- ￥1080 - 45885
- PROSPEC
- 以色列
- cyt-670
- 2025年12月27日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
for future use below -18°C
- 保质期：
See instructions
- 英文名：
sCD40L, His
- 库存：
部分小规格有备货
- 供应商：
上海经科化学科技有限公司
- CAS号：
无
- 规格：
5ug/20ug/1mg
| 规格： | 5ug | 产品价格： | ￥1080.0 |
|---|---|---|---|
| 规格： | 20ug | 产品价格： | ￥2415.0 |
| 规格： | 1mg | 产品价格： | ￥45885.0 |
CATALOGUE NUMBER
CYT-670
SYNONYMS
INTRODUCTION
DESCRIPTION
CD40LG Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 169 amino acids (113-261 a.a.) and having a molecular mass of 18.3kDa.
The CD40LG is purified by proprietary chromatographic techniques.
SOURCE
PHYSICAL APPEARANCE
FORMULATION
The CD40LG solution (0.5mg/ml) 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol and 0.2M NaCl.
STABILITY
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
PURITY
AMINO ACID SEQUENCE
SAFETY DATA SHEET
SDS
USAGE
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文献和实验CD40LG Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 169 amino acids (113-261 a.a.) and having a molecular mass of 18.3kDa.
The CD40LG is purified by proprietary chromatographic techniques.
Purification of Human Multiprotein Complexes using OneSTrEP Technology
. For more theoretical background and a protocol for purification of recombinant Strep -tag® fusion proteins from E.coli please refer to Schmidt and Skerra (2007). In comparison to other commonly used purification strategies (i.e. HA and FLAG double-tag
Purification of Human Multiprotein Complexes using OneSTrEP Technology (PROT41)
complexes from human HeLa S3 cells in a scale and purity optimized for characterization by mass spectrometry. For this purpose, we use stably expressed One-STrEP -tag ® fusion proteins. This approach was successfully used in characterization of histone
[资源] 申请上传 Current Protocols In Protein Science （60M） 见公共邮箱
Proteins Introduction Unit 6.1 Overview of the Purification of Recombinant Proteins Produced in Escherichia coli Unit 6.2 Preparation of Soluble Proteins from Escherichia coli Unit 6.3 Preparation and Extraction of Insoluble (Inclusion-Body) Proteins
技术资料