protein

Angiostatin Kringles 1-4, Human

MBS634949

0.05 mg

380 USD

Protein

Angiostatin Kringles 1-4, Human

Angiostatin Kringles 1-4

angiostatin; Plasminogen; plasminogen; angiostatin; plasmin heavy chain A; plasmin light chain B; plasminogen

Plg; Plg; Pg; AI649309

PLMN_MOUSE

Human fluid.

Highly Purified. ~ 98% (SDS-PAGE)

Supplied as a liquid in 20mM Hepes, 40mM sodium chloride, pH 8.0.

1mg/ml

Aliquot to avoid repeated freezing and thawing and store at -70 degree C. Aliqots are stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

ELISA (EL/EIA)

Activity: Biologically active. Human angiostatin significantly inhibits bFGF-induced endothelial cell proliferation and migration at concentration ranging from 300nM-1uM. Embryonic vascular system undergoes a series of complex, highly regulated series of events involving differentiation, migration and association of primitive endothelial cells. This process is termed vasculogenesis. A further remodeling of the primitive vascular system forms the mature cardiovascular system. This process is known as angiogenesis (sprouting of new capillary vessels from pre-existing vasculature). Angiogenesis accounts for the formation of vasculature into previously avascular organs such as brain and kidney. Angiogenic activity in the adult is required during the normal tissue repair, and for the remodeling of the female reproductive organs (ovulation and placental development). Certain pathological conditions, such as tumor growth and diabetic retinopathy, also require angiogenesis. Recent studies have identified several proteolytic fragments or cryptic domains of proteins that act as inhibitors of angiogenesis. These include fragments of plasminogen such as Angiostatin protein (kringles 1-4) and kringles 1-5, C-terminal proteolytic fragment of Collagen XVIII (Endostatin protein), the NC10 domain of collagen 15 (Restin), the C-terminal hemopexin-like domain of MMP-2 (PEX), the N-terminal fragment of prolactin, and the N-terminally truncated platelet factor. Angiostatin protein, a proteolytic fragment of plasminogen, is comprised of the first four kringle regions. It prevents the growth of endothelial cells, and its systemic administration inhibits the growth of primary carcinomas in mice. Kringles 1-3 fragment has a greater inhibitory activity than the Kringles 1-4 fragment. The protease-activated Kringles 1-5 is the most potent plasminogen fragment with over 50-fold greater endothelial cell specific inhibitory activity. Its systemic administration inhibited the growth of fibrosarcoma and significantly reduced neovascularization.

Molecular Biology; MB-Coagulation Factors

Purified human Kringles 1-4 (MW ~50kD doublet) is prepared from human fluids negative for HBsAg, HIV, and HCV.

38000582

AAR07361.1

P20918

50kD

Activation Of Matrix Metalloproteinases Pathway (819052); Blood Clotting Cascade Pathway (198388); Complement And Coagulation Cascades Pathway (198335); Complement And Coagulation Cascades Pathway (83270); Complement And Coagulation Cascades Pathway (484); Degradation Of The Extracellular Matrix Pathway (819051); Dissolution Of Fibrin Clot Pathway (819733); Extracellular Matrix Organization Pathway (819039); Hemostasis Pathway (819701); Influenza A Pathway (217174)

Plasminogen: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. Defects in PLG are the cause of plasminogen deficiency (PLGD). PLGD is characterized by decreased serum plasminogen activity. Two forms of the disorder are distinguished: type 1 deficiency is additionally characterized by decreased plasminogen antigen levels and clinical symptoms, whereas type 2 deficiency, also known as dysplasminogenemia, is characterized by normal, or slightly reduced antigen levels, and absence of clinical manifestations. Plasminogen deficiency type 1 results in markedly impaired extracellular fibrinolysis and chronic mucosal pseudomembranous lesions due to subepithelial fibrin deposition and inflammation. The most common clinical manifestation of type 1 deficiency is ligneous conjunctivitis in which pseudomembranes formation on the palpebral surfaces of the eye progresses to white, yellow-white, or red thick masses with a wood-like consistency that replace the normal mucosa. Belongs to the peptidase S1 family. Plasminogen subfamily. Protein type: Secreted; EC 3.4.21.7; Motility/polarity/chemotaxis; Protease; Secreted, signal peptide. Cellular Component: extrinsic to plasma membrane; extracellular space; extrinsic to external side of plasma membrane; cell surface; intracellular membrane-bound organelle; cell; plasma membrane; extracellular region. Molecular Function: peptidase activity; protein domain specific binding; hydrolase activity; serine-type peptidase activity; serine-type endopeptidase activity; endopeptidase activity; apolipoprotein binding; catalytic activity; receptor binding. Biological Process: tissue remodeling; proteolysis; myoblast differentiation; muscle maintenance; extracellular matrix disassembly; fibrinolysis; negative regulation of angiogenesis; negative regulation of fibrinolysis; proteolysis involved in cellular protein catabolic process; tissue regeneration; hemostasis; positive regulation of fibrinolysis; blood coagulation

0.05 mg

380 USD

0.1 mg

540