| Species |
Human |
| Protein Construction |
Transferrin (Val20-Pro698)_x000D_
Accession # AAH59367 |
His |
| N-term |
C-term |
|
| Purity |
> 95% as determined by BisTris PAGE
> 95% as determined by HPLC |
| Endotoxin Level |
Less than 1EU per μg by the LAL method. |
| Biological Activity |
Measured by its binding ability in a functional ELISA. Immobilized Transferrin, His, Human at 2μg/ml (100μl/well) on the plate can bind Biotinylated Human Transferrin R, His Tag. Test result was comparable to standard batch. |
| Expression System |
HEK293 |
| Theoretical Molecular Weight |
76.3 kDa |
| Apparent Molecular Weight |
Due to glycosylation, the protein migrates to 78-82 kDa based on Bis-Tris PAGE result. |
| Formulation |
Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). |
| Reconstitution |
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water. |
| Storage & Stability |
Upon receiving, the product remains stable up to 6 months at -20 °C or below. Upon reconstitution, the product should be stable for 3 months at -80 °C. Avoid repeated freeze-thaw cycles. |
| Target Background |
Transferrin (Tf), an iron transporter, is mainly biosynthesized in the liver, but can also be biosynthesized in the brain; i.e., by oligodendrocytes and the choroid plexus, a cerebrospinal fluid (CSF) producing tissue. The CSF contains two Tf isoforms, brain-type Tf and serum-type Tf, which differ in their glycan structures. Brain-type Tf is uniquely glycolsylated with biantennary asialo- and agalacto-complex type N-glycans that carry bisecting β1,4-GlcNAc and core α1,6-Fuc. The glycans of serum-type Tf in the CSF are similar to those of Tf in serum. |
| Synonyms |
Serotransferrin; Transferrin; Siderophilin; TF; PRO1557; PRO2086; HEL-S-71p; TFQTL1 |
For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.
