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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:
IL22, Sf9
- 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:
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: | ¥20286.0 |

CATALOGUE NUMBER
CYT-1092
SYNONYMS
INTRODUCTION
DESCRIPTION
IL22 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (34-179 a.a.) fused to a 9 aa His Tag at C-terminus containing a total of 155 amino acids and having a molecular mass of 17.8kDa.
IL22 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
SOURCE
Sf9, Baculovirus cells.
PHYSICAL APPEARANCE
Sterile filtered colorless solution.
FORMULATION
IL22 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 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.
PURITY
Greater than 90.0% as determined by SDS-PAGE.
AMINO ACID SEQUENCE
ADPAPISSHC RLDKSNFQQP YITNRTFMLA KEASLADNNT DVRLIGEKLF HGVSMSERCY LMKQVLNFTL EEVLFPQSDR FQPYMQEVVP FLARLSNRLS TCHIEGDDLH IQRNVQKLKD TVKKLGESGE IKAIGELDLL FMSLRNACIH HHHHH.
BIOLOGICAL ACTIVITY
The ED50 as determined by its ability to induce IL-10 secretion using COLO 205 human colorectal adenocarcinoma cell is ≤ 1.2 ng/ml.
SAFETY DATA SHEET
SDS
USAGE
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文献和实验IL22 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (34-179 a.a.) fused to a 9 aa His Tag at C-terminus containing a total of 155 amino acids and having a molecular mass of 17.8kDa.
IL22 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Lectin Glycoprofiling of Recombinant Therapeutic Interleukin-7
glycoproteins and particularly relevant for a first study of lot-to-lot comparison, or detection of unwanted glycans. In this chapter, we describe a lectin array-type method specifically designed for the study of recombinant therapeutic interleukin-7 (rhIL
Purification of Recombinant p53 from Sf9 Insect Cells
We describe a method for purifying recombinant p53 from baculovirus infected cells in one step by anion exchange chromatography. The p53 is full-length with no flanking sequences and its expression is driven by the baculovirus polyhedron
Cell surface expression of recombinant olfactory receptors (ORs) is a major limitation in characterizing their functional nature. We have shown that the recombinant expression of a human OR, OR 17-210, in the baculovirus/Sf9
技术资料




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