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Human ErbB3 / Her3 Protein, Strep Tag  pdf  pdf  pdf


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ER3-H5288-25ug
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ER3-H5288-250ug
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Synonym

ERBB3, HER3, LCCS2, MDA-BF-1, MGC88033, c-erbB3, erbB3-S, p180-ErbB3, p45-sErbB3, p85-sErbB3

Source

Recombinant Human ErbB-3 /HER3 Protein, With C-Twin Strep Tag (rh ErbB3/HER3,twin strep tag) Ser 20 - Thr 643 (Accession # NP_001973.2) was produced in human 293 cells (HEK293) at ACROBiosystems.

Molecular Characterization

rh ErbB3/HER3,twin strep tag is fused with a Twin-Strep tag at the C-terminus, and has a calculated MW of 71.7 kDa. The predicted N-terminus is Ser 20. DTT-reduced Protein migrates as 100-110 kDa in SDS-PAGE due to glycosylation.

Endotoxin

Less than 1.0 EU per μg of the rh ErbB3/HER3,twin strep tag by the LAL method.

Purity

>95% as determined by SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization.

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Reconstitution

See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage

Avoid repeated freeze-thaw cycles.

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

 

SDS-PAGE


Recombinant Human ErbB-3 /HER3 Protein, With C-Twin Strep Tag
The purity of rh ErbB3/HER3,twin strep tag was determined by DTT-reduced (+) SDS-PAGE and staining overnight with Coomassie Blue.
 
 

Background

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.

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References

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