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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:
IL4, 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:
2ug/10ug/1mg
| 规格: | 2ug | 产品价格: | ¥1080.0 |
|---|---|---|---|
| 规格: | 10ug | 产品价格: | ¥2415.0 |
| 规格: | 1mg | 产品价格: | ¥87906.0 |

CATALOGUE NUMBER
CYT-483
SYNONYMS
INTRODUCTION
DESCRIPTION
The IL-4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
SOURCE
PHYSICAL APPEARANCE
FORMULATION
STABILITY
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze thaw cycles.
BIOLOGICAL ACTIVITY
The ED50 for this effect is <0.5ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.
AMINO ACID SEQUENCE
PURITY
SAFETY DATA SHEET
SDS
USAGE
BACKGROUND
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文献和实验Interleukin-4 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 150 amino acids fragment (25-153) and having a total molecular mass of 17.2kDa.
The IL-4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Construction of Recombinant Human Cytomegalovirus
genome. These studies can extend to the introduction of viral or foreign genetic material into ectopic sites in the viral genome, to investigate viral cis -control sequences or to phenotypically modify or tag the recombinant virus. Genetically modified
This method describes the conjugation of a synthetic glycopeptide to the N-terminus of a recombinant human interleukin-2 (IL-2) protein fragment. The IL-2 protein fragment is produced as an affinity-tagged fusion protein in Escherichia coli
Quality Assessment of Recombinant Proteins Produced in Plants
Plant-based expression technologies for recombinant proteins have begun to receive acceptance for pharmaceuticals and other commercial markets. Protein products derived from plants offer safer, more cost-effective, and less capital-intensive
技术资料







