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  6. Invitrogen™ Bolt™ Bis-Tris Welcome Pack, 12%

Invitrogen™ Bolt™ Bis-Tris Welcome Pack, 12%

Catalog No. NW0012A
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Catalog No. NW0012A Supplier Invitrogen™ Supplier No. NW0012A
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Description

The Bolt Welcome Pack provides all of the necessary Bolt gels and buffers you will need to begin using the Mini Gel Tank.

The Bolt Welcome Pack provides all of the necessary Bolt gels and buffers you will need to begin using the Mini Gel Tank. The Mini Gel Tank is compatible with Novex gels, NuPAGE gels, and Bolt Bis-Tris Plus gels. Each Mini Gel Tank can accommodate up to two gels per run. The unique tank design enables convenient side-by-side gel loading and enhanced viewing during use. Optimized conditions using constant voltage allow for Bolt Bis-Tris Plus gels to be run in approximately 20 minutes.

The Welcome Pack contains:
• Mini Gel Tank (A25977)
• Bolt Bis-Tris Plus gels (2 boxes, 20 gels)
• Bolt MES Running Buffer, 20X (B0002)
• Bolt LDS Sample Buffer, 4X (B0007)
• Bolt Sample Reducing Agent, 10X (B0009)
• PageRuler Plus Prestained Protein Ladder, 10 to 250 kDa (26619)

About the Mini Gel Tank
The Mini Gel Tank is compatible with Novex gels, NuPAGE gels, and Bolt Bis-Tris Plus gels. Each Mini Gel Tank can accommodate up to two gels per run. The unique tank design enables convenient side-by-side gel loading and enhanced viewing during use. Optimized conditions using constant voltage allow for Bolt Bis-Tris Plus gels to be run in approximately 20 minutes. Run times may vary depending on buffer conditions and power supplies used.

About Bolt Bis-Tris Plus Gels
Bolt Bis-Tris Plus gels are precast polyacrylamide gels designed for optimal separation of your small- to medium-sized proteins under denaturing conditions. Bolt Bis-Tris Plus gels are designed to deliver consistent gel performance and provide a neutral pH environment that minimizes protein modifications. Bolt gels are ideal for western blot transfer and analysis, and any other techniques where protein integrity is crucial. Also use Bolt gels to obtain optimal results for your day-to-day protein separation needs. Bolt Bis-Tris Plus gels come in four polyacrylamide concentrations: 8, 10, 12, and 4-12% gradient and multiple well formats. Bolt Bis-Tris gels feature wedge-shaped wells, which can easily load up to two times more sample volume allowing for detection of proteins in very dilute samples or visualization of low-abundance proteins.

For transferring your proteins to a membrane, we recommend using for Bolt Transfer Buffer (BT0006) for traditional wet transfer using the Mini Blot Module (B1000). Alternatively, rapid semi-dry transfer can be done using the Invitrogen Power Blotter or rapid dry transfer using the iBlot 2 Gel Transfer Device (IB21001).

Warranty

Up to 12 months

Specifications

Gel Percentage 12%
Gel Size Mini
Gel Thickness 1.0 mm
Gel Type Bis-Tris
Separation Range 3.5 to 80 kDa
Wells 10-well
Quantity 1 Welcome Pk. kit
Shipping Condition Approved for shipment at room temperature and wet ice
Product Line Bolt, WedgeWell
For Use With (Equipment) Mini Gel Tank

Frequently Asked Questions (FAQs)

Can I prepare my protein sample with the reducing agent and store it for future use?

DTT is not stable, so it must be added and the reduction performed just prior to loading your samples.
My LDS or SDS sample buffer precipitates when stored at 4 degrees C. Can I warm it up? Can I store it at room temperature?

Precipitation of the LDS or SDS at 4 degrees C is normal. Bring the buffer to room temperature and mix until the LDS/SDS goes into solution. If you do not want to wait for it to dissolve, you can store the sample buffer at room temperature.
What are the storage conditions for Bolt gels?

Similar to NuPAGE gels with storage temperatures of 4 to 25 degrees C.
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.

I used one of your protein standards for a western transfer and noticed that some of the higher-molecular weight bands transferred very poorly to the membrane. Can you offer some tips?

- Increase voltage, current or length of time for transfer
- SDS in the gel and in the SDS-protein complexes promotes elution of the protein from the gels but inhibits binding of the protein to membranes. This inhibition is higher for nitrocellulose than for PVDF. For proteins that are difficult to elute from the gel such as large molecular weight proteins, a small amount of SDS may be added to the transfer buffer to improve transfer. We recommend pre-equilibrating the gel in 2X Transfer buffer (without methanol) containing 0.02-0.04% SDS for 10 minutes before assembling the sandwich and then transferring using 1X transfer buffer containing 10% methanol and 0.01%SDS.
- Methanol removes the SDS from SDS-protein complexes and improves the binding of protein to the membrane, but has some negative effects on the gel itself, leading to a decrease in transfer efficiency. It may cause a reduction in pore size, precipitation of some proteins, and some basic proteins to become positively charged or neutral. Make sure that the methanol concentration in the transfer buffer is not more than 10-20% and that high-quality, analytical grade methanol is used.

I used one of your pre-stained standards on a Tris-Glycine gel and noticed that the molecular weights of the proteins were different than on a NuPAGE Bis-Tris gel. What is the reason for this?

Pre-stained standards have a dye that is covalently bound to each protein that will result in the standard migrating differently in different buffer systems (i.e., different gels). As a result, using a pre-stained standard for molecular weight estimation will only give the apparent molecular weight of the protein. Pre-stained standards may be used for molecular weight approximation, confirming gel migration and estimating blotting efficiency but for accurate molecular weight estimation, an unstained standard should be used.

I used one of your protein standards and am seeing some extra bands in the lane. Can you offer some suggestions?

- While loading, take care to make sure that there is no cross-contamination from adjacent sample lanes.
- Make sure that the correct amount of standard is loaded per lane. Loading too much protein can result in extra bands and this is a problem especially with silver-stained gels.
- Improper storage of the standard or repeated freeze/thawing can result in protein degradation.

I used one of your protein standards and the bands look non-distinct and smeary. What should I do?

Here are some suggestions:

- Make sure that the correct amount of standard is loaded per lane. Loading too much protein can cause smearing and this is a problem especially with silver stained gels.
- Bands will not be as well resolved in low percentage gels. Try using a higher percentage gel.
- If the bands look smeary and non-distinct after a western transfer/detection, this may be due to the antibody being too concentrated. Follow the manufacturer's recommended dilution or determine the optimal antibody concentration by dot-blotting.

A couple of bands in my protein standard are missing on the gel. Can you help me troubleshoot?

Here are some suggestions:

- Check the gel type/percentage of the gel that was used. Depending on the gel type and/or percentage, all the bands may not be seen. For example, the smallest bands of the protein standard may not resolve on a very low percentage gel whereas the higher molecular weight bands may not resolve on a high percentage gel.
- Check the expiration date on the protein standard. Expired lots may result in faded or missing bands due to protein degradation.
- Check the storage conditions for the protein standard. Improper storage conditions will compromise the stability of the proteins in the standard.
- Make sure that the protein standard was not heated/boiled prior to loading on the gel. Our protein standards are ready to load and we do not recommend heating/boiling them as this may cause degradation of proteins in the standard.

What is the composition of the PageRuler Plus Prestained Protein Ladder?

The PageRuler Plus Prestained Protein Ladder is a mixture of nine (9) blue-, orange- and green-stained proteins (10 to 250 kDa) for use in protein electrophoresis (SDS-PAGE) and western blotting. Two orange reference bands at ~70 kDa and 25 kDa and one green reference band at 10 kDa highlight the blue-stained protein ladder.
What are the storage conditions and shelf life for the PageRuler Prestained Protein Ladder and PageRuler Plus Prestained Protein Ladder?

We recommend storing these ladders at -20 degrees C where they are stable for a year. They are stable for up to 3 months at 4 degrees C.