Code | CSB-YP001268HU |
MSDS | |
Size | Pls inquire |
Source | Yeast |
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Code | CSB-EP001268HU |
MSDS | |
Size | Pls inquire |
Source | E.coli |
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Code | CSB-EP001268HU-B |
MSDS | |
Size | Pls inquire |
Source | E.coli |
Conjugate | Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag. |
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Code | CSB-BP001268HU |
MSDS | |
Size | Pls inquire |
Source | Baculovirus |
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Code | CSB-MP001268HU |
MSDS | |
Size | Pls inquire |
Source | Mammalian cell |
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This ADA protein is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
Adenosine deaminase (ADA) is a crucial enzyme involved in purine metabolism. It catalyzes the deamination of adenosine and 2′‐deoxyadenosine to inosine and 2′‐deoxyinosine, respectively, along with ammonia [1]. ADA is implicated in various physiological processes and diseases. For instance, studies have shown a relationship between serum ADA levels and conditions like diabetes mellitus [2][3], autoimmune hepatitis [4], epilepsy [5], rheumatoid arthritis [6], and even neuroprotection in the brain [7].
Research has also highlighted the significance of ADA in different tissues. It is widely distributed in the brain and is associated with neuroprotective effects in the striatum [7]. ADA has the highest activity in lymphoid tissues, particularly in T lymphocytes, and is crucial in regulating adenosine levels [8].
The inhibition of ADA has shown promise in attenuating inflammation in experimental colitis, indicating its potential as a target for therapeutic interventions in inflammatory conditions [9]. Additionally, the down-regulation of ADA gene expression has been linked to chronic heart failure, shedding light on ADA's role in the pathophysiology of this condition [10].
References:
[1] A. Cortés, E. Gracia, E. Moreno, J. Mallol, C. Lluı́s, E. Canelaet al., Moonlighting adenosine deaminase: a target protein for drug development, Medicinal Research Reviews, vol. 35, no. 1, p. 85-125, 2014. https://doi.org/10.1002/med.21324
[2] Y. Singh, S. Noarem, P. Devi, V. Kshetrimayum, R. Marbaniang, U. Debbarmaet al., Serum levels of adenosine deaminase and insulin in type 2 diabetes mellitus, International Journal of Biochemistry Research & Review, p. 18-23, 2020. https://doi.org/10.9734/ijbcrr/2020/v29i730202
[3] V. Khemka, D. Bagchi, A. Ghosh, O. Sen, A. Bir, S. Chakrabartiet al., Raised serum adenosine deaminase level in nonobese type 2 diabetes mellitus, The Scientific World Journal, vol. 2013, p. 1-5, 2013. https://doi.org/10.1155/2013/404320
[4] M. Torğutalp, C. Efe, H. Babaoğlu, & T. Kav, Relationship between serum adenosine deaminase levels and liver histology in autoimmune hepatitis, World Journal of Gastroenterology, vol. 23, no. 21, p. 3876, 2017. https://doi.org/10.3748/wjg.v23.i21.3876
[5] S. Pençe, I. Erkutlu, N. Kurtul, M. Alptekin, & Ü. Tan, Effects of progesterone on total brain tissue adenosine deaminase activity in experimental epilepsy, International Journal of Neuroscience, vol. 119, no. 2, p. 204-213, 2009. https://doi.org/10.1080/00207450802055374
[6] K. Vinapamula, S. Pemmaraju, S. Bhattaram, A. Bitla, & S. Manohar, Serum adenosine deaminase as inflammatory marker in rheumatoid arthritis, Journal of Clinical and Diagnostic Research, 2015. https://doi.org/10.7860/jcdr/2015/14296.6483
[7] R. Tamura, H. Ohta, Y. Satoh, S. Nonoyama, Y. Nishida, & M. Nibuya, Neuroprotective effects of adenosine deaminase in the striatum, Journal of Cerebral Blood Flow & Metabolism, vol. 36, no. 4, p. 709-720, 2016. https://doi.org/10.1177/0271678x15625077
[8] I. Norstrand, V. Siverls, & R. Libbin, Regional distribution of adenosine deaminase in the
human neuraxis, Enzyme, vol. 32, no. 1, p. 20-25, 1984. https://doi.org/10.1159/000469446
[9] L. Antonioli, M. Fornai, R. Colucci, N. Ghisu, F. Settimo, G. Nataleet al., Inhibition of adenosine deaminase attenuates inflammation in experimental colitis, Journal of Pharmacology and Experimental Therapeutics, vol. 322, no. 2, p. 435-442, 2007. https://doi.org/10.1124/jpet.107.122762
[10] I. Hisatome, Adenosine and cardioprotection in chronic heart failure: genes and protein expression, Hypertension Research, vol. 30, no. 9, p. 757-758, 2007. https://doi.org/10.1291/hypres.30.757
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