Recombinant human Her2 Protein with C-6×His tag
Figure 1. Human Her2 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 : | ERBB2,CD340,HER-2/neu,HER2,MLN19,NEU,NGL,TKR1 |
Expression Host : HEK293
The protein has a predicted molecular mass of 70.2 kDa after removal of the signal peptide.The apparent molecular mass of Her2-His is approximately 100-130 kDa due to glycosylation.
This gene encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized.
The protein has a predicted molecular mass of 70.2 kDa after removal of the signal peptide.The apparent molecular mass of Her2-His is approximately 100-130 kDa due to glycosylation.
This gene encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized.
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