Receptor Tyrosine-Protein Kinase ErbB-4 (ERBB4) Antibody
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Description
ERBB4 Antibody is a Rabbit Polyclonal against ERBB4.
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Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Target: Receptor Tyrosine-Protein Kinase ErbB-4 (ERBB4) Immunogen: v-erb-a erythroblastic leukemia viral oncogene homolog 4 (avian) |
| Host | Rabbit |
| Reactivity | Mouse, Rat |
| Assay Type | Concentration: 2 mg/ml |
| Recommended Dilution | WB: 1/500 - 1/1000, IHC: 1/50 - 1/100. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Observed MW | Observed MW: 180 kDa |
| Purity | ≥ 95% (SDS-PAGE) |
| Purification | Purified by immunogen affinity chromatography. |
| Size 1 | 100 µg |
| Form | Liquid |
| Tested Applications | ELISA, WB, IHC |
| Buffer | PBS, pH 7.3, with 0.02% sodium azide and 50% glycerol. |
| Availability | Shipped within 5-12 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q15303 |
| 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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