DDR1 Kinase / MCK10 / CD167 recombinant protein

Recombinant Mouse DDR1 Kinase / MCK10 / CD167 Protein (Fc tag)

Cat. Num. AAA2546766

• Gene Names: Ddr1; Cak; Nep; PTK3A; CD167a; AI323681; 6030432F18
• Purity: > 95 % as determined by SDS-PAGE
• Synonyms: DDR1 Kinase / MCK10 / CD167; Recombinant Mouse DDR1 Kinase / MCK10 / CD167 Protein (Fc tag); CR974483.1; 6030432F18; AI323681; CD167a; Cak; Nep; PTK3A; DDR1 Kinase / MCK10 / CD167 recombinant protein

• Host: Human Cells
• Purity/Purification: > 95 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 874

• Application Notes: The secreted recombinant mouse DDR1/Fc is a disulfide-linked homodimer. The reduced monomer comprises 636 amino acids and has a calculated molecular mass of 71 kDa. As a result of glycosylation, the apparent molecular mass of rmDDR1/Fc monomer is approximately 80-90 kDa in SDS-PAGE under reducing conditions.
• Predicted N Terminal: Asp 20
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for DDR1 Kinase / MCK10 / CD167 recombinant protein

Background: Discoidin domain receptor family, member 1 (DDR1), also known as or CD167a (cluster of differentiation 167a), and Mammary carcinoma kinase 10 (MCK10), belongs to a subfamily of tyrosine kinase receptors with an extracellular domain homologous to Dictyostellium discoideum protein discoidin 1. Receptor tyrosine kinases play a key role in the communication of cells with their microenvironment. These kinases are involved in the regulation of cell growth, differentiation and metabolism. Expression of DDR1/MCK10/CD167 is restricted to epithelial cells, particularly in the kidney, lung, gastrointestinal tract, and brain. In addition, it has been shown to be significantly overexpressed in several human tumors. DDR1/MCK10/CD167 plays an important role in regulating attachment to collagen, chemotaxis, proliferation, and MMP production in smooth muscle cells. DDR1 functions in a feedforward loop to increase p53 levels and at least some of its effectors. Inhibition of DDR1 function resulted in strikingly increased apoptosis of wild-type p53-containing cells in response to genotoxic stress through a caspase-dependent pathway.

Description: A DNA sequence encoding the extracellular domain of mouse DDR1 (NP_766550.1) (Met 1-Thr 414) was fused with the Fc region of human IgG1 at the C-terminus

NCBI and Uniprot Product Information

• NCBI GI #: 119709814
• NCBI GeneID: 12305
• NCBI Accession #: NP_766550.1
• NCBI GenBank Nucleotide #: NM_172962.1
• UniProt Accession #: Q03146
• Molecular Weight: 97,207 Da
• NCBI Official Full Name: epithelial discoidin domain-containing receptor 1 isoform 2
• NCBI Official Synonym Full Names: discoidin domain receptor family, member 1
• NCBI Official Symbol: Ddr1
• NCBI Official Synonym Symbols: Cak; Nep; PTK3A; CD167a; AI323681; 6030432F18
• NCBI Protein Information: epithelial discoidin domain-containing receptor 1
• UniProt Protein Name: Epithelial discoidin domain-containing receptor 1
• UniProt Gene Name: Ddr1
• UniProt Synonym Gene Names: Cak; Eddr1; Mpk6; Epithelial discoidin domain receptor 1

Uniprot Description

DDR1: Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing. Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11. Interacts (via PPxY motif) with WWC1 (via WW domains) in a collagen-regulated manner. Forms a tripartite complex with WWC1 and PRKCZ, but predominantly in the absence of collagen. Interacts (tyrosine phosphorylated) with SHC1. Interacts with SRC. Interacts with MYH9. Interacts with CDH1. Interacts with PTPN11. Interacts with NCK2. Detected in T-47D, MDA-MB-175 and HBL-100 breast carcinoma cells, A-431 epidermoid carcinoma cells, SW48 and SNU-C2B colon carcinoma cells and Hs 294T melanoma cells. 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. Abundant in breast carcinoma cell lines. In the colonic mucosa, expressed in epithelia but not in the connective tissue of the lamina propria. In the thyroid gland, expressed in the epithelium of the thyroid follicles. In pancreas, expressed in the islets of Langerhans cells, but not in the surrounding epithelial cells of the exocrine pancreas. In kidney, expressed in the epithelia of the distal tubules. Not expressed in connective tissue, endothelial cells, adipose tissue, muscle cells or cells of hematopoietic origin. Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. 5 isoforms of the human protein are produced by alternative splicing.

Protein type: DDR family; EC 2.7.10.1; Kinase, protein; Membrane protein, integral; Protein kinase, TK; Protein kinase, tyrosine (receptor); TK group

Chromosomal Location of Human Ortholog: 17 B1|17 18.7 cM

Cellular Component: basolateral plasma membrane; extracellular space; plasma membrane; receptor complex

Molecular Function: collagen binding

Biological Process: ear development; embryo implantation; negative regulation of cell proliferation; peptidyl-tyrosine phosphorylation; protein amino acid autophosphorylation; regulation of cell growth; regulation of cell-matrix adhesion; smooth muscle cell migration