- ￥2310 - 5820
- Sino Biological
- 北京
- 10818-H32H
- 2025年08月12日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
-20℃ to -80℃
- 保质期：
12个月
- 英文名：
Recombinant Human CD38 Protein (His & FLAG Tag)
- 库存：
99
- 供应商：
北京义翘神州科技股份有限公司
- 规格：
10.00 µg/20.00 µg/50.00 µg
| 规格： | 10.00 µg | 产品价格： | ￥2310.0 |
|---|---|---|---|
| 规格： | 20.00 µg | 产品价格： | ￥3870.0 |
| 规格： | 50.00 µg | 产品价格： | ￥5820.0 |
蛋白名称：CD38蛋白, CD38 protein
蛋白构建：A DNA sequence encoding the extracellular domain of human CD38 (NP_001766.2) (Val 43 – Ile 300) was fused with a polyhistidine tag and a flag tag at the N-terminus.
表达宿主：HEK293 Cells
蛋白纯度：> 93 % as determined by SDS-PAGE
蛋白活性：0
蛋白内毒素：< 1.0 EU per μg of the protein as determined by the LAL method
预测N端：His
蛋白分子量：The secreted recombinant human CD38 comprises 285 amino acids with a predicted molecular mass of 33.2 kDa. As a result of glycosylation, rhCD38 migrates as an approximately 42-45 kDa band in SDS-PAGE under reducing conditions.
蛋白NP号：NP_001766.2
蛋白氨基酸序列：Val43-Ile300
蛋白标签：N-His & FLAG
蛋白保存条件：Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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文献和实验Strep/FLAG Tandem Affinity Purification (SF‐TAP) to Study Protein Interactions
a methodological workflow based on an SF?TAP tag comprising a doublet Strep?tag II and a FLAG moiety optimized for rapid as well as efficient tandem affinity purification of native proteins and protein complexes in higher eukaryotic cells. Depending
Using the scan‐x Web Site to Predict Protein Post‐Translational Modifications
spectrometry data is providing evidence that almost every protein in the cell undergoes some form of post?translational modification. We describe a protocol to use the scan?x Web site to view predicted acetylation sites in the human proteome and predicted
Protein Components of the microRNA Pathway and Human Diseases
, Exportin-5 (Exp-5), TAR RNA binding protein (TRBP) and fragile X mental retardation protein (FMRP), are each related, in various ways, to specific genetic diseases.
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