IHUMSIL17DRAFLY5UG

Human, Mouse IL-17D Recombinant Protein (Animal Free) Lyophilized

Human, Mouse IL-17D Recombinant Protein (Animal Free) Lyophilized

696.39 €

MBS8432857-INQUIRE

Human, Mouse IL-17D Recombinant Protein (Animal Free) Lyophilized

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40-724

Vitronectin Recombinant Protein (Animal Free)

Vitronectin is a secreted glycoprotein that is synthesized in the liver. It circulates primarily in monomeric form, but can undergo conformational change to a structure that forms disulfide-linked multimers. The multimeric vitronectin can efficiently bind to, and incorporate into, the extracellular matrix. Within the matrix, vitronectin can support cell adhesion through binding to various integrins and other proteoglycans. Additionally, recombinant vitronectin can function as a chemically-defined matrix component in human embryonic stem cell renewal media. Recombinant Human Vitronectin is a 459 amino acid, single-chain, monomeric protein, which migrates at an apparent molecular weight of 75 kDa by SDS-PAGE under reducing conditions. The calculated molecular weight of Recombinant Human Vitronectin is 52.2 kDa.

621.71 €

100-385S-AF

Human Vitronectin (Animal Free) Recombinant Protein

Vitronectin is a secreted glycoprotein that is synthesized in the liver. It circulates primarily in monomeric form, but can undergo conformational change to a structure that forms disulfide-linked multimers. The multimeric vitronectin can efficiently bind to, and incorporate into, the extracellular matrix. Within the matrix, vitronectin can support cell adhesion through binding to various integrins and other proteoglycans. Additionally, recombinant vitronectin can function as a chemically-defined matrix component in human embryonic stem cell renewal media. Recombinant Human Vitronectin is a 459 amino acid, single-chain, monomeric protein, which migrates at an apparent molecular weight of 75 kDa by SDS-PAGE under reducing conditions. The calculated molecular weight of Recombinant Human Vitronectin is 52.2 kDa.

454.12 €

100-409-AF

human Enterokinase (Animal Free) Recombinant Protein

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Enterokinase sequentially cleaves carboxyl side of D-D-D-D-K. Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light chain consists of 235 amino acid residues. The calculated molecular weight of Recombinant Human Enterokinase is 108.7 kDa.

499.87 €

100-409S-AF

human Enterokinase (Animal Free) Recombinant Protein

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Enterokinase sequentially cleaves carboxyl side of D-D-D-D-K. Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light chain consists of 235 amino acid residues. The calculated molecular weight of Recombinant Human Enterokinase is 108.7 kDa.

355.12 €