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Catalog Number | orb1290925 |
---|---|
Category | Proteins |
Description | Recombinant human TNFSF15 protein with N-terminal human Fc tag |
Reactivity | Human |
Tag | N-Human Fc Tag |
Form/Appearance | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8% trehalose is added as protectants before lyophilization. Please see Certificate of Analysis for specific instructions of reconstitution. |
Purity | The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining. |
MW | The protein has a predicted molecular mass of 46.6 kDa after removal of the signal peptide. The apparent molecular mass of hFc-TNFSF15 is approximately 35-55kDa due to glycosylation. |
Target | TNFSF15 |
UniProt ID | O95150 |
Source | Mammalian |
Storage | Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing). Lyophilized proteins are shipped at ambient temperature. |
Buffer/Preservatives | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8% trehalose is added as protectants before lyophilization. Please see Certificate of Analysis for specific instructions. |
Alternative names | TL1;VEGI Read more... |
Note | For research use only |
Expiration Date | 6 months from date of receipt. |
Human NTRK1 Protein, hFc Tag on SDS-PAGE under reducing condition.
The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining. | |
The protein has a predicted molecular mass of 47.6 kDa after removal of the signal peptide. The apparent molecular mass of hFc-mTNFSF15 is approximately 55-70 kDa due to glycosylation. | |
Mammalian |
The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining. | |
The protein has a predicted molecular mass of 46.6 kDa after removal of the signal peptide. The apparent molecular mass of hFc-cTNFSF15 is approximately 35-55 kDa due to glycosylation. | |
Mammalian |
97.30% | |
48.9 kDa (predicted) |