SYPRO™ Protein Gel Stains

Citations & References (61)

Invitrogen™

SYPRO™ Protein Gel Stains

Name: SYPRO™ Protein Gel Stains
SKU: S6653

SYPRO Rubyタンパク質ゲル染色剤は、高感度ですぐに使用可能な蛍光染色剤で、ポリアクリルアミドゲル電気泳動（PAGE）によって分離されたタンパク質を検出に使用します。1Dおよび2D PAGEでの使用に最適です。SYPRO Rubyゲル染色剤の感度は詳細を見る

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製品番号（カタログ番号）	色	数量
S6653	Red	500 μL
S6650	Orange	500 μL
S6651	Orange	10x50 μL
S12010	Tangerine	500 μL
S6654 または、製品番号S-6654	Red	10x50 μL
S12001	Ruby	200 mL
S12000	Ruby	1 L
S21900	Ruby	5 L

8 オプション

製品番号（カタログ番号） S6653

価格（JPY）

66,600

Each

お問い合わせください ›

色:

Red

数量:

500 μL

一括またはカスタム形式をリクエストする

SYPRO Rubyタンパク質ゲル染色剤は、高感度ですぐに使用可能な蛍光染色剤で、ポリアクリルアミドゲル電気泳動（PAGE）によって分離されたタンパク質を検出に使用します。1Dおよび2D PAGEでの使用に最適です。SYPRO Rubyゲル染色剤の感度は、最適な銀染色法と同等以上です。染色したタンパク質は、適切なフィルターまたはレーザーを含む標準的なUVまたは青色光トランスイルミネーターまたはイメージング装置で確認できます。

特長：
•シンプルな染色手順—脱色または時間的制約のあるステップは不要です
• 3桁にわたる線形定量範囲
• 質量分析およびマイクロシーケンシングに適合しています

すべての蛍光染色の比較 ›

研究用途にのみご使用ください。診断目的には使用できません。

仕様

濃度5000X in DMSO

検出位置ゲル内検出

検出法蛍光

励起／発光300、550/630 nm

製品ラインSYPRO

製品タイプタンパク質ゲル染色

数量500 μL

出荷条件室温

標的分子タンパク質

色Red

標識または色素SYPRO レッド

Unit SizeEach

組成および保存条件

室温で保存し、光から保護します。

よくあるご質問（FAQ）

If I increase the final concentration of my SYPRO Orange or SYPRO Red staining solution above 1X, can I increase the signal of my stained proteins?

No. Dye concentrations higher than 1X do not give better detection. Instead, background fluorescence increases and, as the dye concentration increases, the dye becomes self-quenching and the signal actually decreases.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

Can I dry my SYPRO Ruby, SYPRO Orange, or SYPRO Red stained gels?

Gels stained with SYPRO dyes can be dried between sheets of cellophane, although there is sometimes a slight decrease in sensitivity. If the gels are dried onto paper, the light will scatter and the sensitivity will decrease. Other plastics are not recommended, as the plastic typically used is not transparent to UV light.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

Can I pre-stain proteins with SYPRO Ruby, SYPRO Orange or SYPRO Red Protein Gel Stains and then run them through a gel?

No. Loading solutions contain so much SDS that SYPRO Ruby, SYPRO Orange and SYPRO Red dyes simply localize in the free SDS and bind very little of the proteins. Proteins can be covalently pre-labeled with ATTO-TAG CBQCA (Cat. No. A2333), DDAO succinimidyl ester (Cat. No. C34553) or TAMRA-succinimidyl ester (Cat. No. C2211) dyes, or the TC-FLAsH Expression Analysis Detection Kits (Cat. No. A10067 for orange fluorescence, Cat. No. A10068 for red fluorescence) prior to electrophoresis without affecting protein migration through the gel.

SYPRO Orange or SYPRO Red Protein Gel Stain can be diluted 5000-fold into the cathode (upper) buffer tank to stain proteins during electrophoresis without affecting migration. The problem with doing this is that there is considerable background fluorescence in the gels from the dye interacting with SDS. This can be reduced after electrophoresis by destaining in 7.5% acetic acid for 15-60 minutes. This method also results in poorer protein sensitivity than the standard post-staining method, requires the same amount of time before the gel can be imaged, and contaminates the electrophoresis apparatus.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

引用および参考文献 (61)

引用および参考文献

Abstract

Design and characterization of a compact dual channel virus counter.

Authors:Stoffel CL,Kathy RF,Rowlen KL

Journal:Cytometry. Part A : the journal of the International Society for Analytical Cytology

PubMed ID:15830378

Adenosine to inosine editing by ADAR2 requires formation of a ternary complex on the GluR-B R/G site.

Authors:Jaikaran DC, Collins CH, MacMillan AM

Journal:J Biol Chem

PubMed ID:12163487

'RNA editing by members of the ADAR (adenosine deaminase that acts on RNA) enzyme family involves hydrolytic deamination of adenosine to inosine within the context of a double-stranded pre-mRNA substrate. Editing of the human GluR-B transcript is catalyzed by the enzyme ADAR2 at the Q/R and R/G sites. We have ... More

Defining the SNARE complex binding surface of alpha-SNAP: implications for SNARE complex disassembly.

Authors:Marz KE, Lauer JM, Hanson PI

Journal:J Biol Chem

PubMed ID:12730228

'N-Ethylmaleimide-sensitive factor (NSF) and its adaptor protein alpha-soluble NSF attachment protein (alpha-SNAP) sustain membrane trafficking by disassembling soluble NSF attachment protein receptor (SNARE) complexes that form during membrane fusion. To better understand the role of alpha-SNAP in this process, we used site-directed mutagenesis to identify residues in alpha-SNAP that interact ... More

Involvement of DnaE, the second replicative DNA polymerase from Bacillus subtilis, in DNA mutagenesis.

Authors:Le Chatelier E, Bécherel OJ, d'Alençon E, Canceill D, Ehrlich SD, Fuchs RP, Jannière L

Journal:J Biol Chem

PubMed ID:14593098

'In a large group of organisms including low G + C bacteria and eukaryotic cells, DNA synthesis at the replication fork strictly requires two distinct replicative DNA polymerases. These are designated pol C and DnaE in Bacillus subtilis. We recently proposed that DnaE might be preferentially involved in lagging strand ... More

Dynamics of myo1c (myosin-ibeta ) lipid binding and dissociation.

Authors:Tang N, Lin T, Ostap EM

Journal:J Biol Chem

PubMed ID:12221091

'Myosin-I is the single-headed member of the myosin superfamily that associates with lipid membranes. Biochemical experiments have shown that myosin-I membrane binding is the result of electrostatic interactions between the basic tail domain and acidic phospholipids. To better understand the dynamics of myosin-I membrane association, we measured the rates of ... More

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