DDR1 Protein, Human (sf9, His-GST)

The DDR1 protein is a tyrosine kinase and cell surface receptor for fibrillar collagen that tightly regulates cell attachment and affects extracellular matrix processes. Upon collagen binding, DDR1 initiates a signaling cascade involving SRC, activating MAP kinase. DDR1 Protein, Human (sf9, His-GST) is the recombinant human-derived DDR1 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of DDR1 Protein, Human (sf9, His-GST) is 470 a.a., with molecular weight of ~80 kDa.

DDR1 protein serves as a tyrosine kinase and functions as a cell surface receptor for fibrillar collagen, playing a pivotal role in regulating cell attachment to the extracellular matrix and influencing processes such as extracellular matrix remodeling, cell migration, differentiation, survival, and proliferation. Upon collagen binding, DDR1 initiates a signaling cascade involving SRC and activates MAP kinases. This activation, in turn, leads to the up-regulation of matrix metalloproteinases MMP2, MMP7, and MMP9, facilitating extracellular matrix remodeling and promoting cell migration and wound healing. DDR1's significance extends to various physiological processes, including normal blastocyst implantation during pregnancy, mammary gland differentiation, lactation, and the maintenance of ear morphology and hearing. Additionally, DDR1 contributes to arterial wound healing by promoting smooth muscle cell migration and plays a role in tumor cell invasion, further underscoring its diverse functional repertoire. Notably, DDR1 phosphorylates PTPN11 as part of its regulatory activities.

Human

Sf9 insect cells

N-His;N-GST

Q08345 (R444-V913)

780  [NCBI]

Approximately 80 kDa

Greater than 80% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.