Mouse DDR1 / CD167a Protein (GST Tag)

Produkt-Information von DDR1 / CD167a Protein

QC Testing von DDR1 / CD167a Protein

Purity:	> 95 % as determined by SDS-PAGE	SDS-PAGE: DDR1 / CD167a protein
Endotoxin:	< 1.0 EU per μg of the protein as determined by the LAL method
Stability:	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal:	Met
Molecular Mass:	The recombinant mouse DDR1/GST chimera consists of 668 amino acids and has a calculated molecular mass of 75.8kDa. The recombinant protein migrates as an approximately 68 kDa band in SDS-PAGE under reducing conditions.
Formulation:	Lyophilized from a 0.2μm filtered solution of 20mM Tris, 500mM NaCl, pH 7.4, 10%glycerol, 2mM DTT. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.

Usage Guide von DDR1 / CD167a Protein

Verwandte Produkte & Themen von DDR1 / CD167a Protein

Enzyme>>Protein Kinase>>Receptor Tyrosine Kinase>>DDR1/MCK10/CD167

Signal Transduction>>Protein Kinase>>Receptor Tyrosine Kinase>>DDR1/MCK10/CD167

Cancer>>Growth Factor & Receptor>>Receptor Tyrosine Kinase>>DDR1/MCK10/CD167

Immunology>>Cluster of Differentiation>>Other>>DDR1/MCK10/CD167

Beschreibung von DDR1 / CD167a Protein

Mouse epithelial discoidin domain-containing receptor 1, also known as Tyrosine kinase DDR, Discoidin receptor tyrosine kinase, CD167a, and DDR1, is a single-pass type I membrane protein. It belongs to the protein kinase superfamily and Insulin receptor subfamily. DDR1 contains one?F5/8 type C domain and one protein kinase domain. DDR1 is expressed at low levels in most adult tissues and is highest in the brain, lung, placenta and kidney. Lower levels of expression are detected in melanocytes, heart, liver, skeletal muscle and pancreas. DDR1 is abundantly expressed in breast carcinoma cell lines. DDR1 regulates cell adhesion and a broad range of cell behavior. DDR1 plays an important role as a collagen receptor, mediating intimal thickening after vascular injury. DDR1 and DDR2 are tyrosine kinase receptors activated by triple-helical collagens. Aberrant expression and signaling of these receptors have been implicated in several human diseases linked to accelerated matrix degradation and remodeling including tumor invasion, atherosclerosis and liver fibrosis.

References

1. Hou G. et al., 2001, J Clin Invest. 107 (6): 727-35.
2. Abdulhussein R. et al., 2004, J Biol Chem. 279 (30): 31462-70.
3. Mihai C. et al., 2009, J Mol Biol. 385 (2): 432-45.
4. Wang CZ. et al., 2009, Am J Physiol Cell Physiol. 297 (2): C419-29.
5. Flynn LA. et al., 2010, J Mol Biol. 395 (3): 533-43.

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