Beta-galactosidase Enzyme Acceptor
For Laboratory Research Only. Not for Clinical or Personal Use.
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Beta-galactosidase Enzyme Acceptor
Description:
Beta-galactosidase Enzyme Acceptor (Omega peptide)_x000D__x000D_ _x000D_
_x000D_ This Molecular Depot product has been used in the following publication:_x000D_ _x000D_ _x000D_ _x000D_ Download Alpha Complementation Product Line Brochure._x000D__x000D_ _x000D_Catalog # _x000D_P2010005 _x000D__x000D_ _x000D_Size _x000D_1.0 mg _x000D__x000D_ _x000D_Other Names _x000D_Beta-galactosidase Omega Domain _x000D__x000D_ _x000D_Supplied as _x000D_White lyophilized powder. _x000D__x000D_ _x000D_Molecular Weight _x000D_113 kDa (997 amino residues) _x000D__x000D_ _x000D_Purity _x000D_>95% (SDS PAGE) _x000D__x000D_ _x000D_Storage _x000D_-20°C. Avoid repeated freeze/thaw cycles. _x000D__x000D_ _x000D_Suggested buffer _x000D_Beta-galactosidase Enzyme Acceptor Stabilization Buffer (B2010002) _x000D__x000D_ _x000D_Keywords _x000D_Beta-galactosidase Omega Domain, Enzyme Acceptor, alpha complementation, LacZ. _x000D__x000D_ _x000D_ _x000D_Related products _x000D_Beta-galactosidase Enzyme Donor (Alpha Peptide), Beta-galactosidase Enzyme Acceptor Stabilization Buffer, Beta-galactosidase Alpha Complementation Kit. _x000D_About Beta-galactosidase Alpha Complementation
_x000D_Beta-galactosidase Alpha-Complementation is a biochemical phenomenon first documented by Agnes Ullmann, while working in the lab of François Jacob and Jacques Monod. By means of molecular cloning, the native E. coli β-galactosidase enzyme can be split in two inactive fragments of different sizes. The smaller fragment, known as the alpha-peptide or enzyme donor, is about 100 amino residues in length and is inactive on its own (incapable of hydrolyzing a β-galactosidase substrate). The larger fragment, known as the omega fragment or enzyme acceptor, is about 900 amino residues in length and is also inactive on its own. Upon mixing the enzyme donor with the enzyme acceptor, the β-galactosidase enzyme is reconstituted and is now capable of hydrolyzing colorimetric substrates such as ONPG.
_x000D_Both enzyme donor and enzyme acceptor can be cloned and expressed in special E. coli strains to yield highly pure, zero-background enzyme fragments (i.e. an enzyme donor and enzyme acceptor without measurable catalytic activities, when assayed individually). Interestingly, it was discovered that various analytes can be conjugated to the enzyme donor moiety and the enzyme donor-enzyme acceptor association modulated by an analyte-binding molecule (such as an antibody). As a result, an alpha-complementation-based assay can be developed.
_x000D_ _x000D_References
_x000D_- _x000D_
- Kras, E. (2019). Beta-galactosidase: properties, structure and functions. New York: Nova Science Publishers. _x000D_
- Arndt, T. (2017). Cloned Enzyme Donor Immunoassay. Lexikon Der Medizinischen Laboratoriumsdiagnostik, 1–2. _x000D_
- Jeon, S. I., Yang, X., and Andrade, J. D. (2004). Modeling of homogeneous cloned enzyme donor immunoassay. Analytical Biochemistry, 333(1), 136–147. _x000D_
- Tachi, T., Kaji, N., Tokeshi, M., and Baba, Y. (2009). Microchip-based Homogeneous Immunoassay Using a Cloned Enzyme Donor. Analytical Sciences, 25(2), 149–151. _x000D_
- Khanna, P. L., and Worthy, T. E. (1993). CEDIA: A Recombinant-Based Homogeneous Enzyme Immunoassay. _x000D_
Short Description:
Catalog #: P2010005 (1 mg)Weight:
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