Difference between revisions of "Part:BBa K5374000"

 
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SPARC (Secreted Protein Acidic and Rich in Cysteine), also known as osteonectin, is a matricellular protein that influences cell-matrix interactions and has a strong affinity for collagen. It plays a role in tissue remodeling and wound healing. SPARC binds to various types of collagen, particularly type I collagen, facilitating cellular adhesion and migration.
 
SPARC (Secreted Protein Acidic and Rich in Cysteine), also known as osteonectin, is a matricellular protein that influences cell-matrix interactions and has a strong affinity for collagen. It plays a role in tissue remodeling and wound healing. SPARC binds to various types of collagen, particularly type I collagen, facilitating cellular adhesion and migration.
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SPARC (Secreted Protein Acidic and Rich in Cysteine) and OD (Osteonectin Domain): This domain is involved in regulating the interaction between cells and the extracellular matrix (ECM), particularly binding to collagen and influencing matrix remodeling. It plays a role in tissue repair and bone mineralization.
  
 
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Revision as of 07:23, 16 September 2024


SPARC/OD. A collagen-binding domain involved in tissue repair and bone mineralization through ECM in

SPARC (Secreted Protein Acidic and Rich in Cysteine), also known as osteonectin, is a matricellular protein that influences cell-matrix interactions and has a strong affinity for collagen. It plays a role in tissue remodeling and wound healing. SPARC binds to various types of collagen, particularly type I collagen, facilitating cellular adhesion and migration.

SPARC (Secreted Protein Acidic and Rich in Cysteine) and OD (Osteonectin Domain): This domain is involved in regulating the interaction between cells and the extracellular matrix (ECM), particularly binding to collagen and influencing matrix remodeling. It plays a role in tissue repair and bone mineralization.

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal EcoRI site found at 484
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal EcoRI site found at 484
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal EcoRI site found at 484
    Illegal BamHI site found at 288
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal EcoRI site found at 484
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal EcoRI site found at 484
  • 1000
    COMPATIBLE WITH RFC[1000]