Other Proteins

Recombinant Human ANGPTL-7 (Legacy Tebubio ref. 167130-22). Angiopoietin-like 7 (ANGPTL-7), or Cornea-Derived Transcript 6 (CDT6), is a member of the angiopoietin family of structurally related proteins, characterized by a coiled N-terminal domain and a C-terminal fibrinogen like domain. While ANGPTL-7 shares the structural features of the angiopoietin family, it plays a critical role in blocking the vascular endothelial Tie2 receptor to which other family members bind. Through the blocking of the Tie2 receptor, ANGPTL-7 does not act as a "true" angiopoietin, but rather as a morphogen that contributes to the avascularity and transparency of the cornea during both embryo and adult development. Human ANGPTL-7 is expressed at high levels in the avascular corneal stromal layer, a site of pathological angiogenesis normally devoid of blood vessels, suggesting that the protein acts as a negative regulator of angiogenesis in a manner similar to that of angiopoietin-1 and angiopoietin-2. In mou

Recombinant Human ANGPTL-7 (Legacy Tebubio ref. 167130-22). Angiopoietin-like 7 (ANGPTL-7), or Cornea-Derived Transcript 6 (CDT6), is a member of the angiopoietin family of structurally related proteins, characterized by a coiled N-terminal domain and a C-terminal fibrinogen like domain. While ANGPTL-7 shares the structural features of the angiopoietin family, it plays a critical role in blocking the vascular endothelial Tie2 receptor to which other family members bind. Through the blocking of the Tie2 receptor, ANGPTL-7 does not act as a "true" angiopoietin, but rather as a morphogen that contributes to the avascularity and transparency of the cornea during both embryo and adult development. Human ANGPTL-7 is expressed at high levels in the avascular corneal stromal layer, a site of pathological angiogenesis normally devoid of blood vessels, suggesting that the protein acts as a negative regulator of angiogenesis in a manner similar to that of angiopoietin-1 and angiopoietin-2. In mou

Recombinant Murine Granzyme B (Legacy Tebubio ref. 167140-03). Granzyme B is a cysteine protease found in the cytoplasmic granules of cytolytic T lymphocytes (CTL) and natural killer (NK) cells. Granzyme B is required for the induction of target cell lysis, which occurs as part of cell-mediated immune responses, and can activate apoptosis in target cells by both caspase-dependent and caspase-independent mechanisms. Proteolytic cleavage of substrates by Granzyme B takes place primarily after aspartic acid residues. Recombinant Murine Granzyme B is a glycosylated 227 amino acid protein, comprising the mature active portion of the murine Granzyme B precursor. The apparent molecular weight is 28.9 kDa by mass spectrometry.

Recombinant Murine Granzyme B (Legacy Tebubio ref. 167140-03). Granzyme B is a cysteine protease found in the cytoplasmic granules of cytolytic T lymphocytes (CTL) and natural killer (NK) cells. Granzyme B is required for the induction of target cell lysis, which occurs as part of cell-mediated immune responses, and can activate apoptosis in target cells by both caspase-dependent and caspase-independent mechanisms. Proteolytic cleavage of substrates by Granzyme B takes place primarily after aspartic acid residues. Recombinant Murine Granzyme B is a glycosylated 227 amino acid protein, comprising the mature active portion of the murine Granzyme B precursor. The apparent molecular weight is 28.9 kDa by mass spectrometry.

Recombinant Human PAI-1 (Legacy Tebubio ref. 167140-04). Plasminogen Activator Inhibitor-1 (PAI-1, Serpin E1) is a member of the serpin family of serine protease inhibitors, and is the primary inhibitor of urokinase and tissue plasminogen activator (tPA). PAI-1 is expressed predominantly in adipose, liver and vascular tissues, but is also produced by certain tumor cells. Elevated levels of PAI-1 are associated with obesity, diabetes and cardiovascular disease, and increased production of PAI-1 is induced by various obesity-related factors, such as TNFalpha, glucose, insulin, and very-low-density lipoprotein. The obesity-related elevation of PAI-1 levels, along with the consequential deficiency in plasminogen activators, can lead directly to increased risk of thrombosis and other coronary diseases. Accordingly, PAI-1 has been implicated as an important molecular link between obesity and coronary disease. PAI-1 can also specifically bind vitronectin (VTN) to form a stable active complex

Recombinant Human PAI-1 (Legacy Tebubio ref. 167140-04). Plasminogen Activator Inhibitor-1 (PAI-1, Serpin E1) is a member of the serpin family of serine protease inhibitors, and is the primary inhibitor of urokinase and tissue plasminogen activator (tPA). PAI-1 is expressed predominantly in adipose, liver and vascular tissues, but is also produced by certain tumor cells. Elevated levels of PAI-1 are associated with obesity, diabetes and cardiovascular disease, and increased production of PAI-1 is induced by various obesity-related factors, such as TNFalpha, glucose, insulin, and very-low-density lipoprotein. The obesity-related elevation of PAI-1 levels, along with the consequential deficiency in plasminogen activators, can lead directly to increased risk of thrombosis and other coronary diseases. Accordingly, PAI-1 has been implicated as an important molecular link between obesity and coronary disease. PAI-1 can also specifically bind vitronectin (VTN) to form a stable active complex

Recombinant Human PAI-2 (Legacy Tebubio ref. 167140-06). PAI-2 is an inhibitory serpin expressed mainly in keratinocytes, activated monocytes, and placental trophoblasts. It exists predominantly as a 47 kDa, nonglycosylated, intracellular protein, which can be induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated forms of PAI-2 are equally effective as inhibitors of urokinase-type plasminogen activator (uPA), the only established physiological target of this serpin. PAI-2 has a unique ability to form dormant polymers spontaneously and reversibly under physiological conditions. The physiological relevance of this property, which is neither a consequence of any mutation in the PAI-2 gene nor associated with any known disorder, is still unclear. However, it appears that the formation of intracellular, dormant polymers may be important for the controlled release of the inhibitor from PAI-2 producing cells. Plasma levels of PAI-2 are usually low or undetectable,

Recombinant Human PAI-2 (Legacy Tebubio ref. 167140-06). PAI-2 is an inhibitory serpin expressed mainly in keratinocytes, activated monocytes, and placental trophoblasts. It exists predominantly as a 47 kDa, nonglycosylated, intracellular protein, which can be induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated forms of PAI-2 are equally effective as inhibitors of urokinase-type plasminogen activator (uPA), the only established physiological target of this serpin. PAI-2 has a unique ability to form dormant polymers spontaneously and reversibly under physiological conditions. The physiological relevance of this property, which is neither a consequence of any mutation in the PAI-2 gene nor associated with any known disorder, is still unclear. However, it appears that the formation of intracellular, dormant polymers may be important for the controlled release of the inhibitor from PAI-2 producing cells. Plasma levels of PAI-2 are usually low or undetectable,

Recombinant Human sDLL-4 (Legacy Tebubio ref. 167140-07). Human sDLL-4 comprises the extracellular signaling domain of DLL, a member of a structurally-related family of single-pass type I transmembrane proteins that serve as ligands for Notch receptors. DLL-4 functions to specifically activate the Notch-1 and Notch-4 receptors. The Notch signaling pathway regulates endothelial cell differentiation, proliferation and apoptosis, and is essential for the development, maintenance and remodeling of the vascular system. Targeted deletion of the DLL-4 gene in mice resulted in severe vascular defects and death before birth. Up-regulation of DLL-4 expression has been implicated in the vascular development of certain tumors. The human DLL-4 gene consists of a 503 amino acid extracellular domain with one DSL domain, eight EGF-like repeats, a 21 amino acid transmembrane domain, and a 135 amino acid cytoplasmic domain. Recombinant Human sDLL-4 is a 54.3 kDa glycoprotein containing 498 amino acid re