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北京云肽生物科技有限公司
NanoTag Biotechnologies,2015年在哥廷根成立,专注于生产生化和荧光应用的单域抗体(纳米抗体/VHH抗体)和试剂。 可稳定提供荧光标记的单域抗体,新型标签“ALFA”单域抗体及其纯化系统,用于IP的Selector resins,以满足各种实验的要求。
我们北京云肽生物科技有限公司作为NanoTag公司的特约经销商为客户提供,正规进口,保证原装正品,货期稳定,折扣好的服务标准
NanoTag N1520 ALFA elution peptide 10mg,产品简介:
产品品牌:NanoTag
产品货号:N1520
产品名称:ALFA elution peptide
产品规格:10mg
产品说明:
一个小瓶含有 10 mg ALFA 洗脱肽,用于制备用于 ALFA 选择器 PE 的天然洗脱缓冲液。我们建议将冻干肽溶解在 250 μL 纯水中,以获得 100 倍储备溶液。该肽不能有效地从ALFA选择器ST(超紧密)中洗脱ALFA标记的蛋白质。
请注意:每单位的阿尔法选择PE均包括一个含有10 mg冻干肽(足以容纳25 mL洗脱缓冲液)的小瓶。如果您的实验需要更多的洗脱肽,这是适合您的产品。
| 生产于: | 合成肽 |
| 抗原: | ALFA-tag |
| 特 异性: | 获得NbALFA,NbALFA-PE和NbALFA-CE的认可 |
| 配方: | 含有10mg ALFA洗脱肽的冻干粉末。用 250 μL 无菌水复溶以获得 100 倍储备溶液 (20 mM)。 |
| Shipping: | Ambient temperature |
| Storing: | Vials containing lyophilized peptide can be stored at 4 °C for up to 6 months. When reconstituted in water, aliquot and store at -20°C or below. |
| Protocols: | Please dissolve the lyophilized peptide (10 mg) in 250 µl of distilled water. This results in an ALFA peptide concentration of 40 mg/ml equivalent to 20 mM (100x). Detail protocols for IP and elutions using the ALFA system can be found here in the ALFA Selector Manual Protocols can be found on our Resources page. |
| References: | Götzke et al. 2019 The ALFA-tag is a highly versatile tool for nanobody-based bioscience applications. |
| Notice: | To be used in vitro/ for research only. Non-toxic, non-hazardous, non-infectious. |
| Legal terms: | By purchasing this product you agree to our general terms and conditions. |
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This specfic protocol is the latest incarnation of peptide mapping procedures that have been developed here in the TVL/MBVL of the Salk Institute over the last 20 years. Wade Gibson developed the first peptide mapping protocol
Predicting Peptide Retention Times for Proteomics
. Petritis, K., Kangas, L.J., Yan, B., Monroe, M.E., Strittmatter, E.F., Qian, W.J., Adkins, J.N., Moore, R.J., Xu, Y., Lipton, M.S., Camp, D.G. 2nd, and Smith, R.D. 2006. Improved peptide elution time
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region of interest, and 2) the length of the “bait” peptide is sufficient for recognition by the candidate reader protein(s). Histones are most heavily modified at their N- and C-terminal tails, which are relatively unstructured and jut away
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