ARG70764
Human HER2 recombinant protein (Active) (His-tagged, C-ter)
Human HER2 recombinant protein (Active) (His-tagged, C-ter) for SDS-PAGE
Overview
| Product Description | HEK293 expressed, His-tagged (C-ter) Active Human HER2 recombinant protein |
|---|---|
| Tested Application | SDS-PAGE |
| Target Name | HER2 |
| Species | Human |
| A.A. Sequence | Thr23 - Thr652 |
| Expression System | HEK293 |
| Activity | Active |
| Activity Note | Determinedd by its ability to bind human Her2 Antibody in functional ELISA. Immobilized Recombinant human Her2 Protein can bind human Her2 Antibody. |
| Alternate Names | Phospho HER2 antibody; Phospho Receptor tyrosine-protein kinase erbB-2 antibody; ERBB2 / HER2 antibody; ERBB2 / HER2 phospho (Tyr877) antibody |
Properties
| Form | Powder |
|---|---|
| Purification Note | Endotoxin level is less than 0.1 EU/µg of the protein, as determined by the LAL test. |
| Purity | > 85% (by SDS-PAGE) |
| Buffer | PBS (pH 7.4) |
| Reconstitution | It is recommended to reconstitute the lyophilized protein in sterile water to a concentration not less than 200 μg/mL and incubate the stock solution for at least 20 min at room temperature to make sure the protein is dissolved completely. |
| Storage Instruction | For long term, lyophilized protein should be stored at -20°C or -80°C. After reconstitution, aliquot and store at -20°C or -80°C for up to one month. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. |
| Note | For laboratory research only, not for drug, diagnostic or other use. |
Bioinformation
| Gene Symbol | ERBB2 |
|---|---|
| Gene Full Name | Phospho Receptor tyrosine-protein kinase erbB-2 (HER2) Antibody Duo |
| Background | Her2 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. [provided by RefSeq, Jul 2008] |
| Function | Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization. In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth. [UniProt] |
| PTM | Autophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit (Probable). Ligand-binding increases phosphorylation on tyrosine residues (PubMed:27134172). Signaling via SEMA4C promotes phosphorylation at Tyr-1248 (PubMed:17554007). Dephosphorylated by PTPN12 (PubMed:27134172). |
