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Mouse Anti-DDAH1 Recombinant Antibody (CBYCD-195) (CBMAB-D0442-YC)

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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYCD-195
Antibody Isotype
IgG
Application
WB, ICC, IHC-P, IHC-Fr, ELISA

Basic Information

Immunogen
Dimethylarginine Dimethylaminohydrolase 1
Specificity
Human
Antibody Isotype
IgG
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!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Dimethylarginine Dimethylaminohydrolase 1
Introduction
DDAH1 belongs to the dimethylarginine dimethylaminohydrolase (DDAH) gene family. The encoded enzyme plays a role in nitric oxide generation by regulating cellular concentrations of methylarginines, which in turn inhibit nitric oxide synthase activity.
Entrez Gene ID
UniProt ID
Alternative Names
Dimethylarginine Dimethylaminohydrolase 1; Dimethylargininase-1; EC 3.5.3.18; DDAH-1; DDAHI; DDAH;
Function
Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
Biological Process
Arginine catabolic process Source: BHF-UCL
Arginine metabolic process Source: GO_Central
Citrulline metabolic process Source: UniProtKB
Negative regulation of cell population proliferation Source: BHF-UCL
Negative regulation of cellular response to hypoxia Source: BHF-UCL
Negative regulation of vascular permeability Source: BHF-UCL
Nitric oxide mediated signal transduction Source: ProtInc
Positive regulation of angiogenesis Source: Ensembl
Positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
Regulation of nitric-oxide synthase activity Source: Reactome
Regulation of systemic arterial blood pressure Source: BHF-UCL
Cellular Location
Cytosol; Extracellular exosome
More Infomation

Xie, Z., Hou, L., Shen, S., Wu, Y., Wang, J., Jie, Z., ... & Fan, S. (2022). Mechanical force promotes dimethylarginine dimethylaminohydrolase 1-mediated hydrolysis of the metabolite asymmetric dimethylarginine to enhance bone formation. Nature communications, 13(1), 1-15.

Kopaliani, I., Jarzebska, N., Billoff, S., Kolouschek, A., Martens-Lobenhoffer, J., Bornstein, S. R., ... & Rodionov, R. N. (2021). Overexpression of dimethylarginine dimethylaminohydrolase 1 protects from angiotensin II-induced cardiac hypertrophy and vascular remodeling. American Journal of Physiology-Heart and Circulatory Physiology, 321(5), H825-H838.

Wang, D., Li, H., Weir, E. K., Xu, Y., Xu, D., & Chen, Y. (2019). Dimethylarginine dimethylaminohydrolase 1 deficiency aggravates monocrotaline-induced pulmonary oxidative stress, pulmonary arterial hypertension and right heart failure in rats. International Journal of Cardiology, 295, 14-20.

Wang, Y., Wang, E., Zhang, Y., Madamsetty, V. S., Ji, B., Radisky, D. C., ... & Mukhopadhyay, D. (2019). Neuropilin‐1 maintains dimethylarginine dimethylaminohydrolase 1 expression in endothelial cells, and contributes to protection from angiotensin II–induced hypertension. The FASEB Journal, 33(1), 494-500.

Reddy, K. R. K., Dasari, C., Duscharla, D., Supriya, B., Ram, N. S., Surekha, M. V., ... & Ummanni, R. (2018). Dimethylarginine dimethylaminohydrolase-1 (DDAH1) is frequently upregulated in prostate cancer, and its overexpression conveys tumor growth and angiogenesis by metabolizing asymmetric dimethylarginine (ADMA). Angiogenesis, 21(1), 79-94.

Buijs, N., Oosterink, J. E., Jessup, M., Schierbeek, H., Stolz, D. B., Houdijk, A. P., ... & van Leeuwen, P. A. (2017). A new key player in VEGF-dependent angiogenesis in human hepatocellular carcinoma: dimethylarginine dimethylaminohydrolase 1. Angiogenesis, 20(4), 557-565.

Xu, X., Zhang, P., Kwak, D., Fassett, J., Yue, W., Atzler, D., ... & Chen, Y. (2017). Cardiomyocyte dimethylarginine dimethylaminohydrolase-1 (DDAH1) plays an important role in attenuating ventricular hypertrophy and dysfunction. Basic research in cardiology, 112(5), 1-11.

Hulin, J. A., Tommasi, S., Elliot, D., Hu, D. G., Lewis, B. C., & Mangoni, A. A. (2017). MiR-193b regulates breast cancer cell migration and vasculogenic mimicry by targeting dimethylarginine dimethylaminohydrolase 1. Scientific reports, 7(1), 1-15.

Li, T., Feng, R., Zhao, C., Wang, Y., Wang, J., Liu, S., ... & Lu, Z. (2017). Dimethylarginine dimethylaminohydrolase 1 protects against high-fat diet-induced hepatic steatosis and insulin resistance in mice. Antioxidants & Redox Signaling, 26(11), 598-609.

Shi, L., Zhao, C., Wang, H., Lei, T., Liu, S., Cao, J., & Lu, Z. (2017). Dimethylarginine dimethylaminohydrolase 1 deficiency induces the epithelial to mesenchymal transition in renal proximal tubular epithelial cells and exacerbates kidney damage in aged and diabetic mice. Antioxidants & Redox Signaling, 27(16), 1347-1360.

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

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