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Endostatin is a cleaved product of the carboxyl-terminal domain of collagen XVIII. It functions as an anti-angiogenic cytokine that is expressed in various organs especially with high levels in liver, lung, and kidney. Endostatin inhibits angiogenesis by blocking the pro-angiogenic activities of VEGF and FGF-basic. In-vitro studies have shown endostatin blocks the proliferation and organization of endothelial cells into new blood vessels. In animal studies endostatin inhibited angiogenesis and growth of both primary tumors and secondary metastasis.

ENDOTHALL DIMETHYL ESTER, 1000 ug/mL

Enrofloxacin

Enrofloxacin

Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys(DDDDK↑). Enterokinase will not work if the recognition site is followed by a proline. rbEKhas the highest activity than EK of other species and is used wildly in biochemical applications. rbEK with 6 × His-tag binds with Ni2+ affinity chromatography and was designed for removing from digestion system.

Recombinant Bovine Enterokinase (His-tagged) (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids, 6 × His at C-terminus. A fully biologically active molecule, rbEK has a molecular mass of 40 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys(DDDDK↑). Enterokinase will not work if the recognition site is followed by a proline. rbEKhas the highest activity than EK of other species and is used wildly in biochemical applications. rbEK with 6 × His-tag binds with Ni2+ affinity chromatography and was designed for removing from digestion system.

Recombinant Bovine Enterokinase (His-tagged) (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids, 6 × His at C-terminus. A fully biologically active molecule, rbEK has a molecular mass of 40 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys(DDDDK↑). Enterokinase will not work if the recognition site is followed by a proline. rbEKhas the highest activity than EK of other species and is used wildly in biochemical applications. rbEK with 6 × His-tag binds with Ni2+ affinity chromatography and was designed for removing from digestion system.

Recombinant Bovine Enterokinase (His-tagged) (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids, 6 × His at C-terminus. A fully biologically active molecule, rbEK has a molecular mass of 40 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Recombinant Enterokinase protein

Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. 
Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys. 
Enterokinase will not work if the recognition site is followed by a proline. rbEK with 6 × His-tag binds with Ni²⁺ affinity chromatography and was designed for removing from digestion system.

Recombinant Bovine Enterokinase (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids. A fully biologically active molecule, rbEK has a molecular mass of 22.7 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. 
Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys. 
Enterokinase will not work if the recognition site is followed by a proline. rbEK with 6 × His-tag binds with Ni²⁺ affinity chromatography and was designed for removing from digestion system.

Recombinant Bovine Enterokinase (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids. A fully biologically active molecule, rbEK has a molecular mass of 22.7 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. 
Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys. 
Enterokinase will not work if the recognition site is followed by a proline. rbEK with 6 × His-tag binds with Ni²⁺ affinity chromatography and was designed for removing from digestion system.

Recombinant Bovine Enterokinase (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids. A fully biologically active molecule, rbEK has a molecular mass of 22.7 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Environmental Calibration Standard

Eosin Y Disodium Salt

Eosin Y Disodium Salt

Eosin Y Disodium Salt

Eosin Y Disodium Salt

Eosin Y Disodium Salt

Eosin Y TS, (U.S.P. Test Solution)

Eosin Y TS, (U.S.P. Test Solution)

Eosin Y, Free Acid

Eosin Y, Reagent, ACS

Eosin Y, Reagent, ACS

Eosin Y, Reagent, ACS

Eosin Y, Reagent, ACS

CCL11 is a potent eosinophil chemoattractant that was originally purified from bronchoalveolar lavage fluid of guinea pigs sensitized by aerosol challenge with ovalbumin. Human CCL11 cDNA encodes a 97 amino acid residue precursor protein from which the aminoterminal 23 amino acid residues are cleaved to generate the 74 amino acid residue mature human CCL11. At the protein sequence level, mature human CCL11 is approximately 60% identical to mature mouse and guinea pig CCL11. Human CCL11 is chemotactic for eosinophils, but not mononuclear cells or neutrophils. The CC chemokine receptor 3 (CCR3) has now been identified to be a specific human CCL11 receptor. CCR3 has also been shown to serve as a cofactor for a restricted subset of primary HIV viruses and binding of CCL11 to CCR3 inhibited infection by the HIV isolates.

CCL11 is a potent eosinophil chemoattractant that was originally purified from bronchoalveolar lavage fluid of guinea pigs sensitized by aerosol challenge with ovalbumin. Human CCL11 cDNA encodes a 97 amino acid residue precursor protein from which the aminoterminal 23 amino acid residues are cleaved to generate the 74 amino acid residue mature human CCL11. At the protein sequence level, mature human CCL11 is approximately 60% identical to mature mouse and guinea pig CCL11. Human CCL11 is chemotactic for eosinophils, but not mononuclear cells or neutrophils. The CC chemokine receptor 3 (CCR3) has now been identified to be a specific human CCL11 receptor. CCR3 has also been shown to serve as a cofactor for a restricted subset of primary HIV viruses and binding of CCL11 to CCR3 inhibited infection by the HIV isolates.

CCL11 is a potent eosinophil chemoattractant that was originally purified from bronchoalveolar lavage fluid of guinea pigs sensitized by aerosol challenge with ovalbumin. Human CCL11 cDNA encodes a 97 amino acid residue precursor protein from which the aminoterminal 23 amino acid residues are cleaved to generate the 74 amino acid residue mature human CCL11. At the protein sequence level, mature human CCL11 is approximately 60% identical to mature mouse and guinea pig CCL11. Human CCL11 is chemotactic for eosinophils, but not mononuclear cells or neutrophils. The CC chemokine receptor 3 (CCR3) has now been identified to be a specific human CCL11 receptor. CCR3 has also been shown to serve as a cofactor for a restricted subset of primary HIV viruses and binding of CCL11 to CCR3 inhibited infection by the HIV isolates.

CCL11 is a potent eosinophil chemoattractant that was originally purified from bronchoalveolar lavage fluid of guinea pigs sensitized by aerosol challenge with ovalbumin. Human CCL11 cDNA encodes a 97 amino acid residue precursor protein from which the aminoterminal 23 amino acid residues are cleaved to generate the 74 amino acid residue mature human CCL11. At the protein sequence level, mature human CCL11 is approximately 60% identical to mature mouse and guinea pig CCL11. Human CCL11 is chemotactic for eosinophils, but not mononuclear cells or neutrophils. The CC chemokine receptor 3 (CCR3) has now been identified to be a specific human CCL11 receptor. CCR3 has also been shown to serve as a cofactor for a restricted subset of primary HIV viruses and binding of CCL11 to CCR3 inhibited infection by the HIV isolates.

EPA 200.7 Cal Std 6 in 2 Percent HNO3 + Tr HF