Yes, Tris buffers should work.
P6611
HIS-Select® Nickel Affinity Gel
(1:1 suspension in a 20% ethanol solution)
HIS-Select® Nickel Affinity Gel
1 of 1 reviewers received a sample product or took part in a promotion
Synonym(s):
Ni-NTA resin, nickel charged agarose
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| Pack Size | SKU | Availability | Price |
|---|---|---|---|
| 5 mL | Available to ship TODAYfromBangalore Non-Bonded Warehouse | ₹15,501.40 | |
| 25 mL | Available to ship TODAYfromBangalore Non-Bonded Warehouse | ₹56,387.43 | |
| 100 mL | Available to ship TODAYfromBangalore Non-Bonded Warehouse | ₹1,59,906.90 | |
| 500 mL | Available to ship TODAYfromBangalore Non-Bonded Warehouse | ₹6,66,733.40 |
About This Item
NACRES:
NA.56
UNSPSC Code:
12352200
₹15,501.40
Available to ship TODAYDetails
conjugate
magnetic beads
Quality Level
form
(1:1 suspension in a 20% ethanol solution)
feature
hydrophilic
packaging
pkg of 1 mL, pkg of 100 mL, pkg of 25 mL, pkg of 5 mL, pkg of 500 mL
concentration
1.5-2.4 mL/mL (suspension in packed gel)
technique(s)
protein purification: suitable
color
faint blue to very dark blue
matrix
6% Beaded Agarose
capacity
>15 mg/mL, gel binding capacity (protein)(with an approx. 30 kDa protein)
transition temp
flash point 32 °C (closed cup)
storage temp.
2-8°C
General description
HIS-Select® Nickel Affinity Gel is an immobilized metal ion affinity chromatography (IMAC) product, used for the purification of His-tagged proteins. While the unique, non-charged, hydrophilic linkage of the proprietary quadridentate NTA chelate group to the beaded agarose charged with nickel ensures high selectivity for small to medium scale His-tag protein purification, it also results in reduced non-specific binding of other proteins. HIS-Select Nickel Affinity Gel is selective for recombinant proteins with His-tags and exhibits low non-specific binding of other proteins. The selectivity can be modulated with the inclusion of imidazole during chromatography.
Application
Features and Benefits
- High selectivity for higher purity.
- Unique non-charged hydrophilic linkage reduces non-specific binding.
- Binding capacity for histidine-tagged protein is greater than 15 mg/mL.
- Binding under denaturing or non-denaturing conditions.
- One-step purification.
- Minimizes unwanted ionic interactions.
- Minimal nickel leaching.
- Bead size: 45-165 μm.
Physical form
1:1 suspension in a 20% ethanol solution
Preparation Note
HIS-Select Nickel Affinity Gel is stable for at least one year when stored properly. The HIS-Select Nickel Affinity Gel should be cleaned after each use and an antimicrobial agent such as 20% ethanol should be added to the storage buffer.
Other Notes
It is also available with the EZview™ technology (Product Code E3528).
Legal Information
HIS-Select is a registered trademark of Merck KGaA, Darmstadt, Germany
1 of 1
This Item | |||
|---|---|---|---|
| matrix 6% Beaded Agarose | matrix Highly cross-linked 6% Beaded Agarose | matrix 6% Beaded Agarose | matrix - |
| form (1:1 suspension in a 20% ethanol solution) | form suspension | form (1:1 suspension in a 30% ethanol solution) | form slurry |
| technique(s) protein purification: suitable | technique(s) affinity chromatography: suitable | technique(s) protein purification: suitable | technique(s) - |
| capacity >15 mg/mL, gel binding capacity (protein)(with an approx. 30 kDa protein) | capacity 15 mg/mL, gel binding capacity (protein)(with an approx. 30 kDa protein) | capacity >15 mg/mL, agarose binding capacity (protein)(with an approx. 30 kDa protein) | capacity - |
| packaging pkg of 1 mL, pkg of 25 mL, pkg of 500 mL, pkg of 100 mL, pkg of 5 mL | packaging - | packaging - | packaging - |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
signalword
Warning
hcodes
Hazard Classifications
Flam. Liq. 3
Storage Class
3 - Flammable liquids
wgk
WGK 3
flash_point_f
89.6 °F - closed cup
flash_point_c
32 °C - closed cup
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Global Trade Item Number
| SKU | GTIN |
|---|---|
| P6611-5ML | 04061838256225 |
| P6611-500ML | 04061838256218 |
| P6611-100ML | 04061838256201 |
| P6611-1ML | 04061838216915 |
| P6611-25ML | 04061838114563 |
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Can Tris buffers be used instead of phosphate buffer for HIS-Select® Nickel Affinity Gel, Product P6611?
1 answer-
Helpful?
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Can I use SDS with HIS-Select® Nickel Affinity Gel, Product P6611?
1 answer-
0.1% SDS has been used with some samples, with no adverse effects on the observed protein binding. However, SDS will effectively coat proteins and may block the binding to the column. It is probably very protein-specific and an SDS concentration that works for one protein may not work for another.
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What is the Department of Transportation shipping information for this product?
1 answer-
Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
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What needs to be done if the HIS-Select® Nickel Affinity Gel, Product P6611, resin turns brown on reuse?
1 answer-
During purification many protein extracts tend to discolor an affinity gel during the loading step. The original color will return after the wash or elution step. If the color is still not changing strip and recharge the affinity gel with nickel. Wash with EDTA and recharge with Nickel solution.
Helpful?
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Can imidazole be used with HIS-Select® Nickel Affinity Gel, Product P6611?
1 answer-
For column chromatography, no more than 20 mM is suggested in the extract, equilibration, and wash buffers to prevent non-specific binding of proteins. No more than 250 mM is suggested for the elution buffers. Many proteins will elute with imidazole levels as low as 100 to 200 mM. For batch methods the imidazole concentration may have to be reduced or eliminated.When a protein is expressed at low levels, the presence of the imidazole limits the binding of the protein in the batch method but not when used in a column.
Helpful?
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Why won't my recombinant protein with a histidine-containing tag bind to HIS-Select® Nickel Affinity Gel, Product P6611?
1 answer-
Verify the pH and composition of sample and equilibration buffers. Make sure there are no chelating or reducing agents present in the extraction buffer. If using the batch mode, remove imidazole. Run the affinity purification under denaturing conditions. Run a Western blot of the extract to verify that the recombinant protein is present.
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