Cat: IPD-X14434

Recombinant Human DDR1 Protein(HEK293) , His

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Analytical Data

  • Gene name

    DDR1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    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 (By similarity). Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11.

  • Species

    Human

  • Source

    HEK293

  • Tag

    C- His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    Q08345

  • Expression Region

    21-417aa

  • Molecular Weight

    46.8 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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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.

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