Recombinant human CD30 protein with C-terminal 6×His tag
Figure 1. Human CD30 Protein, His Tag on SDS-PAGE under reducing condition.
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| Amount : | 50 µg |
| Purification : | The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining. |
| Content : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose is added as protectants before lyophilization. |
| Storage condition : | Store at -80°C for 12 months (Avoid repeated freezing and thawing) |
| Alternative Name : | TNFRSF8,CD30,D1S166E,Ki-1 |
Expression Host : HEK293
The protein has a predicted molecular mass of 39.3 kDa after removal of the signal peptide. The apparent molecular mass of CD30-His is approximately 55-70 kDa due to glycosylation.
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor is expressed by activated, but not by resting, T and B cells. TRAF2 and TRAF5 can interact with this receptor, and mediate the signal transduction that leads to the activation of NF-kappaB. This receptor is a positive regulator of apoptosis, and also has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
The protein has a predicted molecular mass of 39.3 kDa after removal of the signal peptide. The apparent molecular mass of CD30-His is approximately 55-70 kDa due to glycosylation.
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor is expressed by activated, but not by resting, T and B cells. TRAF2 and TRAF5 can interact with this receptor, and mediate the signal transduction that leads to the activation of NF-kappaB. This receptor is a positive regulator of apoptosis, and also has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
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