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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 CD153 / CD30L / TNFSF8 Protein (Fc Tag)
- 库存:
99
- 供应商:
北京义翘神州科技股份有限公司
- 规格:
1.00 mg/5.00 µg/50.00 µg/100.00 µg/200.00 µg
| 规格: | 1.00 mg | 产品价格: | ¥22680.0 |
|---|---|---|---|
| 规格: | 5.00 µg | 产品价格: | ¥580.0 |
| 规格: | 50.00 µg | 产品价格: | ¥1080.0 |
| 规格: | 100.00 µg | 产品价格: | ¥1780.0 |
| 规格: | 200.00 µg | 产品价格: | ¥4520.0 |
蛋白名称:Human CD153 / CD30L / TNFSF8 Protein (Fc Tag)
蛋白构建:A DNA sequence encoding the extracellular domain (Gln 63-Asp 234) of human CD30 Ligand (NP_001235.1) was fused with the Fc region of human IgG1 at the N-terminus.
表达宿主:HEK293 Cells
蛋白纯度:> 95 % as determined by SDS-PAGE
蛋白活性:Measured by its binding ability in a functional ELISA. Immobilized human CD30L-hFc (Cat: 10040-H01H) at 2 μg/ml (100 μl/well) can bind human CD30/TNFRSF8-Fch (Cat: 10777-H03H), the EC50 of human CD30/TNFRSF8-Fch is 15-60 ng/mL.
蛋白内毒素:< 1.0 EU per μg of the protein as determined by the LAL method
预测N端:Arg 23
蛋白分子量:The recombinant human Fc/CD30L is a disulfide-linked homodimeric protein. The reduced monomer consists of 429 amino acids and has a predicted molecular mass of 47.8 kDa. As a result of glycosylation, the apparent molecular mass of rh Fc/CD30L monomer is approximately 60-65 kDa in SDS-PAGE under reducing conditions.
蛋白NP号:NP_001235.1
蛋白氨基酸序列:Gln63-Asp234
蛋白标签:N-human IgG1-Fc
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Clonality - X Chromosome Inactivation Assay
) Forward and reverse primers, each 20 µM (Human Androgen Receptor Gene (HUMARA) CAG trinucleotide repeat microsatellite primers are described in Allen et al) AmpliTaq Gold, 5 U/ml (Perkin Elmer) a 32P-dCTP, 20 µCi/µl (NEN) Gel-Mix 6 (Life Technologies
Clonality - X Chromosome Inactivation Assay
of HpaII and HhaI sites near the polymorphic CAG repeat in the human androgen-receptor gene correlates with X chromosome inactivation. Am J Hum Genet 51:1229-39, 1992 . Enomoto T, Fujita M, Inoue M, Tanzawa O, Nomura T, Shroyer K. Analysis
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
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