Analytical Data
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Gene name
DDR1
- Application
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Alternative Names
CD167a; CAK; DDR; EDDR1; MCK10; NEP; NTRK4; PTK3; PTK3A; RTK6; TRKE; Cell adhesion kinase; Epithelial discoidin domain receptor 1; Mammary carcinoma kinase 10
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by reducing SDS-PAGE.
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Uniprot
Q08345
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Expression Region
His568~Phe829
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Molecular Weight
33kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
DDR1 (Discoidin Domain Receptor 1) is a receptor tyrosine kinase that plays a crucial role in cellular communication, particularly in the context of cell adhesion and the response to extracellular matrix components. Its significance has been increasingly recognized in various fields, including cancer research, fibrosis, and neurodegenerative diseases. The DDR1 receptor is activated by collagens, which are key components of the extracellular matrix, and this interaction influences cellular processes such as proliferation, differentiation, and survival. Dysregulation of DDR1 signaling has been implicated in pathological conditions, making it a target of interest for therapeutic intervention. To understand its function and therapeutic potential better, researchers have turned to recombinant protein technologies to produce functional DDR1 proteins for in vitro studies. These studies aim to elucidate the molecular mechanisms underlying DDR1 signaling pathways and their effects on cellular behavior. By investigating the structure and function of DDR1, scientists hope to develop novel strategies to modulate its activity in disease contexts. Furthermore, the generation of DDR1 recombinant proteins allows for the identification of potential small molecule inhibitors that could be developed as drugs to modulate DDR1 activity and provide new avenues for treating diseases associated with its dysregulation. Overall, the study of DDR1 recombinant proteins represents a promising area of research with the potential to impact our understanding of its role in health and disease.
