Minicelda XCell SureLock™

Citas y referencias (11)

Invitrogen™

Minicelda XCell SureLock™

The XCell SureLock Mini-Cell is a vertical mini-protein gel electrophoresis system compatible with all Invitrogen mini precast gels and SurecastMás información

Número de catálogo	Cantidad
EI0001	1 unit

Número de catálogo EI0001

Precio (CLP)

861.387

Añadir al carro de la compra

Cantidad:

1 unit

Precio (CLP)

861.387

Añadir al carro de la compra

The XCell SureLock Mini-Cell is a vertical mini-protein gel electrophoresis system compatible with all Invitrogen mini precast gels and Surecast handcast gels. The Mini-Cell is simple, sturdy, and easy to use. Rather than using clamps, the system incorporates the use of a gel tension wedge to make setup quick and convenient.

How the system works
The XCell SureLock Mini-Cell holds gels firmly with a simple gel tension wedge. When the lever on the gel tension wedge is pushed forward into the locked position, an even, horizontal force is generated. This seals the gel/buffer core assembly firmly into position in the lower buffer chamber. The positive locking action of the gel tension wedge ensures a trouble-free, leak-free gel run every time.

The XCell SureLock Mini-Cell can be used for wet transfers using the XCell II Blot Module. The XCell II Blot Module is used in place of the gel/buffer core assembly. It requires less than 200 mL of transfer buffer for western, southern, and northern transfers. Tough platinized titanium and stainless steel electrodes create a uniform electrical field without clamps or hinged gel holders. Maximum blot size is 9 cm x 9 cm.

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

Especificaciones

Cantidad1 unit

Condiciones de envíoTemperatura ambiente

CapacidadHasta dos minigeles

Para utilizar con (equipo)XCell SureLock™ Mini

Gel CompatibilityMinigeles Novex™, geles NuPAGE™

Tamaño de gelMini (8 cm x 8 cm)

Tensión máx.500 V DC

Línea de productosXCell SureLock

TipoMinisistema de electroforesis con miniceldas Vertical

Unit SizeEach

Contenido y almacenamiento

Almacenar a temperatura ambiente. Garantía de un año desde el momento de la compra.

Preguntas frecuentes

Can I use FMC 10 cm x 10 cm gels with the XCell SureLock unit?

No. The FMC gels are 10 cm x 10 cm but are slightly thinner so they do not fit properly in the XCell SureLock unit, and as a result the inner buffer chamber will leak.

Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.

I am transferring a Tris-Glycine gel using constant voltage and the current reading is way over the expected starting current. Can you offer some suggestions?

The most common cause of abnormally high current is the transfer buffer. If the transfer buffer is too concentrated, this leads to increased conductivity and current. High current may also occur if Tris-HCl is accidentally substituted for the Tris base required in the transfer buffer. This will again result in low buffer pH and lead to increased conductivity and current and subsequently, overheating. We recommend checking the transfer buffer and its reagent components and re-diluting or remaking the buffer.

Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.

I ran my protein under native conditions on a Tris-Glycine gel. It has a pI that is higher than the pH of the Tris-Glycine transfer buffer. Can you offer some tips for transferring it?

- Increase the pH of Tris-Glycine transfer buffer to 9.2, allowing all the proteins below pI 9.2 to transfer towards the anode electrode.
- Use the Tris-Glycine transfer buffer and place a membrane on both sides of the gel. If there are any proteins that are more basic than the pH of the transfer buffer, they will be captured on the extra membrane placed on the cathode side of the gel. Both membranes can then be developed in the same manner.
- Prior to blotting, incubate the gel for 15 minutes in Tris-Glycine transfer buffer containing 0.1% SDS. The small amount of SDS will give the proteins enough charge to move unidirectionally towards the anode and in most cases, should not denature the protein. Proceed with the transfer using regular Tris-Glycine transfer buffer.

Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.

I had problems transferring my larger-molecular weight proteins from my NuPAGE gel. Can you please offer some suggestions?

For proteins larger than 100 kDa, we recommend pre-equilibrating the gel in 2X NuPAGE Transfer buffer (without methanol) containing 0.02-0.04% SDS for 10 minutes before assembling the sandwich and then transferring using 1X NuPAGE transfer buffer containing methanol and 0.01% SDS.

Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.

What causes empty spots on my membrane after transfer?

Here are possible causes and solutions:

- Presence of air bubbles between the gel and the membrane preventing the transfer of proteins. Be sure to remove all air bubbles between the gel and membrane by rolling a glass pipette over the membrane surface.
- Expired or creased membranes used. Use fresh, undamaged membranes.

Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.

View all Minicelda XCell SureLock™ FAQs

Citations & References (11)

Citations & References

Abstract

Enzymatic hydrolysis of pyridoxine-5'-beta-D-glucoside is catalyzed by intestinal lactase-phlorizin hydrolase.

Authors: Mackey Amy D; Henderson George N; Gregory Jesse F 3rd;

Journal:J Biol Chem

PubMed ID:12023280

'An obligatory step in the mammalian nutritional utilization of pyridoxine-5''-beta-D-glucoside (PNG) is the intestinal hydrolysis of its beta-glucosidic bond that releases pyridoxine (PN). This laboratory previously reported the purification and partial characterization of a novel cytosolic enzyme, designated PNG hydrolase, which hydrolyzed PNG. An investigation of the subcellular distribution of ... More

Definition of genetically distinct attenuation mechanisms in naturally virulence-attenuated Listeria monocytogenes by comparative cell culture and molecular characterization.

Authors:Roberts A, Chan Y, Wiedmann M,

Journal:Appl Environ Microbiol

PubMed ID:16000803

'Listeria monocytogenes is a foodborne pathogen able to cause serious disease in humans and animals. Not all isolates are equally pathogenic, however, and several isolates have been characterized as naturally virulence attenuated. We sought to identify the genetic basis of natural virulence attenuation using cell culture assays and molecular techniques. ... More

Combined effect of epinephrine and exercise on calpain/calpastatin and cathepsin B and L activity in porcine longissimus muscle.

Authors:Ertbjerg P, Henckel P, Karlsson A, Larsen LM, Møller AJ,

Journal:J Anim Sci

PubMed ID:10492449

The objective of the study was to improve the understanding of the relationship between the effect of epinephrine plus exercise and meat tenderness. The calpain, calpastatin, and cathepsin B + L activities and postmortem proteolysis in porcine longissimus muscle were studied. The muscle glycogen stores were depleted in five pigs ... More

Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease.

Authors:Zheng L, Nukuna B, Brennan ML, Sun M, Goormastic M, Settle M, Schmitt D, Fu X, Thomson L, Fox PL, Ischiropoulos H, Smith JD, Kinter M, Hazen SL,

Journal:J Clin Invest

PubMed ID:15314690

In recent studies we demonstrated that systemic levels of protein-bound nitrotyrosine (NO(2)Tyr) and myeloperoxidase (MPO), a protein that catalyzes generation of nitrating oxidants, serve as independent predictors of atherosclerotic risk, burden, and incident cardiac events. We now show both that apolipoprotein A-I (apoA-I), the primary protein constituent of HDL, is ... More

Regulation of the mitogen-activated protein kinase p44 ERK activity during anoxia/recovery in rainbow trout hypodermal fibroblasts.

Authors:Ossum CG, Wulff T, Hoffmann EK,

Journal:J Exp Biol

PubMed ID:16621957

It is well known from various mammalian cells that anoxia has a major impact on the mitogen-activated protein kinase ERK, but a possible similar effect in fish cells has not been investigated. Here we characterise a p44ERK-like protein in the rainbow trout cell line RTHDF and study the effect of ... More

View all Minicelda XCell SureLock™ citations