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Mouse Anti-CTH Recombinant Antibody (4E1-1B7) (V2LY-0125-LY256)


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Published Data
V2LY-0125-LY256-1
Mouse Anti-CTH Recombinant Antibody (4E1-1B7) (V2LY-0125-LY256) in WB
Hepatic expression of Mpst, Cth, Tst, Cbs, and Gpx1 in mice lacking Mpst, Cth, or both. Expression of Mpst (A), Cth (B), Tst (C), Cbs (D), and Gpx1 (E) in the livers of wild-type WT, Mpst (1st)-KO, Cth-KO, and Mpst (1st)/Cth-DKO mice was compared using Gapdh (A) as a loading control with that in WT liver as 1. ...View More
Akahoshi, N., Minakawa, T., Miyashita, M., Sugiyama, U., Saito, C., Takemoto, R., ... & Ishii, I. (2020). Increased urinary 3-mercaptolactate excretion and enhanced passive systemic anaphylaxis in mice lacking mercaptopyruvate sulfurtransferase, a model of mercaptolactate-cysteine disulfiduria. International Journal of Molecular Sciences, 21(3), 818. Distributed under Open Access license CC BY 4.0, without modification.
V2LY-0125-LY256-2
Mouse Anti-CTH Recombinant Antibody (4E1-1B7) (V2LY-0125-LY256) in Immunoblotting
(A-D) Hcy down-regulated CSE mRNA and protein expressions in raw264.7 macrophages in dose- and time-dependent manners (E,F). Effect of l-homocystine and l-cysteine on CSE protein expression. CSE protein expression was evaluated by immunoblotting analysis while CSE mRNA level determined by quantitative PCR. GAPDH protein and 18S mRNA served as loading controls. Mean ± SEM, n = 3-8. ...View More
Li, J. J., Li, Q., Du, H. P., Wang, Y. L., You, S. J., Wang, F., ... & Hu, L. F. (2015). Homocysteine triggers inflammatory responses in macrophages through inhibiting CSE-H2S signaling via DNA hypermethylation of CSE promoter. International journal of molecular sciences, 16(6), 12560-12577. Distributed under Open Access license CC BY 4.0, without modification.
V2LY-0125-LY256-3
Mouse Anti-CTH Recombinant Antibody (4E1-1B7) (V2LY-0125-LY256) in IF
Immunofluorescent photograph of CSE in the cochlea (bar = 200 µm). CSE protein was positively expressed in the stria vascularis (yellow arrow) and the wall of the spiral modiolar artery (red arrow). ...View More
Li, X., Mao, X. B., Hei, R. Y., Zhang, Z. B., Wen, L. T., Zhang, P. Z., ... & Qiao, L. (2011). Protective role of hydrogen sulfide against noise-induced cochlear damage: a chronic intracochlear infusion model. PloS one, 6(10), e26728. Distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Summary

Host Animal
Mouse
Specificity
Guinea pig, Human
Clone
4E1-1B7
Antibody Isotype
IgG1, κ
Application
ELISA, WB

Basic Information

Immunogen
Full length recombinant CTH.
Host Species
Mouse
Specificity
Guinea pig, Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody

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

Format
Liquid
Buffer
PBS
Preservative
None
Concentration
Batch dependent
Purity
>95% as determined by analysis 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
Entrez Gene ID
1491
UniProt ID
P32929
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.
More Infomation

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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