Receptor Tyrosine-Protein Kinase ErbB-4 (ERBB4) Antibody
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Description
ERBB4 Antibody is a Mouse Monoclonal against ERBB4.
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Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Target: Receptor Tyrosine-Protein Kinase ErbB-4 (ERBB4) Immunogen: Purified recombinant fragment of human ERBB4 (AA: 1159-1308) expressed in E. coli. |
| Host | Mouse |
| Reactivity | Human |
| Assay Type | Concentration: 1 mg/ml |
| Recommended Dilution | ELISA: 1/10000, IHC: 1/200 - 1/1000, FCM: 1/200 - 1/400. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Monoclonal |
| Isotype | IgG1 |
| Observed MW | 146.8 kDa |
| Purification | Purified from ascites by Protein G chromatography. |
| Size 1 | 100 µl |
| Form | Liquid |
| Tested Applications | ELISA, IHC, FCM |
| Buffer | PBS, containing 0.05% sodium azide. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q15303 |
| Gene ID | 2066 |
| OMIM | 600543 |
| Background | Antibody anti-ERBB4 |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. |
Descripción
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ERBB4 antibody
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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