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ERBB3,HER3,LCCS2,MDA-BF-1,MGC88033,c-erbB3,erbB3-S,p180-ErbB3,p45-sErbB3,p85-sErbB3
MABSol® Biotinylated Human ErbB3, His Tag, primary amine labeling (ER3-H8223) is expressed from human HEK293 cells. It contains AA Ser 20 - Thr 643 (Accession # NP_001973.2). It is the biotinylated form of Human ErbB3, His Tag (ER3-H5223).
Predicted N-terminus: Ser 20
Request for sequence
This protein carries a polyhistidine tag at the C-terminus
The protein has a calculated MW of 69.5 kDa. The protein migrates as 85-95 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
The primary amines in the side chains of lysine residues and the N-terminus of the protein are conjugated with biotins using standard chemical labeling method. A standard biotin reagent (13.5 angstroms) is used in this product.
Passed as determined by the HABA assay / binding ELISA.
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
>90% as determined by SEC-MALS.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.
Contact us for customized product form or formulation.
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
ErbB3,also known as Her3 (human epidermal growth factor receptor 3), is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. This membrane-bound glycoprotein has a neuregulin binding domain but has not an active kinase domain. It therefore can bind the ligand but cannot mediate the intracellular signal transduction through protein phosphorylation. However, it does form heterodimers with ErbB2 or other EGFR members responsible for tyrosine phosphorylation to give a receptor complex and initiate the related pathway, which lead to cell proliferation or differentiation. Overexpression of this protein has been reported in numerous cancers, including prostate, bladder, and breast tumors. This protein has different isoforms derived from alternative splicing variants, and among which, the secreted isoform lacking the intermembrane region modulates the activity of membrane-bound form.
