DDR2 Protein, Human (sf9, His-GST)

The DDR2 protein is a tyrosine kinase critical in tissue remodeling, acting as a cell surface receptor for fibrillar collagen and affecting cell differentiation, extracellular matrix remodeling, migration, and proliferation. DDR2 is critical for bone development and centrally regulates osteoblast differentiation and chondrocyte maturation through MAP kinase signaling and activation of RUNX2. DDR2 Protein, Human (sf9, His-GST) is the recombinant human-derived DDR2 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of DDR2 Protein, Human (sf9, His-GST) is 434 a.a., with molecular weight of ~77 kDa.

DDR2 protein, a tyrosine kinase integral to the regulation of tissue remodeling, functions as a cell surface receptor for fibrillar collagen, exerting control over cell differentiation, extracellular matrix remodeling, cell migration, and proliferation. Crucial for normal bone development, DDR2 plays a central role in osteoblast differentiation and chondrocyte maturation through a signaling pathway involving MAP kinases, culminating in the activation of the transcription factor RUNX2. Additionally, DDR2 regulates extracellular matrix remodeling by up-regulating collagenases MMP1, MMP2, and MMP13, thereby facilitating cell migration and tumor cell invasion. Its involvement extends to promoting fibroblast migration and proliferation, contributing to the dynamic process of cutaneous wound healing.

Human

Sf9 insect cells

N-His;N-GST

Q16832 (R422-E855)

4921  [NCBI]

Approximately 77 kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.