Tinciones de gel de proteínas SYPRO™

Citas y referencias (61)

Invitrogen™

Tinciones de gel de proteínas SYPRO™

Name: Tinciones de gel de proteínas SYPRO™
SKU: S6653

La tinción de gel de proteína SYPRO Ruby es una tinción fluorescente lista para usar de alta sensibilidad para laMás información

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Número de catálogo	Color	Cantidad
S6653	Rojo	500 μl
S6650	Naranja	500 μl
S6651	Naranja	10 x 50 μl
S12010	Mandarina	500 μl
S6654 también denominado S-6654	Rojo	10 x 50 μl
S12001	Rubí	200 ml
S12000	Rubí	1 l
S21900	Rubí	5 l

8 opciones

Número de catálogo S6653

Precio (MXN)

Color:

Rojo

Cantidad:

500 μl

Pedido a granel o personalizado

La tinción de gel de proteína SYPRO Ruby es una tinción fluorescente lista para usar de alta sensibilidad para la detección de proteínas totales separadas por la electroforesis en gel de poliacrilamida (PAGE). Ideal para usar en la PAGE 1D y 2D. La sensibilidad de la tinción de gel SYPRO Ruby es comparable o superior a las mejores técnicas de tinción de plata Las proteínas teñidas se pueden ver con un transiluminador de luz azul o UV estándar o con un equipo de adquisición de imágenes que contenga los filtros o láseres adecuados.

Características:
• Procedimiento de tinción sencillo: no es necesaria la decoloración ni los pasos sincronizados
• Rango de cuantificación lineal a lo largo de tres órdenes de magnitud
• Compatibilidad con espectrometría de masas y microsecuenciación.

Compare todas las tinciones fluorescentes ›

Para uso exclusivo en investigación.No apto para uso en procedimientos diagnósticos.

Especificaciones

Concentración5000X en DMSO

Ubicación de detecciónDetección en gel

Método de detecciónFluorescencia

Excitación/emisión300, 550/630 nm

Línea de productosSYPRO

Tipo de productoTinción para geles de proteínas

Cantidad500 μl

Condiciones de envíoTemperatura ambiente

Molécula dianaproteína

ColorRojo

Etiqueta o tinteSYPRO Red

Unit SizeEach

Contenido y almacenamiento

Almacenar a temperatura ambiente y proteger de la luz.

Preguntas frecuentes

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.

Citations & References (61)

Citations & References

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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