Analytical Data
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Gene name
DDR1
- Application
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Alternative Names
DDR1；CAK；EDDR1；NEP；Epithelial discoidin domain-containing receptor 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q08345-2
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Expression Region
444-876aa
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AA Sequence
RRLLSKAERRVLEEELTVHLSVPGDTILINNRPGPREPPPYQEPRPRGNP PHAAPCVPNGSAYSGDYMEPEKPGAPLLPPPPQNSVPHYAEADIVTLQGV TGGNTYAVPALPPGAVGDGPPRVDFPRSRLRFKEKLGEGQFGEVHLCEVD SPQDLVSLDFPLNVRKGHPLLVAVKILRPDATKNARNDFLKEVKIMSRLK DPNIIRLLGVCVQDDPLCMITDYMENGDLNQFLSAHQLEDKAAEGAPGDG QAAQGPTISYPMLLHVAAQIASGMRYLATLNFVHRDLATRNCLVGENFTI KIADFGMSRNLYAGDYYRVQGRAVLPIRWMAWECILMGKFTTASDVWAFG VTLWEVLMLCRAQPFGQLTDEQVIENAGEFFRDQGRQVYLSRPPACPQGL YELMLRCWSRESEQRPPFSQLHRFLAEDALNTV
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Molecular Weight
77 kDa
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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 primarily binds to collagen, playing a crucial role in various cellular processes including cell adhesion, migration, and signaling. Its involvement in pathological conditions such as fibrosis, cancer progression, and inflammation has made it a significant target for biomedical research. The understanding of DDR1's structure and function is essential for elucidating its mechanisms in these diseases. Research on DDR1 recombinant proteins aims to explore its functional roles at a molecular level, enabling scientists to investigate the receptor's signaling pathways and interactions with collagen and other extracellular matrix components. These studies can facilitate the development of targeted therapies that modulate DDR1 activity, potentially offering new strategies for treating conditions where DDR1 is implicated. Additionally, recombinant DDR1 proteins serve as valuable tools for drug screening and the discovery of novel collagen-based therapeutics. By generating and characterizing these proteins, researchers can better define their structural features and functional properties, paving the way for innovative approaches in both basic science and clinical applications.
