Human Receptor Tyrosine-Protein Kinase Erbb-4 (ERBB4) Protein
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Description
Human Receptor Tyrosine-Protein Kinase Erbb-4 (ERBB4) Protein is a recombinant Human protein produced in a Mammalian cell expression system.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Receptor Tyrosine-Protein Kinase Erbb-4 (ERBB4) |
| Host | Mammalian cells |
| Origin | Human |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 98.36 kDa Sequence Fragment: Gln26-His641 Tag: N-terminal Fc tag |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Size 1 | 100 µg |
| Size 2 | 1 mg |
| Form | Lyophilized Reconstitute in sterile water to produce a stock solution. |
| Tested Applications | ELISA, WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| Availability | Shipped within 5-12 working days. |
| Storage | Store at 2-8 °C if the entire vial will be used within 1 week. Aliquot and store at -20 °C for long-term storage. Avoid repeated freeze-thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q15303 |
| Background | Protein ERBB4 |
| Note | This product is for research use only. This product is shipped with ice packs. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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This gene is a member of the Tyr protein kinase family and the epidermal growth factor receptor subfamily. It encodes a single-pass type I membrane protein with multiple cysteine rich domains, a transmembrane domain, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins and other factors and induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. Mutations in this gene have been associated with cancer. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.
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