Recombinant Human HER3/ErbB3 Protein (aa 730-1065, His &GST Tag)(Active)

Recombinant Human HER3/ErbB3 Protein (aa 730-1065, His &GST Tag)(Active)

SKU #	PKSH031765
Expression Host	Baculovirus-Insect Cells

Description

Synonyms	EEBB3,ErbB-3,HER3,LCCS2,MDA-BF-1,c-erbB-3,c-erbB3,erbB3-S,p180-ErbB3,p45-sErbB3,p85-sErbB3
Species	Human
Expression Host	Baculovirus-Insect Cells
Sequence	Pro 730-Ser 1065
Accession	NP_001973.2
Calculated Molecular Weight	65.0 kDa
Observed Molecular Weight	65 kDa
Tag	N-His-GST
Bio-activity	1. No Kinase Activity 2. Using the Octet RED System, the affinity constant (Kd) of human ErBB3-GST bound to human NRG1 (aa 2-224) was 20 nM.

Properties

Purity	> 75 % as determined by reducing SDS-PAGE.
Endotoxin	< 1.0 EU per g of the protein as determined by the LAL method.
Storage	Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80. Reconstituted protein solution can be stored at 4-8 for 2-7 days. Aliquots of reconstituted samples are stable at < -20 for 3 months.
Shipping	This product is provided as lyophilized powder which is shipped with ice packs.
Formulation	Lyophilized from sterile 50mM Tris, 100mM NaCl, pH 7.5, 10% glycerol, 1mM GSH Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual.
Reconstitution	Please refer to the printed manual for detailed information.

Background
ErbB3, also known as Her3(human epidermal growth factor receptor3), 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., and therefore can not mediate the intracellular signal transduction through protein phosphorylation. However, its heterodimer with ErbB2 or other EGFR members responsible for tyrosine phosphorylation forms a receptor complex with high affinity, and initiates the related pathway which lead to cell proliferation or differentiation. ErbB3 has been shown to implicated 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.