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Mouse Anti-ERBB3 Recombinant Antibody (RTJ.1) (CBMAB-C11517-LY)

The product is antibody recognizes ERBB3. The antibody RTJ.1 immunoassay techniques such as: IHC-F.
See all ERBB3 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
RTJ.1
Antibody Isotype
IgM
Application
IHC-F

Basic Information

Immunogen
Human c-erbB-3 Peptide
Specificity
Human
Antibody Isotype
IgM
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Concentration
0.5 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Erb-B2 Receptor Tyrosine Kinase 3
Introduction
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. [provided by RefSeq, Jul 2008]
Entrez Gene ID
2065
UniProt ID
P21860
Alternative Names
Erb-B2 Receptor Tyrosine Kinase 3; V-Erb-B2 Avian Erythroblastic Leukemia Viral Oncogene Homolog 3; Tyrosine Kinase-Type Cell Surface Receptor HER3; Human Epidermal Growth Factor Receptor 3; Proto-Oncogene-Like Protein C-ErbB-3; EC 2.7.10.1; HER3; Lethal Congenital Contracture Syndrome 2; Receptor Tyrosine-Protein Kinase ErbB-3; P180-ErbB3;
Research Area
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 (PubMed:20682778).

May also be activated by CSPG5 (PubMed:15358134).

Involved in the regulation of myeloid cell differentiation (PubMed:27416908).
Biological Process
Cranial nerve development Source: BHF-UCL
Extrinsic apoptotic signaling pathway in absence of ligand Source: BHF-UCL
Heart development Source: BHF-UCL
Negative regulation of cell adhesion Source: BHF-UCL
Negative regulation of neuron apoptotic process Source: BHF-UCL
Negative regulation of secretion Source: BHF-UCL
Negative regulation of signal transduction Source: BHF-UCL
Nervous system development Source: GO_Central
Neuron apoptotic process Source: BHF-UCL
Peripheral nervous system development Source: BHF-UCL
Phosphatidylinositol 3-kinase signaling Source: BHF-UCL
Positive regulation of cell population proliferation Source: GO_Central
Positive regulation of kinase activity Source: GO_Central
Positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
Positive regulation of protein tyrosine kinase activity Source: BHF-UCL
Regulation of cell population proliferation Source: BHF-UCL
Schwann cell differentiation Source: BHF-UCL
Signal transduction Source: UniProtKB
Transmembrane receptor protein tyrosine kinase signaling pathway Source: BHF-UCL
Wound healing Source: BHF-UCL
Cellular Location
Isoform 1: Cell membrane
Isoform 2: Secreted
Involvement in disease
Lethal congenital contracture syndrome 2 (LCCS2):
A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy, and congenital non-progressive joint contractures (arthrogryposis). The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth. LCCS2 patients manifest craniofacial/ocular findings, lack of hydrops, multiple pterygia, and fractures, as well as a normal duration of pregnancy and a unique feature of a markedly distended urinary bladder (neurogenic bladder defect). The phenotype suggests a spinal cord neuropathic etiology.
Erythroleukemia, familial (FERLK):
An autosomal dominant myeloproliferative disorder characterized by neoplastic proliferation of erythroblastic and myeloblastic elements with atypical erythroblasts and myeloblasts in the peripheral blood. Disease penetrance is incomplete.
Topology
Extracellular: 20-643
Helical: 644-664
Cytoplasmic: 665-1342
PTM
Autophosphorylated (PubMed:20351256). Ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase (PubMed:20682778).

Tchekmedyian, V., Dunn, L., Sherman, E., Baxi, S. S., Grewal, R. K., Larson, S. M., ... & Ho, A. L. (2022). Enhancing radioiodine incorporation in BRAF-mutant, radioiodine-refractory thyroid cancers with Vemurafenib and the anti-ErbB3 monoclonal antibody CDX-3379: results of a pilot clinical trial. Thyroid, 32(3), 273-282.

De Bacco, F., Orzan, F., Erriquez, J., Casanova, E., Barault, L., Albano, R., ... & Boccaccio, C. (2021). ERBB3 overexpression due to miR-205 inactivation confers sensitivity to FGF, metabolic activation, and liability to ERBB3 targeting in glioblastoma. Cell Reports, 36(4), 109455.

Ngan, H. L., Liu, Y., Fong, A. Y., Poon, P. H. Y., Yeung, C. K., Chan, S. S. M., ... & Lui, V. W. Y. (2020). MAPK pathway mutations in head and neck cancer affect immune microenvironments and ErbB3 signaling. Life science alliance, 3(6).

Kiavue, N., Cabel, L., Melaabi, S., Bataillon, G., Callens, C., Lerebours, F., ... & Bidard, F. C. (2020). ERBB3 mutations in cancer: biological aspects, prevalence and therapeutics. Oncogene, 39(3), 487-502.

Hafeez, U., Parslow, A. C., Gan, H. K., & Scott, A. M. (2020). New insights into ErbB3 function and therapeutic targeting in cancer. Expert review of anticancer therapy, 20(12), 1057-1074.

Xu, X., Li, L., Li, X., Tao, D., Zhang, P., & Gong, J. (2020). Aptamer-protamine-siRNA nanoparticles in targeted therapy of ErbB3 positive breast cancer cells. International Journal of Pharmaceutics, 590, 119963.

Jang, W. J., Jung, S. K., Vo, T. T. L., & Jeong, C. H. (2019). Anticancer activity of paroxetine in human colon cancer cells: Involvement of MET and ERBB3. Journal of Cellular and Molecular Medicine, 23(2), 1106-1115.

Drilon, A., Somwar, R., Mangatt, B. P., Edgren, H., Desmeules, P., Ruusulehto, A., ... & Ganji, G. (2018). Response to ERBB3-Directed Targeted Therapy in NRG1-Rearranged CancersERBB3-Directed Targeted Therapy in NRG1-Rearranged Cancers. Cancer discovery, 8(6), 686-695.

Nguyen, D. Q., Hoang, D. H., Nguyen Vo, T. T., Huynh, V., Ghoda, L., Marcucci, G., & Nguyen, L. X. T. (2018). The role of ErbB3 binding protein 1 in cancer: Friend or foe?. Journal of cellular physiology, 233(12), 9110-9120.

Loree, J. M., Bailey, A. M., Johnson, A. M., Yu, Y., Wu, W., Bristow, C. A., ... & Raghav, K. (2018). Molecular landscape of ERBB2/ERBB3 mutated colorectal cancer. JNCI: Journal of the National Cancer Institute, 110(12), 1409-1417.

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For research use only. Not intended for any clinical use.

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