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- Prospecbio
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- cyt-1070
- 2025年12月28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：
TPO, CHO
- 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：
1ug/5ug/50ug
| 规格： | 1ug | 产品价格： | ￥1080.0 |
|---|---|---|---|
| 规格： | 5ug | 产品价格： | ￥2415.0 |
| 规格： | 50ug | 产品价格： | ￥14500.0 |
CATALOGUE NUMBER
CYT-1070
SYNONYMS
INTRODUCTION
| Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney which regulates the production of platelets by the bone marrow. TPO stimulates the production as well as differentiation of megakaryocytes, the bone marrow cells which fragment into large numbers of platelets. |
DESCRIPTION
Thrombopoietin Human Recombinant produced in CHO cells has a molecular weight range of 80-90kDa due to glycosylation.
The TPO is purified by proprietary chromatographic techniques.
SOURCE
Chinese Hamster Ovary Cells.
PHYSICAL APPEARANCE
FORMULATION
TPO protein solution contains phosphate buffered saline (pH7.4) and 2% albumin.
STABILITY
Thrombopoietin although stable at room temperature for 1 week, should be stored between 2-8°C.
PURITY
Greater than 98% as determined by SDS-PAGE.
BIOLOGICAL ACTIVITY
The ED50 as determined by the dose-dependent stimulation of MO7e cells corresponding to a specific activity of 3x105 units/mg.
SAFETY DATA SHEET
SDS
USAGE
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文献和实验Thrombopoietin Human Recombinant produced in CHO cells has a molecular weight range of 80-90kDa due to glycosylation.
The TPO is purified by proprietary chromatographic techniques.
in emergencies such as bleeding. Forty years ago, it was recognized that a humoral regulator circulating in thrombocytopenic animals was able to stimulate platelet production in normal recipients (1 ). Termed thrombopoietin (TPO), the properties of this activity
Construction of Recombinant Human Cytomegalovirus
The use of reverse genetics to generate recombinant viruses allows the researcher to investigate the exact functional significance of particular viral genes during the virus life cycle, by means of their deletion or modification in the viral
range of recombinant proteins. Here, we describe the methodology associated with expressing a variety of molecular chaperones in Chinese hamster ovary (CHO) lines in order to improve their recombinant protein production capacity. These chaperones include
技术资料