Anti-Cystathionase Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, IHC-P, ICC |
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Primary Accession | P32929 |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Clonality | Polyclonal |
Format | Lyophilized |
Description | Rabbit IgG polyclonal antibody for Cystathionine gamma-lyase(CTH) detection. Tested with WB, IHC-P, ICC in Human;Mouse;Rat. |
Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
Gene ID | 1491 |
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Other Names | Cystathionine gamma-lyase, 4.4.1.1, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH |
Calculated MW | 44508 MW KDa |
Application Details | Immunocytochemistry , 0.5-1 µg/ml, Human, - Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, Rat, Mouse, By Heat Western blot, 0.1-0.5 µg/ml, Human, Rat, Mouse |
Subcellular Localization | Cytoplasm. |
Protein Name | Cystathionine gamma-lyase |
Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. |
Immunogen | A synthetic peptide corresponding to a sequence in the middle region of human Cystathionase(112-131aa DVYGGTNRYFRQVASEFGLK), different from the related rat and mouse sequences by two amino acids. |
Purification | Immunogen affinity purified. |
Cross Reactivity | No cross reactivity with other proteins |
Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
Name | CTH |
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Function | Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate (PubMed:10212249, PubMed:18476726, PubMed:19261609, PubMed:19961860). Part of the L- cysteine derived from the trans-sulfuration pathway is utilized for biosynthesis of the ubiquitous antioxidant glutathione (PubMed:18476726). Besides its role in the conversion of L- cystathionine into L-cysteine, it utilizes L-cysteine and L- homocysteine as substrates (at much lower rates than L,L-cystathionine) to produce the endogenous gaseous signaling molecule hydrogen sulfide (H2S) (PubMed:10212249, PubMed:19019829, PubMed:19261609, PubMed:19961860). In vitro, it converts two L-cysteine molecules into lanthionine and H2S, also two L-homocysteine molecules to homolanthionine and H2S, which can be particularly relevant under conditions of severe hyperhomocysteinemia (which is a risk factor for cardiovascular disease, diabetes, and Alzheimer's disease) (PubMed:19261609). Lanthionine and homolanthionine are structural homologs of L,L-cystathionine that differ by the absence or presence of an extra methylene group, respectively (PubMed:19261609). 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 (PubMed:22169477). By generating the gasotransmitter H2S, it participates in a number of physiological processes such as vasodilation, bone protection, and inflammation (Probable) (PubMed:29254196). Plays an essential role in myogenesis by contributing to the biogenesis of H2S in skeletal muscle tissue (By similarity). Can also accept homoserine as substrate (By similarity). Catalyzes the elimination of selenocystathionine (which can be derived from the diet) to yield selenocysteine, ammonia and 2-oxobutanoate (By similarity). |
Cellular Location | Cytoplasm. |
Tissue Location | Highly expressed in liver (PubMed:10727430, PubMed:20305127). Also in muscle and lower expression in most tissues except heart, pituitary gland, spleen, thymus, and vascular tissue, where it is hardly detected (PubMed:20305127) |

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Provided below are standard protocols that you may find useful for product applications.
Background
CTH(CYSTATHIONINE GAMMA-LYASE),also called CYSTATHIONASE, is an enzyme which breaks down cystathionine into cysteine and alpha-ketobutyrate.And the CTH gene is mapped on 1p31.1. In some bacteria and mammals, including humans, this enzyme takes part in generating hydrogen sulfide and that genetic deletion of this enzyme in mice markedly reduced H2S levels in the serum, heart, aorta, and other tissues. Mutant mice lacking CTH displayed pronounced hypertension and diminished endothelium-dependent vasorelaxation. Cystathionine was physiologically activated by calcium and calmodulin, which is a mechanism for H2S formation in response to vascular activation.

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