Other Proteins

Recombinant Human Neuroserpin (Legacy Tebubio ref. 167130-14). Neuroserpin is an inhibitory serpin that is expressed predominantly in the central nervous system. Although the physiological target of neuroserpin is still unclear, cumulative evidence suggests that it plays an important role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis, and the subsequent development of neuronal plasticity. In the adult brain, neuroserpin is secreted from the growth cones of neurons in areas where synaptic changes are associated with learning and memory (i.e. cerebral cortex, hippocampus, and amygdala.) The neuroprotective role of neuroserpin has been demonstrated in transgenic mice lacking neuroserpin expression. The deficiency of neuroserpin in these mice was associated with motor neuron disease characterized by axonal degradation. In humans, defects in neuroserpin, caused by point mutations in the neuroserpin gene, underlie a hereditary disorder called the

Recombinant Human Neuroserpin (Legacy Tebubio ref. 167130-14). Neuroserpin is an inhibitory serpin that is expressed predominantly in the central nervous system. Although the physiological target of neuroserpin is still unclear, cumulative evidence suggests that it plays an important role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis, and the subsequent development of neuronal plasticity. In the adult brain, neuroserpin is secreted from the growth cones of neurons in areas where synaptic changes are associated with learning and memory (i.e. cerebral cortex, hippocampus, and amygdala.) The neuroprotective role of neuroserpin has been demonstrated in transgenic mice lacking neuroserpin expression. The deficiency of neuroserpin in these mice was associated with motor neuron disease characterized by axonal degradation. In humans, defects in neuroserpin, caused by point mutations in the neuroserpin gene, underlie a hereditary disorder called the

Recombinant Human Relaxin-2 (Legacy Tebubio ref. 167130-15). Relaxin-2 is a peptide hormone structurally related to insulin, which is expressed in the placenta, decidua, prostate, and ovaries during pregnancy. Of the three known relaxin genes, relaxin-2 is the only relaxin known to circulate in the blood. Relaxin-2 binds specifically to the LGR7 and LGR8 receptors, previously identified as "orphan" G protein-coupled receptors. Signaling by relaxin-2 through its target receptors enhances the growth of pubic ligaments, and the ripening of the cervix during birth. Recombinant Human Relaxin-2 is a non-glycosylated, 6.0 kDa, disulfide-linked, heterodimeric protein consisting of a 24 amino acid A-chain, and a 29 amino acid B-chain.

Recombinant Human Relaxin-2 (Legacy Tebubio ref. 167130-15). Relaxin-2 is a peptide hormone structurally related to insulin, which is expressed in the placenta, decidua, prostate, and ovaries during pregnancy. Of the three known relaxin genes, relaxin-2 is the only relaxin known to circulate in the blood. Relaxin-2 binds specifically to the LGR7 and LGR8 receptors, previously identified as "orphan" G protein-coupled receptors. Signaling by relaxin-2 through its target receptors enhances the growth of pubic ligaments, and the ripening of the cervix during birth. Recombinant Human Relaxin-2 is a non-glycosylated, 6.0 kDa, disulfide-linked, heterodimeric protein consisting of a 24 amino acid A-chain, and a 29 amino acid B-chain.

Recombinant Human ANGPTL-3 (Legacy Tebubio ref. 167130-18). ANGPTL-3 (Angiopoietin like protein 3) 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. It is primarily expressed in the liver and can exert activities related to both angiogenesis and lipid metabolism. ANGPTL-3 inhibits lipoprotein lipase (LPL) and endothelial lipase (EL), which has the effect of increasing plasma levels of triglycerides and HDL associated cholesterol. The fibrinogen like portion of the ANGPTL-3 protein can bind alpha-5/beta-3 integrins leading to endothelial cell adhesion and migration. Recombinant human ANGPTL-3 is a glycoprotein that migrates by SDS-PAGE analysis at an apparent molecular weight of 62 kDa, and contains 452 amino acid residues including a C-terminal His tag.

Recombinant Human ANGPTL-3 (Legacy Tebubio ref. 167130-18). ANGPTL-3 (Angiopoietin like protein 3) 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. It is primarily expressed in the liver and can exert activities related to both angiogenesis and lipid metabolism. ANGPTL-3 inhibits lipoprotein lipase (LPL) and endothelial lipase (EL), which has the effect of increasing plasma levels of triglycerides and HDL associated cholesterol. The fibrinogen like portion of the ANGPTL-3 protein can bind alpha-5/beta-3 integrins leading to endothelial cell adhesion and migration. Recombinant human ANGPTL-3 is a glycoprotein that migrates by SDS-PAGE analysis at an apparent molecular weight of 62 kDa, and contains 452 amino acid residues including a C-terminal His tag.

Recombinant Human C1 Inhibitor (Legacy Tebubio ref. 167130-20). C1 inhibitor is a member of the serpin family of structurally related proteins, and is the primary regulator of the immune complement system. C1 inhibitor is a protease inhibitor that functions to inhibit the complement system in order to prevent over-activation or spontaneous activation. Inhibition is achieved by binding to and irreversibly inhibiting the C1r and C1s proteases of the C1 complex, which has the effect of shutting down all subsequent downstream events in the complement activation cascade. C1 inhibitor can also inhibit various other proteases, including Kallikrein, Factor XIa, and Factor XIIa. Deficiencies in C1 inhibitor are the primary cause of hereditary angioedema (HAE, hereditary angioneurotic edema), a disease characterized by edema in the respiratory and gastrointestinal tracts. In certain clinical situations, the direct administration of C1 inhibitor can be used to treat HAE and certain other conditi

Recombinant Human C1 Inhibitor (Legacy Tebubio ref. 167130-20). C1 inhibitor is a member of the serpin family of structurally related proteins, and is the primary regulator of the immune complement system. C1 inhibitor is a protease inhibitor that functions to inhibit the complement system in order to prevent over-activation or spontaneous activation. Inhibition is achieved by binding to and irreversibly inhibiting the C1r and C1s proteases of the C1 complex, which has the effect of shutting down all subsequent downstream events in the complement activation cascade. C1 inhibitor can also inhibit various other proteases, including Kallikrein, Factor XIa, and Factor XIIa. Deficiencies in C1 inhibitor are the primary cause of hereditary angioedema (HAE, hereditary angioneurotic edema), a disease characterized by edema in the respiratory and gastrointestinal tracts. In certain clinical situations, the direct administration of C1 inhibitor can be used to treat HAE and certain other conditi

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