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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:
tPrl R
- 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: | ¥52000.0 |

CATALOGUE NUMBER
CYT-532
SYNONYMS
INTRODUCTION
DESCRIPTION
The Prolactin Receptor is purified by proprietary chromatographic techniques.
SOURCE
PHYSICAL APPEARANCE
FORMULATION
SOLUBILITY
STABILITY
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
PURITY
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.
AMINO ACID SEQUENCE
BIOLOGICAL ACTIVITY
PROTEIN CONTENT
1. UV spectroscopy at 280 nm using the absorbency value of 2.48 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
2. Analysis by RP-HPLC, using a standard solution of PRLr-ECD as a Reference Standard.
SAFETY DATA SHEET
SDS
USAGE
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文献和实验Prolactin Receptor Rainbow Trout Extra Celleular Domain Recombinant ?produced in E.Coli is a non-glycosylated, Polypeptide chain containing 210 amino acids and having a molecular mass of 24034 Dalton.
The Prolactin Receptor is purified by proprietary chromatographic techniques.
Bacterial Expression of Prolactin Family Proteins
Complementary DNAs of three recombinant proteins related to the prolactin family: ovine placental lactogen (oPL), ovine prolactin (oPRL), and rabbit soluble extracellular domain of prolactin receptor (rbPRLR-ECD) were subcloned by different
. By studying the soluble extracellular domain of the receptor, the use of detergents is avoided, and biochemical and biophysical analyses are facilitated. We have expressed the extracellular domain of the EGF receptor (EGFR-ED) by infecting insect cells
Gene Therapy with Plasmids Encoding Cytokine- or Cytokine Receptor-IgG Chimeric Proteins
cytokines (1 ). However, cytokine and soluble cytokine-receptor therapy have been limited by the short half-life (T1/2) of these proteins and the necessity to administer relatively large boluses of recombinant proteins (2 ). This results in transient high
技术资料








