ErbB2/Her2 Protein (AA 23-652) (His tag)

Catalog No. ABIN2181214

Product Details

Target: ErbB2/Her2 (Receptor tyrosine-protein kinase erbB-2 (ErbB2/Her2))

Protein Type: Recombinant

Biological Activity: Active

Protein Characteristics: AA 23-652

Origin: Human

Source: HEK-293 Cells

Purification tag / Conjugate: This ErbB2/Her2 protein is labelled with His tag.

Sequence: AA 23-652

Characteristics: This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 70.2 kDa. The protein migrates as 110-115 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Purity: >95 % as determined by SDS-PAGE.

Sterility: 0.22 μm filtered

Endotoxin Level: Less than 1.0 EU per μg by the LAL method.

Application Details

Restrictions: For Research Use only

Handling

Format: Lyophilized

Buffer: PBS, pH 7.4

Handling Advice: Please avoid repeated freeze-thaw cycles.

Storage: -20 °C

Storage Comment: No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).

References

Hao, Yu, Bai, McBride, Huang: "Cryo-EM Structure of HER2-trastuzumab-pertuzumab complex." in: PLoS ONE, Vol. 14, Issue 5, pp. e0216095, (2020) (PubMed).

Shinozaki, Hashimoto, Fukui, Uchiyama: "Efficient generation of single domain antibodies with high affinities and enhanced thermal stabilities." in: Scientific reports, Vol. 7, Issue 1, pp. 5794, (2019) (PubMed).

Wang, Forterre, Zhao, Frimannsson, Delcayre, Antes, Efron, Jeffrey, Pegram, Matin: "Anti-HER2 scFv-Directed Extracellular Vesicle-Mediated mRNA-Based Gene Delivery Inhibits Growth of HER2-Positive Human Breast Tumor Xenografts by Prodrug Activation." in: Molecular cancer therapeutics, Vol. 17, Issue 5, pp. 1133-1142, (2019) (PubMed).

Hussack, Raphael, Lowden, Henry: "Isolation and characterization of camelid single-domain antibodies against HER2." in: BMC research notes, Vol. 11, Issue 1, pp. 866, (2019) (PubMed).

Ollier, Wassmann, Monney, Ries Fecourt, Gn, C A, Ayoub, Stutz, Gudi, Blein: "Single-step Protein A and Protein G avidity purification methods to support bispecific antibody discovery and development." in: mAbs, Vol. 11, Issue 8, pp. 1464-1478, (2019) (PubMed).

Rosenthal, Stone, Koski, Zimmerman: "LEAPS Vaccine Incorporating HER-2/neu Epitope Elicits Protection That Prevents and Limits Tumor Growth and Spread of Breast Cancer in a Mouse Model." in: Journal of immunology research, Vol. 2017, pp. 3613505, (2018) (PubMed).

Zhou, Chitneni, Devoogdt, Zalutsky, Vaidyanathan: "Fluorine-18 labeling of an anti-HER2 VHH using a residualizing prosthetic group via a strain-promoted click reaction: Chemistry and preliminary evaluation." in: Bioorganic & medicinal chemistry, Vol. 26, Issue 8, pp. 1939-1949, (2018) (PubMed).

Anami, Yamazaki, Xiong, Gui, Zhang, An, Tsuchikama: "Glutamic acid-valine-citrulline linkers ensure stability and efficacy of antibody-drug conjugates in mice." in: Nature communications, Vol. 9, Issue 1, pp. 2512, (2018) (PubMed).

Lowden, Henry: "Oxford nanopore sequencing enables rapid discovery of single-domain antibodies from phage display libraries." in: BioTechniques, Vol. 65, Issue 6, pp. 351-356, (2018) (PubMed).

Shukla, Myers, Woods, Gong, Czapar, Commandeur, Huang, Levine, Steinmetz: "Plant viral nanoparticles-based HER2 vaccine: Immune response influenced by differential transport, localization and cellular interactions of particulate carriers." in: Biomaterials, Vol. 121, pp. 15-27, (2017) (PubMed).

Dakshinamurthy, Mukunda, Prasad Kodaganti, Shenoy, Natarajan, Maliwalave, Halan, Murugesan, Maity: "Charge variant analysis of proposed biosimilar to Trastuzumab." in: Biologicals : journal of the International Association of Biological Standardization, Vol. 46, pp. 46-56, (2017) (PubMed).

Nath, Flemming, Godat, Urh: "Development of NanoLuc bridging immunoassay for detection of anti-drug antibodies." in: Journal of immunological methods, Vol. 450, pp. 17-26, (2017) (PubMed).

Ambrosetti, Paoletti, Bosco, Parisse, Scaini, Tagliabue, de Marco, Casalis: "Quantification of Circulating Cancer Biomarkers via Sensitive Topographic Measurements on Single Binder Nanoarrays." in: ACS omega, Vol. 2, Issue 6, pp. 2618-2629, (2017) (PubMed).

Stojanović, van der Velden, Mulder, Schasfoort, Terstappen: "Quantification of antibody production of individual hybridoma cells by surface plasmon resonance imaging." in: Analytical biochemistry, Vol. 485, pp. 112-8, (2016) (PubMed).

NDong, Tate, Kett, Batra, Demidenko, Lewis, Hoopes, Gerngross, Griswold: "Tumor Cell Targeting by Iron Oxide Nanoparticles Is Dominated by Different Factors In Vitro versus In Vivo." in: PLoS ONE, Vol. 10, Issue 2, pp. e0115636, (2015) (PubMed).

Target Details

Target: ErbB2/Her2 (Receptor tyrosine-protein kinase erbB-2 (ErbB2/Her2))

Alternative Name: Her2 (ErbB2/Her2 Products)

Background: Human Epidermal growth factor Receptor 2 (HER2) is also called ERBB2, HER-2,HER-2 /neu, NEU, NGL,TKR1 and c-erb B2,and is a protein giving higher aggressiveness in breast cancers. It is a member of the ErbB protein family, more commonly known as the epidermal growth factor receptor family. HER2 is a cell membrane surface-bound receptor tyrosine kinase and is normally involved in the signal transduction pathways leading to cell growth and differentiation. HER2 is thought to be an orphan receptor, with none of the EGF family of ligands able to activate it. Approximately 30 % of breast cancers have an amplification of the HER2 gene or overexpression of its protein product. Overexpression of this receptor in breast cancer is associated with increased disease recurrence and worse prognosis. HER2 appears to play roles in development, cancer, communication at the neuromuscular junction and regulation of cell growth and differentiation .

Molecular Weight: 70.2 kDa

NCBI Accession: NP_004439

Pathways: RTK Signaling, Fc-epsilon Receptor Signaling Pathway, EGFR Signaling Pathway, Neurotrophin Signaling Pathway, Skeletal Muscle Fiber Development