Anti-Cystathionase/CTH Antibody Picoband® Fluoro488 Conjugated

Cystathionine gamma-lyase (or cystathionase) is an enzyme which breaks down cystathionine into cysteine and α-ketobutyrate. The International Radiation Hybrid Mapping Consortium mapped the CTH gene to chromosome 1. The CTH gene had earlier been assigned to chromosome 16 by study of somatic cell hybrids. It is demonstrated that hydrogen sulfide (H2S) is physiologically generated by CTH.

E.coli-derived human Cystathionase recombinant protein (Position: D181-H398) . Human Cystathionase shares 85.8% amino acid (aa) sequence identity with both mouse and rat Cystathionase.

Cancer, Cardiovascular, Collagen, Cytoskeleton/ECM, ECM Proteins, Extracellular Matrix, Growth Factors/Hormones, Invasion/Microenvironment, Signal Transduction, Tumor Biomarkers, Tumor Immunology, Tumor-Associated Antigens, Vasculature

Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function. .

1. Donald, L. J., Wang, H. S., Hamerton, J. L. Assignment of the gene for cystathionase (CYS) to human chromosome 16. (Abstract) Cytogenet. Cell Genet. 32: 268 only, 1982. 2. Yang, G., Wu, L., Jiang, B., Yang, W., Qi, J., Cao, K., Meng, Q., Mustafa, A. K., Mu, W., Zhang, S., Snyder, S. H., Wang, R. H2S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase. Science 322: 587-590, 2008.