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- pro-540
- 2026年01月15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：
GLC8
- 库存：
常规产品有备货
- 供应商：
上海经科化学科技有限公司
- CAS号：
无
- 规格：
10ug/50ug/1mg
| 规格： | 10ug | 产品价格： | ￥1080.0 |
|---|---|---|---|
| 规格： | 50ug | 产品价格： | ￥2415.0 |
| 规格： | 1mg | 产品价格： | ￥30429.0 |
CATALOGUE NUMBER
PRO-540
SYNONYMS
INTRODUCTION
DESCRIPTION
GLC8 Yeast (Saccharomyces cerevisiae) Recombinant produced in E.coli is a single, glycosylated polypeptide chain containing 265 amino acids (1-229) and having a molecular mass of 30.7 kDa (molecular size on SDS-PAGE will appear higher).
The GLC8 is fused to a 35 amino acid His Tag at N-Terminus and purified by standard chromatography techniques.
SOURCE
PHYSICAL APPEARANCE
FORMULATION
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.
STABILITY
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
AMINO ACID SEQUENCE
SAFETY DATA SHEET
SDS
PURITY
USAGE
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文献和实验GLC8 Yeast (Saccharomyces cerevisiae) Recombinant produced in E.coli is a single, glycosylated polypeptide chain containing 265 amino acids (1-229) and having a molecular mass of 30.7 kDa (molecular size on SDS-PAGE will appear higher).
The GLC8 is fused to a 35 amino acid His Tag at N-Terminus and purified by standard chromatography techniques.
Expression of Recombinant Matrix Metalloproteinases in Yeast
Deciding what system to use for recombinant matrix metalloproteinase (MMP) expression is often a matter of practicality (i.e., simplicity, cost effectiveness, time considerations). Of course, the final judgment of practicality is determined
Setting Up a Bioreactor for Recombinant Protein Production in Yeast
Scale-up from shake flasks to bioreactors allows for the more reproducible, high-yielding production of recombinant proteins in yeast. The ability to control growth conditions through real-time monitoring facilitates further optimization
Recombinant Collagen Trimers from Insect Cells and Yeast
are not suitable as such for the production of recombinant collagens, however, as bacteria and yeast have no prolyl 4-hydroxylase activity and insect cells have insufficient levels of it. Prolyl 4-hydroxylase, an α2 β2 tetramer in vertebrates, plays a central role
技术资料