TSP is an adhesive protein that can bind to many different cell types, including hematopoietic progenitor cells. It possesses a number of functional domains that serve as receptor recognizing regions. The amino-terminal heparin-binding domain interacts with heparin, other glycosaminoglycans and glycolipids and likely recognizes specific cell surface proteoglycans. The central disulfide cross-linked region is responsible for high affinity binding to one of the CD antigens, CD36 . TSP has been demonstrated to bind to integrin-alpha-V , integrin-beta-3 and integrin-alpha-2b, integrin-beta-3. The carboxy-terminal region of TSP also contains at least one binding epitope for a cell receptor. TSP can interact with fibrinogen and fibronectin. TSP appears to be involved intimately in the regulation of cellular proliferation. It is expressed as an early response gene following treatment of cells with various mitogens and cytokines. It modulates the progression of cells through the cell cycle. It augments the proliferative response to EGF. TSP inhibits endothelial cell chemotactic response to bFGF and reduces their proliferative response to serum and bFGF.
Alternative Names
TSP1 ; THBS1 ; TSP
Quantity
10 µg
Regulatory
RUO
Source
Insect cells
Host
Human
Endotoxin Level
<1.0 EU/μg of recombinant protein as determined by the LAL method.
Biological Activity Comment
Not available at this time
Weight
140.0 kDa
Format
LiquidRecombinant Thrombospondin-1 is presented as liquid formulation of 0.3 M NaCl, 0.02 M NaH2PO4 pH 6.0 .
Purity
>95% as determined by SDS-PAGE
Storage
This cytokine should be stored in working aliquots at 2° - 8°C for one year.