Novex™ Sharp Pre-stained Protein Standard
Novex™ Sharp Pre-stained Protein Standard
Invitrogen™

Novex™ Sharp Pre-stained Protein Standard

Novex Sharp Pre-Stained Protein Standard is designed for accurate, easy, and convenient molecular weight estimation of a wide range ofRead more
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Catalog number LC5800
Price (USD)
228.00
Each
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Price (USD)
228.00
Each
Add to cart
Novex Sharp Pre-Stained Protein Standard is designed for accurate, easy, and convenient molecular weight estimation of a wide range of molecular weight proteins during SDS-PAGE and western blotting. The standard consists of 12 colored bands in the range of 3.5 to 260 kDa and is supplied in a ready-to-use format for direct loading onto gels; no need to heat, reduce, or add sample buffer prior to use.

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Applications
• Monitoring protein migration during SDS-polyacrylamide gel electrophoresis
• Monitoring protein transfer onto membranes after western blotting
• Sizing of proteins on SDS-PAGE gels and western blots

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Detection MethodColorimetric
Number of Markers12
Product TypeProtein Ladder
Ready to LoadYes
Size Range3.5 to 260 kDa
Stain Type3 colors: Pink, Yellow, Blue
Gel CompatibilityBolt™ Bis-Tris Plus Gels, Novex™ Tricine Gels, Novex™ Tris-Glycine Gels, NuPAGE™ Bis-Tris Gels
Molecular Weight (g/mol)260, 160, 110, 80, 60, 50, 40, 30, 20, 15, 10, 3.5 kDa
Product LineNovex™
Quantity2 x 250 μL
Shipping ConditionApproved for shipment on Wet or Dry Ice
System TypeWestern Blotting, SDS-PAGE
Unit SizeEach
Contents & Storage
Novex™ Sharp Pre-stained Protein Standards are provided as 2 x 250 μL (total of 50 applications of 10 μL each) of ready-to-use standard mixture. The Novex™ Sharp Pre-Stained standard loading buffer consists of 65 mM Tris pH 6.5, 30% glycerol, 2% SDS, and 2.5 mM ETDA.

Store at -20°C.

Frequently asked questions (FAQs)

Why can I not see the 3.5 kDa band of the Invitrogen Sharp Pre-Stained Standard on my NuPAGE gels?

The 3.5 kDa band is visible only on NuPAGE gels with 1X MES SDS running buffer.

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

What are the different molecular weight estimations for the Invitrogen Sharp Pre-Stained standard on the different Invitrogen gel types?

Invitrogen Sharp Pre-Stained Standard molecular weight estimations are the same in NuPAGE Bis-Tris, NuPAGE Tris-Acetate, Invitrogen Tris-Glycine, and Tricine Gels. The appearance/migration of the protein bands may differ depending upon the gel type and running conditions

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

What are the recommended protocols for preparing Invitrogen protein standards to load on a gel?

Invitrogen protein standards do not require any additional preparation. Thaw protein standards at room temperature, vortex to mix well, and load.

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

I used one of your pre-stained protein standards for a western transfer and I noticed that the intensity of the band faded from the membrane during the transfer process. Why is this?

The fading is most likely due to detergent in the western blocking/washing solutions that can remove some of the proteins from the membrane. The dye itself will not wash off of the proteins because it is covalently bound. We have found that smaller pore size membranes retain the proteins better during blocking and wash procedures, and hence recommend use of 0.2 µm instead of 0.45 µm membranes for best resolution and protein retention. After transfer, it is a good idea to circle the pre-stained bands with a pencil on the membrane, so band positions can be identified after blocking and processing.

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

I used one of your protein standards for a western transfer and noticed that some of the lower-molecular weight protein bands passed through the membrane. How can I resolve this issue?

- Decrease voltage, current or length of transfer time
- Make sure that the methanol concentration in the transfer buffer is proper; use a methanol concentration of 10-20% methanol removes the SDS from SDS-protein complexes and improves the binding of protein to the membrane.
- Make sure that the SDS concentration (if added) in the transfer buffer is proper, don't use more than 0.02-0.04% SDS. Using too much SDS can prevent binding of proteins to the membrane.
- Check the pore size of the membrane and the size of the target protein. Proteins smaller than 10 kDa will easily pass through a 0.45 µm pore size membrane. If proteins smaller than 10 kDa are of interest, it would be better to use a 0.2 µm pore size membrane.

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