偶联物
magnetic beads
质量水平
形式
(1:1 suspension in a 20% ethanol solution)
特点
hydrophilic
包装
pkg of 1 mL
pkg of 100 mL
pkg of 25 mL
pkg of 5 mL
pkg of 500 mL
浓度
1.5-2.4 mL/mL (suspension in packed gel)
技术
protein purification: suitable
颜色
faint blue to very dark blue
基质
6% Beaded Agarose
容量
>15 mg/mL, gel binding capacity (protein)(with an approx. 30 kDa protein)
转变温度
flash point 32 °C (closed cup)
储存温度
2-8°C
一般描述
应用
特点和优势
- 带来更高纯度的高选择性。
- 特有的非电荷亲水性连接减少非特异性结合。
- 组氨酸标签蛋白结合容量超过15 mg/mL。
- 在变性或非变性条件下都能结合。
- 一步完成纯化。
- 最大限度减少不必要的离子相互作用。
- 极低的镍浸出。
- 粒径:45-165 μm。
联系
外形
储存及稳定性
法律信息
相关产品
警示用语:
Warning
危险声明
危险分类
Flam. Liq. 3
储存分类代码
3 - Flammable liquids
WGK
WGK 3
闪点(°F)
89.6 °F - closed cup
闪点(°C)
32 °C - closed cup
法规信息
Can imidazole be used with HIS-Select® Nickel Affinity Gel, Product P6611?
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.
Can Tris buffers be used instead of phosphate buffer for HIS-Select® Nickel Affinity Gel, Product P6611?
Yes, Tris buffers should work.
Why won't my recombinant protein with a histidine-containing tag bind to HIS-Select® Nickel Affinity Gel, Product P6611?
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.
Can I use SDS with HIS-Select® Nickel Affinity Gel, Product P6611?
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.
What needs to be done if the HIS-Select® Nickel Affinity Gel, Product P6611, resin turns brown on reuse?
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.
Which document(s) contains shelf-life or expiration date information for a given product?
If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.
How do I get lot-specific information or a Certificate of Analysis?
The lot specific COA document can be found by entering the lot number above under the "Documents" section.
How do I find price and availability?
There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote. USA customers: 1-800-325-3010 or view local office numbers.
What is the Department of Transportation shipping information for this product?
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.
My question is not addressed here, how can I contact Technical Service for assistance?
Ask a Scientist here.
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