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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:
IL29 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:
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: | ¥45885.0 |

CATALOGUE NUMBER
CYT-864
SYNONYMS
INTRODUCTION
IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
IFN-Lambda 1 antiviral and antiproliferative activity requires Interferon-Lambda 2 receptor tyrosine residues.
DESCRIPTION
SOURCE
PHYSICAL APPEARANCE
FORMULATION
STABILITY
PURITY
AMINO ACID SEQUENCE
SAFETY DATA SHEET
SDS
USAGE
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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文献和实验IL 29 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (20-200 a.a) and having a molecular mass of 22.7kDa.IL 29 is fused to a 23 amino acid His-tag at N-terminus & 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







