features include:
• Sensitive—Pro-Q Diamond Phosphoprotein Gel Stain offers detection level down to 1–16 ng of phosphoprotein per band
• Convenient—selectively stain phosphoproteins in acrylamide gels, without the need for blotting or phosphoprotein-specific antibodies and western blot analysis. SYPRO Ruby Gel Stain is subsequently used for total protein staining and simplifies the determination of phosphorylation level
• Linear signal—quantify with ease as Pro-Q Diamond Phosphoprotein Gel Stain and SYPRO Ruby Gel Stain exhibit excellent linearity over three orders of magnitude, ideal for quantitation
Features include:
• Sensitive—Pro-Q Diamond Phosphoprotein Gel Stain offers detection level down to 1–16 ng of phosphoprotein per band
• Convenient—selectively stain phosphoproteins in acrylamide gels, without the need for blotting or phosphoprotein-specific antibodies and western blot analysis. SYPRO Ruby Gel Stain is subsequently used for total protein staining and simplifies the determination of phosphorylation level
• Linear signal—quantify with ease as Pro-Q Diamond Phosphoprotein Gel Stain and SYPRO Ruby Gel Stain exhibit excellent linearity over three orders of magnitude, ideal for quantitation
For Research Use Only. Not for use in diagnostic procedures.
規格
DescriptionMultiplexed Proteomics™ Phosphoprotein Gel Stain Kit #2
Detection LocationIn-Gel Detection
Detection MethodFluorescence
Product LinePRO-Q, SYPRO
Product TypePhosphoprotein Gel Stain Kit
Quantity1 Set, 200 mL per Dye
Shipping ConditionRoom Temperature
Target MoleculeProteins (Phosphoproteins)
Label or DyeSYPRO Ruby, Pro-Q Diamond
Unit SizeEach
內容物與存放
• Pro-Q Diamond Phosphoprotein Gel Stain, 200 mL
• SYPRO Ruby Protein Gel Stain, 200 mL
Store at room temperature and protect from light.
• SYPRO Ruby Protein Gel Stain, 200 mL
Store at room temperature and protect from light.
引用資料與參考文獻 (18)
引用資料與參考文獻
Abstract
Initial analysis of the phosphoproteome of Chinese hamster ovary cells using electrophoresis.
Journal:J Biomol Tech
PubMed ID:15585821
'Protein phosphorylation is a common post-translational modification of enormous biological importance. Analysis of phosphorylation at the global level should shed light on the use of this modification to regulate metabolism, signal transduction, and other processes. We have begun a proteomic analysis of phosphorylation using two-dimensional gel electrophoresis. Chinese hamster ovary
Comparative proteomes of the proliferating C(2)C(12) myoblasts and fully differentiated myotubes reveal the complexity of the skeletal muscle differentiation program.
Journal:Mol Cell Proteomics
PubMed ID:15286212
'When cultured in low serum-containing growth medium, the mouse C(2)C(12) cells exit cell cycle and undergo a well-defined program of differentiation that culminates in the formation of myosin heavy chain-positive bona fide multinucleated muscle cells. To gain an understanding into this process, we compared total, membrane- and nuclear-enriched proteins, and
Characterization of dynamic and steady-state protein phosphorylation using a fluorescent phosphoprotein gel stain and mass spectrometry.
Journal:Electrophoresis
PubMed ID:15300772
'Protein phosphorylation plays a vital role in the regulation of most aspects of cellular activity, being key to propagating messages within signal transduction pathways and to modulating protein function. Pro-Q Diamond phosphoprotein gel stain is suitable for the fluorescence detection of phosphoserine-, phosphothreonine-, and phosphotyrosine-containing proteins directly in sodium dodecyl
Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics.
Journal:Nat Cell Biol
PubMed ID:15580268
Cofilin is a key regulator of actin cytoskeletal dynamics whose activity is controlled by phosphorylation of a single serine residue. We report the biochemical isolation of chronophin (CIN), a unique cofilin-activating phosphatase of the haloacid dehalogenase (HAD) superfamily. CIN directly dephosphorylates cofilin with high specificity and colocalizes with cofilin in
Determination of in vivo protein phosphorylation in photosynthetic membranes.
Journal:Methods Mol Biol
PubMed ID:19083170
Light- and redox-controlled reversible phosphorylation of thylakoid proteins regulates short- and long-term acclimation of plants to environmental cues. The major phosphoproteins in thylakoids belong to photosystem II and its light-harvesting antenna but phosphorylation of subunits of other thylakoid protein complexes has been detected as well. The detection methods include electrophoretic