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ERBB3 Recombinant Monoclonal Antibody

The recombinant antibody against ERBB3 was produced using a synthesized peptide derived from human ErbB3 as the immunogen. This antibody exists as a non-conjugated isotype Rabbit IgG, Affinity-chromatography purified. This antibody has been validated on ELISA, IF.

ADC-56736A

The recombinant antibody against ERBB3 was produced using a synthesized peptide derived from human ErbB3 as the immunogen. This antibody exists as a non-conjugated isotype Rabbit IgG, Affinity-chromatography purified. This antibody has been validated on ELISA, IF.

$350.00

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Specifications


Cat.No ADC-56736A ClonalityMonoclonal
Target NameERBB3Target SynonymsERBB3, HER3, Receptor tyrosine-protein kinase erbB-3 (EC 2.7.10.1) (Proto-oncogene-like protein c-ErbB-3) (Tyrosine kinase-type cell surface receptor HER3)
FormLiquidSpecies ReactivityHuman
IsotypeRabbit IgGStorage BufferPH 7.4, 0.02% sodium azide and 50% glycerol., 150mM NaCl, Rabbit IgG in phosphate buffered saline
Purification MethodAffinity-chromatography purifiedConjugateNon-conjugated
ApplicationELISA, IFStorageUpon receipt

Immunogen Information


Immunogen DescriptionA synthesized peptide derived from human ErbB3Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDP21860
Background Information
  • Uniprot Id

    P21860

  • Target Species

    Human

  • Target Name

    ERBB3

  • Target Full Name

    Receptor tyrosine-protein kinase erbB-3

  • Target Function

    Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5. Involved in the regulation of myeloid cell differentiation.

  • Target Involvement

    Lethal congenital contracture syndrome 2 (LCCS2)

  • Target Subcellular Location

    [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Secreted.

  • Target Protein Families

    Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily

  • Target Tissue Specificity

    Epithelial tissues and brain.

  • Target Synonyms

    c erbB 3; c erbB3; Erb b2 receptor tyrosine kinase 3; ErbB 3; ERBB3; ERBB3 protein; erbB3 S; ERBB3_HUMAN; Glial growth factor receptor; HER 3; HER3; Human epidermal growth factor receptor 3; LCCS2; MDA BF 1; MGC88033; p180 ErbB3; p45 sErbB3; p85 sErbB3; proto-oncogene-like protein c ErbB 3; proto-oncogene-like protein c ErbB3; Proto-oncogene-like protein c-ErbB-3; Receptor tyrosine protein kinase erbB 3; Receptor tyrosine protein kinase erbB3; Receptor tyrosine-protein kinase erbB-3; Tyrosine kinase type cell surface receptor HER3; Tyrosine kinase-type cell surface receptor HER3; v erb b2 avian erythroblastic leukemia viral oncogene homolog 3; v erb b2 erythroblastic leukemia viral oncogene homolog 3 (avian); v erb b2 erythroblastic leukemia viral oncogene homolog 3

  • Target Background

    This gene encodes a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. This membrane-bound protein has a neuregulin binding domain but not an active kinase domain. It therefore can bind this ligand but not convey the signal into the cell through protein phosphorylation. However, it does form heterodimers with other EGF receptor family members which do have kinase activity. Heterodimerization leads to the activation of pathways which lead to cell proliferation or differentiation. Amplification of this gene and/or overexpression of its protein have been reported in numerous cancers, including prostate, bladder, and breast tumors. Alternate transcriptional splice variants encoding different isoforms have been characterized. One isoform lacks the intermembrane region and is secreted outside the cell. This form acts to modulate the activity of the membrane-bound form. Additional splice variants have also been reported, but they have not been thoroughly characterized.

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