10g

Molecular Formula : C10 H14

Molecular Formula : C10 H12 N4 O4

Molecular Formula : C4H9NO

Molecular Formula : C4H7ClO

Molecular Formula : C6 H11 N O3

Carbamazepin

Carbol Fuchsin

Cardiac Troponin I (cTnI) is a subtype of the troponin family that is commonly used as a marker for myocardial damage. Cardiac troponin I is specific for cardiac tissue and is detected in the serum only if myocardial injury has occurred. Because cardiac troponin I is a very sensitive and specific indicator of heart muscle (myocardium) damage, serum levels can be used to help differentiate between unstable angina and myocardial infarction (heart attack) in people with chest pain or acute coronary syndrome.

Carmine

Catalase, Lyophilized

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 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.

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.

The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Rα, IL-2Rβ, and IL-2Rγ. The IL-2Rα is a type I transmembrane protein consisting of a 219 amino acid (a.a.) extracellular domain, a 19 a.a. transmembrane domain and a 13 a.a. intracellular domain, which is not involved in the transduction of IL-2 signal. Activated T cells, regulatory T cells (Tregs) and NK cells express high levels of CD25 and expression of the high-affinity IL-2Rα is mostly limited to these cell populations. Signaling via IL-2Rα mediates multiple biological processes in various cell populations, e.g. proliferation and differentiation of B cells and NK cells. A soluble form of IL-2Rα (IL-2Rα) appears in serum, concomitant with its increased expression on cells. The function of the soluble IL-2Rα is unclear. Increased levels of IL-2Rα in biological fluids reportedly correlate with increased T and B cell activation and immune system activation. Increased serum concentration of IL-2Rα has been observed in patients with a variety of inflammatory conditions and in the course of some leukemias and lymphomas.