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Recombinant Human HER3/ErbB3 Protein (Fc Tag)(Active)– MSE Supplies LLC

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Recombinant Human HER3/ErbB3 Protein (Fc Tag)(Active)

SKU: PKSH031768-100

  • $ 65895



Recombinant Human HER3/ErbB3 Protein (Fc Tag)(Active)

 

SKU # PKSH031768
Expression Host HEK293 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 HEK293 Cells
Sequence Met 1-Thr 643
Accession NP_001973.2
Calculated Molecular Weight 95.4 kDa
Observed Molecular Weight 130-140 kDa
Tag C-hFc
Bio-activity Measure by its ability to bind with human NRG1-β1 in a functional ELISA.
  

 

Properties

Purity > 90 % as determined by reducing SDS-PAGE.
Endotoxin < 1.0 EU per μg 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 PBS, pH 7.4
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.