BenchMark™ His-tagged Protein Standard
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Invitrogen™

BenchMark™ His-tagged Protein Standard

BenchMark His-tagged Protein Standard is designed as a positive control and for molecular weight sizing in his-tagged fusion protein detection.Read more
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Catalog NumberQuantity
LC5606125 μL
Catalog number LC5606
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334.65
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Price (USD)
334.65
Online Exclusive
344.00
Save 9.35 (3%)
Each
Add to cart
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BenchMark His-tagged Protein Standard is designed as a positive control and for molecular weight sizing in his-tagged fusion protein detection. Each of the ten standard proteins (10-160 kDa) contains a 6X His-tag, enabling the detection of standard proteins with the InVision™ His-tag In-gel Stain (Cat. no. LC6030) or with Anti-His(C-term) Antibody (Cat. no. R930-25) using western detection. The protein standard 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
• Verification of His-tagged fusion protein detection using InVision In-Gel Stain or an Anti-His(C-term) antibody
• Sizing of proteins on SDS-polyacrylamide gels and western blots

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Detection MethodInVision™ His-tag In-gel Stain
Gel CompatibilityNovex™ Tricine Gels, Novex™ Tris-Glycine Gels, NuPAGE™ Bis-Tris Gels, SDS-PAGE Gels
Molecular Weight (g/mol)160, 120, 80, 60, 50, 40, 30, 20, 15, 10 kDa
Product LineBenchMark™
Product TypeProtein Ladder
Quantity125 μL
Ready to LoadYes
Shipping ConditionDry Ice
Stain TypeUnstained
System TypeWestern Blotting, SDS-PAGE
Number of Markers10
Size Range10 to 160 kDa
Unit SizeEach
Contents & Storage
125 μL (25 applications of 5 μL each) is provided in loading buffer consisting of Tris-HCl, SDS, Glycerol, DTT, and Coomassie™ Blue G-250.

Store at -20°C. Avoid repeated freezing and thawing.
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Frequently asked questions (FAQs)

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.

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.

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

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.

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

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.

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

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.

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

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Lot #Certificate TypeDateCatalog Number(s)
3176362Certificate of AnalysisApr 22, 2025LC5606
3104178Certificate of AnalysisFeb 18, 2025LC5606
3068501Certificate of AnalysisJan 24, 2025LC5606
3047152Certificate of AnalysisNov 01, 2024LC5606
3037338Certificate of AnalysisSep 13, 2024LC5606
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