Ambient

Castor Oil, USP

Catalase, Lyophilized

Catalase, Lyophilized

Catalase, Lyophilized

Catechol

Catechol

Catechol

Catechol

Cathepsin B is an enzymatic protein that is a member of the peptidase (or protease) family. Elevated lev- els of cathepsin B occur in a wide variety of disease,causing numerous pathologies including cell death, inflammation, and the production of toxic peptides. For example, neuroscience research suggests that cathepsin B plays a role in inducing epilepsy resulting in a significant amount of cell death. Seizure-induced rats treated with a cathepsin B inhibitor exhibited improved neurological scores and learning ability with reduced neuronal cell death.

Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene. Cystatin-B / CSTB is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. Cystatin-B / CSTB is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. Cystatin-B / CSTB is also thought to play a role in protecting against the proteases leaking from lysosomes.

Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene. Cystatin-B / CSTB is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. Cystatin-B / CSTB is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. Cystatin-B / CSTB is also thought to play a role in protecting against the proteases leaking from lysosomes.

Cathepsin L is an enzyme. Cathepsin L, a lysosomal endopeptidase expressed in most eukaryotic cells, is a member of the papain-like family of cysteine proteinases. Cathepsin L plays a major role in antigen processing, tumor invasion and metastasis, bone resorption, and turnover of intracellular and secreted proteins involved in growth regulation. Unlike the precursor forms of other papain family members, the 43 kDa pro-cathepsin L itself is secreted from various cells. Pro-cathepsin L is the major excreted protein of malignantly transformed mouse fibroblasts and is also one of the major acidic cysteine proteases in mammalian cells.

Cathepsin L is an enzyme. Cathepsin L, a lysosomal endopeptidase expressed in most eukaryotic cells, is a member of the papain-like family of cysteine proteinases. Cathepsin L plays a major role in antigen processing, tumor invasion and metastasis, bone resorption, and turnover of intracellular and secreted proteins involved in growth regulation. Unlike the precursor forms of other papain family members, the 43 kDa pro-cathepsin L itself is secreted from various cells. Pro-cathepsin L is the major excreted protein of malignantly transformed mouse fibroblasts and is also one of the major acidic cysteine proteases in mammalian cells.

Cathepsin L is an enzyme. Cathepsin L, a lysosomal endopeptidase expressed in most eukaryotic cells, is a member of the papain-like family of cysteine proteinases. Cathepsin L plays a major role in antigen processing, tumor invasion and metastasis, bone resorption, and turnover of intracellular and secreted proteins involved in growth regulation. Unlike the precursor forms of other papain family members, the 43 kDa pro-cathepsin L itself is secreted from various cells. Pro-cathepsin L is the major excreted protein of malignantly transformed mouse fibroblasts and is also one of the major acidic cysteine proteases in mammalian cells.

Cation Calibration Standard 2 in HNO3

Cation Calibration Standard 2 in HNO3

Cationic Starch, Nitrogen 0.3 Percent

Cationic Starch, Nitrogen 0.3 Percent

Cationic Starch, Nitrogen 0.3 Percent

Cationic Starch, Nitrogen 0.4 Percent

Cationic Starch, Nitrogen 0.4 Percent

Cationic Starch, Nitrogen 0.4 Percent

GenScript CBP Tag Antibody, mAb, Mouse recognizes CBP-tagged proteins.

GenScript CBP-tag Antibody recognizes CBP tagged fusion proteins.

CCL25 is a new member of the CC family chemokine. It is also called Thymus-expressed chemokine (TECK) because it is restricted produced by thymus and intestine. Especially, the dendritic cells derived from thymus but not bone marrow had been identified to be the source of CCL25. By binding with CCR9, it elicits its effects of chemotactic for thymocytes, macrophages, and dendritic cells. Additionally, CCL25 takes part in regulating the development of T-cells.

CCL25 is a new member of the CC family chemokine. It is also called Thymus-expressed chemokine (TECK) because it is restricted produced by thymus and intestine. Especially, the dendritic cells derived from thymus but not bone marrow had been identified to be the source of CCL25. By binding with CCR9, it elicits its effects of chemotactic for thymocytes, macrophages, and dendritic cells. Additionally, CCL25 takes part in regulating the development of T-cells.

CD160 is a glycosylphosphatidylinositol-anchored Ig domain protein that is expressed on almost all intestinal intraepithelial lymphocytes (IELs), γδ T (gamma delta T) cells, NK (natural killer) cells, and a minor subset of CD4+ and CD8+ T cells. In terms of function, work has centered on the role of CD160 in enhancing NK or CD8 T cell activation. Such effects have been attributed to the ability of CD160 to bind classical and nonclassical MHC class I molecules, although with apparent low affinity, requiring clustering of MHC class I molecules or overexpression of CD160 or MHC class I for detection of the interaction.

CD160 is a glycosylphosphatidylinositol-anchored Ig domain protein that is expressed on almost all intestinal intraepithelial lymphocytes (IELs), γδ T (gamma delta T) cells, NK (natural killer) cells, and a minor subset of CD4+ and CD8+ T cells. In terms of function, work has centered on the role of CD160 in enhancing NK or CD8 T cell activation. Such effects have been attributed to the ability of CD160 to bind classical and nonclassical MHC class I molecules, although with apparent low affinity, requiring clustering of MHC class I molecules or overexpression of CD160 or MHC class I for detection of the interaction.

CD160 is a glycosylphosphatidylinositol-anchored Ig domain protein that is expressed on almost all intestinal intraepithelial lymphocytes (IELs), γδ T (gamma delta T) cells, NK (natural killer) cells, and a minor subset of CD4+ and CD8+ T cells. In terms of function, work has centered on the role of CD160 in enhancing NK or CD8 T cell activation. Such effects have been attributed to the ability of CD160 to bind classical and nonclassical MHC class I molecules, although with apparent low affinity, requiring clustering of MHC class I molecules or overexpression of CD160 or MHC class I for detection of the interaction.