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Mouse Anti-CTH Recombinant Antibody (2D6) (CBMAB-C4913-LY)

This product is antibody recognizes CTH. The antibody 2D6 immunoassay techniques such as: WB, IHC-P.
See all CTH antibodies

Summary

Host Animal
Mouse
Specificity
Human, Monkey, Dog
Clone
2D6
Antibody Isotype
IgG1
Application
WB, IHC-P

Basic Information

Immunogen
Full length human recombinant protein of human CTH produced in HEK293T cell
Specificity
Human, Monkey, Dog
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
1% BSA, 50% glycerol
Preservative
0.02% sodium azide
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Cystathionine Gamma-Lyase
Introduction
CTH (Cystathionine Gamma-Lyase) is a Protein Coding gene. Diseases associated with CTH include Cystathioninuria and Methionine Adenosyltransferase I/Iii Deficiency. Among its related pathways are One carbon pool by folate and Viral mRNA Translation. Gene Ontology (GO) annotations related to this gene include calmodulin binding and carbon-sulfur lyase activity.
Entrez Gene ID
Human1491
Monkey696664
Dog479991
UniProt ID
HumanP32929
MonkeyA0A1D5QLN0
DogE2RDY8
Alternative Names
Cystathionine Gamma-Lyase; Cystathionase (Cystathionine Gamma-Lyase); Cysteine-Protein Sulfhydrase; Gamma-Cystathionase; EC 4.4.1.1; Cysteine Desulfhydrase; Homoserine Dehydratase; Homoserine Deaminase; EC 4.4.1;
Function
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.
Biological Process
Cellular response to leukemia inhibitory factor Source: Ensembl
Cysteine biosynthetic process Source: UniProtKB
Cysteine biosynthetic process via cystathionine Source: BHF-UCL
Cysteine metabolic process Source: ProtInc
Endoplasmic reticulum unfolded protein response Source: UniProtKB
Hydrogen sulfide biosynthetic process Source: UniProtKB
Negative regulation of apoptotic signaling pathway Source: Ensembl
Positive regulation of aortic smooth muscle cell differentiation Source: BHF-UCL
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
Positive regulation of NF-kappaB transcription factor activity Source: Ensembl
Protein homotetramerization Source: UniProtKB
Protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine Source: UniProtKB
Protein sulfhydration Source: UniProtKB
Sulfur amino acid catabolic process Source: Reactome
Transsulfuration Source: BHF-UCL
Cellular Location
Cytoplasm
Involvement in disease
Cystathioninuria (CSTNU):
Autosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine, leading to increased urinary excretion.

Lancien, M., Gueno, L., Salle, S., Merieau, E., Beriou, G., Nguyen, T. H., ... & Louvet, C. (2021). Cystathionine‐gamma‐lyase overexpression in T cells enhances antitumor effect independently of cysteine autonomy. Cancer Science, 112(5), 1723.

Xu, S., Pan, J., Cheng, X., Zheng, J., Wang, X., Guan, H., ... & Zhang, L. (2020). Diallyl trisulfide, a H2S donor, inhibits cell growth of human papillary thyroid carcinoma KTC‐1 cells through a positive feedback loop between H2S and cystathionine‐gamma‐lyase. Phytotherapy Research, 34(5), 1154-1165.

Chen, L., Lu, C., & Hua, Y. (2020). Cystathionine gamma‐lyase aggravates periodontal damage in traumatic occlusion mouse models. Journal of periodontal research, 55(5), 667-675.

Akahoshi, N., Handa, H., Takemoto, R., Kamata, S., Yoshida, M., Onaka, T., & Ishii, I. (2019). Preeclampsia-like features and partial lactation failure in mice lacking cystathionine γ-lyase—an animal model of cystathioninuria. International Journal of Molecular Sciences, 20(14), 3507.

Wang, Y. H., Huang, J. T., Chen, W. L., Wang, R. H., Kao, M. C., Pan, Y. R., ... & Wang, L. H. (2019). Dysregulation of cystathionine γ‐lyase promotes prostate cancer progression and metastasis. EMBO reports, 20(10), e45986.

Lechuga, T. J., Qi, Q. R., Kim, T., Magness, R. R., & Chen, D. B. (2019). E2β stimulates ovine uterine artery endothelial cell H2S production in vitro by estrogen receptor-dependent upregulation of cystathionine β-synthase and cystathionine γ-lyase expression. Biology of reproduction, 100(2), 514-522.

Szijártó, I. A., Markó, L., Filipovic, M. R., Miljkovic, J. L., Tabeling, C., Tsvetkov, D., ... & Gollasch, M. (2018). Cystathionine γ-Lyase–Produced hydrogen sulfide controls endothelial no bioavailability and blood pressure. Hypertension, 71(6), 1210-1217.

Gupta, V., Kapopara, P. R., Khan, A. A., Arige, V., Subramanian, L., Sonawane, P. J., ... & Mahapatra, N. R. (2017). Functional promoter polymorphisms direct the expression of cystathionine gamma-lyase gene in mouse models of essential hypertension. Journal of Molecular and Cellular Cardiology, 102, 61-73.

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For research use only. Not intended for any clinical use.

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