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XCell SureLock™ Mini-Cell
The XCell SureLock Mini-Cell is a vertical mini-protein gel electrophoresis system compatible with all Invitrogen mini precast gels and SurecastRead more
| Catalog Number | Quantity |
|---|---|
| EI0001 | 1 unit |
Catalog number EI0001
Price (EUR)
938,65
Online Exclusive
1.002,00Save 63,35 (6%)
Each
-
Quantity:
1 unit
Price (EUR)
938,65
Online Exclusive
1.002,00Save 63,35 (6%)
Each
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.
See all available electrophoresis chamber systems ›
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.
See all available electrophoresis chamber systems ›
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.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Quantity1 unit
Shipping ConditionRoom Temperature
Capacity2 Mini-gels
For Use With (Equipment)XCell SureLock™ Mini
Gel CompatibilityNovex™ Mini Gels, NuPAGE™ Gels
Gel SizeMini (8 x 8 cm)
Max. Voltage500 VDC
Product LineXCell SureLock
TypeMini-Cell Mini-Vertical Electrophoresis System
Unit SizeEach
Contents & Storage
Store at room temperature. Warrantied for one year from the time of purchasing.
Introducing iBlot 3 Western Blot Transfer System
Featuring higher throughput and built-in cooling for consistent protein transfer
Learn more ›
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Figures
Easy set-up procedure for the XCell SureLock® Mini-Cell.
Side view of the XCell SureLock® Mini-Cell (locked).
Side view of the XCell SureLock® Mini-Cell (unlocked).
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Frequently asked questions (FAQs)
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.
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.
- 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.
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.
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.
Citations & References (11)
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Citations & References
Abstract
Enzymatic hydrolysis of pyridoxine-5'-beta-D-glucoside is catalyzed by intestinal lactase-phlorizin hydrolase.
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
Definition of genetically distinct attenuation mechanisms in naturally virulence-attenuated Listeria monocytogenes by comparative cell culture and molecular characterization.
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.
Combined effect of epinephrine and exercise on calpain/calpastatin and cathepsin B and L activity in porcine longissimus muscle.
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
Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease.
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
Regulation of the mitogen-activated protein kinase p44 ERK activity during anoxia/recovery in rainbow trout hypodermal fibroblasts.
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
11 total citations