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Biotinylated Human DDR1 Protein, His,Avitag™ (MALS & BLI verified)

AIDD‑Ready
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DD1-H82E9-25ug
$360.00
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DD1-H82E9-200ug
$1,565.00
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DD1-H82E9
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Product Details
Performance Data
Reviews & Citations
Resources
  • Product Details
  • Performance Data
  • Reviews & Citations
  • Important Statement
  • Resources
Synonyms

CD167a

Source

Biotinylated Human DDR1, His,Avitag (DD1-H82E9) is expressed from human 293 cells (HEK293). It contains AA Asp 21 - Thr 416 (Accession # Q08345-1).

Predicted N-terminus: Asp 21

Molecular Characterization
Other Tags and Version Biotin & Other Labeled Version

This protein carries a polyhistidine tag at the C-terminus, followed by an Avi tag (Avitag™).

The protein has a calculated MW of 47.5 kDa. The protein migrates as 50-60 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Labeling

Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.

Protein Ratio

Passed as determined by the SABA assay / HABA assay / binding ELISA.

Purity

>95% as determined by SDS-PAGE.

>95% as determined by SEC-MALS.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

Reconstitution

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Shipping and Storage

This product is shipped at ambient temperature.

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:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.
ACRO Quality Management System

Background

Discoidin domain receptor 1 (DDR1) is a member of DDRs, which are members of the receptor tyrosine kinase (RTK). Upon collagen binding, DDR1 undergoes tyrosine autophosphorylation, which consequently triggers downstream genetic and cellular pathways and plays critical roles in the regulation of cellular morphogenesis, differentiation, proliferation, adhesion, migration, and invasion. Research shows that DDR1 is closely related to various human diseases including cancer, fibrosis, atherosclerosis, and other inflammatory disorders. New generation DDR1 inhibitors targeting the allosteric sites outside of the canonical ATP-binding pocket or extracellular domain (allosteric inhibitors) may offer a new opportunity for selective DDR1 inhibition therapy development.