Human Akt1 Protein, His Tag & Strep Tag-null-试剂-生物在线
北京百普赛斯生物科技股份有限公司
Human Akt1 Protein, His Tag & Strep Tag

Human Akt1 Protein, His Tag & Strep Tag

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产品名称: Human Akt1 Protein, His Tag & Strep Tag

英文名称: Human Akt1 Protein, His Tag & Strep Tag

产品编号: AK1-H5283

产品价格: 0

产品产地: USA

品牌商标: ACROBiosystems

更新时间: null

使用范围: null

北京百普赛斯生物科技股份有限公司
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分子量:19.2 kDa

纯度:>92% as determined by SDS-PAGE.

内毒素:Less than 1.0 EU per μg of the Cynomolgus 4-1BB, His Tag by the LAL method.

Buffer:PBS, pH7.4

生物活性:Measured by its binding ability in a functional ELISA. Immobilized Cynomolgus 4-1BB, His Tag (Cat# 41B-C52H4) at 1μg/mL (100 l/well),can bind Human 4-1BB Ligand, Fc Tag (Cat# 41L-H5257) with a linear of 0.01-0.5 ng/mL.

产品特性:Cynomolgus 4-1BB, His Tag is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 19.2 kDa. The predicted N-terminus is Leu 24. The reducing (R) protein migrates as 30-40 kDa in SDS-PAGE .

产品背景:4-1BB is also known as CD137, tumor necrosis factor receptor superfamily member 9 (TNFRSF9), induced by lymphocyte activation (ILA), is a co-stimulatory molecule of the tumor necrosis factor (TNF) receptor superfamily. CD137 can be expressed by activated T cells, but to a larger extent on CD8 than on CD4 T cells. In addition, CD137 expression is found on dendritic cells, follicular dendritic cells, natural killer cells, granulocytes and cells of blood vessel walls at sites of inflammation. The best characterized activity of CD137 is its costimulatory activity for activated T cells. Crosslinking of CD137 enhances T cell proliferation, IL-2 secretion survival and cytolytic activity. Further, it can enhance immune activity to eliminate tumors in mice. CD137 can enhance activation-induced T cell apoptosis when triggered by engagement of the TCR/CD3 complex. In addition, 4-1BB/4-1BBL co-stimulatory pathway has been shown to augment secondary CTL responses to several viruses, and meanwhile augment anti-tumor immunity. 4-1BB thus is a promising candidate for immunotherapy of human cancer. CD137 has been shown to interact with TRAF2. 
SDS-PAGE