Human DDR2 Protein 3173

$270.00 – $900.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Lys22-Arg399

SKU: 3173parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	Q16832
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Discoidin domain receptor (DDR) 2 is a collagen receptor that is implicated in several cancer types including breast and prostate cancers. DDR2 might be closely associated with ovarian cancer progression and metastasis. Its high expression may serve as a potential prognostic biomarker in human ovarian cancer.
molecular weight	The protein has a predicted MW of 43.80 kDa. Due to glycosylation, the protein migrates to 60-70 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human DDR2 Protein 3173

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Discoidin domain receptor (DDR) 2 is a collagen receptor that is implicated in several cancer types including breast and prostate cancers. DDR2 might be closely associated with ovarian cancer progression and metastasis. Its high expression may serve as a potential prognostic biomarker in human ovarian cancer.
Protein names Discoidin domain-containing receptor 2 (Discoidin domain receptor 2) (EC 2.7.10.1) (CD167 antigen-like family member B) (Discoidin domain-containing receptor tyrosine kinase 2) (Neurotrophic tyrosine kinase, receptor-related 3) (Receptor protein-tyrosine kinase TKT) (Tyrosine-protein kinase TYRO10) (CD antigen CD167b)
Gene names DDR2,DDR2 NTRKR3 TKT TYRO10
Protein family Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
Mass 9606Da
Function Tyrosine kinase involved in the regulation of tissues remodeling (PubMed:30449416). It functions as a cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up-regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing.
Catalytic activity BINDING 569..577; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000255\|PROSITE-ProRule:PRU00159"; BINDING 608; /ligand="ATP"; /ligand_id="ChEBI:CHEBI:30616"; /evidence="ECO:0000305"
Subellular location Cell membrane ; Single-pass type I membrane protein .
Tissues Detected in osteocytes, osteoblastic cells in subchondral bone, bone lining cells, tibia and cartilage (at protein level). Detected at high levels in heart and lung, and at low levels in brain, placenta, liver, skeletal muscle, pancreas, and kidney.
Structure Binds hydroxyproline-rich sequence motifs in fibrillar, glycosylated collagen, such as the GQOGVMGFO motif, where O stands for hydroxyproline. Interacts with SRC. Interacts (tyrosine phosphorylated) with SHC1.
Post-translational modification N-glycosylated.; Tyrosine phosphorylated in response to collagen binding. Phosphorylated by SRC; this is required for activation and subsequent autophosphorylation on additional tyrosine residues.
Target Relevance information above includes information from UniProt accession: Q16832
The UniProt Consortium

Data

The purity of Human DDR2 is greater than 95% as determined by SEC-HPLC.

Human DDR2 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.