Code | CSB-YP361972TIQ |
MSDS | |
Size | Pls inquire |
Source | Yeast |
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Code | CSB-EP361972TIQ |
MSDS | |
Size | Pls inquire |
Source | E.coli |
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Code | CSB-EP361972TIQ-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-BP361972TIQ |
MSDS | |
Size | Pls inquire |
Source | Baculovirus |
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Code | CSB-MP361972TIQ |
MSDS | |
Size | Pls inquire |
Source | Mammalian cell |
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Proteinase K (PROK) is a highly active extracellular alkaline serine endopeptidase from Tritirachium album limber, belonging to the subtilisin family [1][2]. It is known for its ability to digest native keratin and is widely used for facilitating nucleic acid isolation by degrading contaminating proteins in cell lysates and for inactivating enzymes such as DNase and RNase without denaturation [3]. Proteinase K is a useful tool for the preparation of protein-free samples of DNA or RNA due to its properties [4]. Moreover, it is used as a research tool for investigating pathogenic mechanisms in neurodegeneration [5]. The enzyme's structure is affected by various factors, which in turn govern its catalytic proficiency, and even small structural changes can have detrimental effects on its activity [6]. Proteinase K has a substrate recognition site that includes specific residues, and its crystal structure has been determined by X-ray diffraction studies [7][8]. Additionally, it is known that the enzyme exhibits a strong similarity to bacterial subtilisins [9].
The enzyme's properties make it a valuable tool in various fields, including molecular biology, biochemistry, and neurodegenerative disease research. Its ability to degrade proteins without denaturation makes it essential in nucleic acid isolation and enzyme inactivation. The structural characteristics and substrate recognition site of Proteinase K provide insights into its catalytic mechanism and potential applications in protein engineering. Furthermore, its similarity to bacterial subtilisins suggests evolutionary and functional relationships that could be explored further.
References:
[1] J. Pandhare, C. Dash, M. Rao, & V. Deshpande, "Slow tight binding inhibition of proteinase k by a proteinaceous inhibitor", Journal of Biological Chemistry, vol. 278, no. 49, p. 48735-48744, 2003. https://doi.org/10.1074/jbc.m308976200
[2] C. Betzel, S. Gourinath, P. Kumar, P. Kaur, M. Perbandt, S. Eschenburget al., "Structure of a serine protease proteinase k from tritirachium album limber at 0.98 å resolution", Biochemistry, vol. 40, no. 10, p. 3080-3088, 2001. https://doi.org/10.1021/bi002538n
[3] J. Arnórsdóttir, "Crystallographic studies on a cold adapted subtilase and proteins involved in mrna processing",. https://doi.org/10.53846/goediss-538
[4] G. Pal, C. Kavounis, K. Jany, & D. Tsernoglou, "The three‐dimensional structure of the complex of proteinase k with its naturally occurring protein inhibitor, pki3", Febs Letters, vol. 341, no. 2-3, p. 167-170, 1994. https://doi.org/10.1016/0014-5793(94)80450-8
[5] S. Abd-Elhadi, A. Honig, D. Simhi-Haham, M. Schechter, E. Linetsky, T. Ben-Huret al., "Total and proteinase k-resistant α-synuclein levels in erythrocytes, determined by their ability to bind phospholipids, associate with parkinson’s disease", Scientific Reports, vol. 5, no. 1, 2015. https://doi.org/10.1038/srep11120
[6] C. Xu, A. Battig, B. Schartel, R. Siegel, J. Senker, I. Forstet al., "Investigation of the thermal stability of proteinase k for the melt processing of poly(l-lactide)", Biomacromolecules, vol. 23, no. 11, p. 4841-4850, 2022. https://doi.org/10.1021/acs.biomac.2c01008
[7] S. Koszelak, J. Ng, J. Day, T. Ko, a. Greenwood, & A. McPherson, "The crystallographic structure of the subtilisin protease from penicillium cyclopium,", Biochemistry, vol. 36, no. 22, p. 6597-6604, 1997. https://doi.org/10.1021/bi963189t
[8] K. Yamashita, Y. Kikkawa, K. Kurokawa, & Y. Doi, "Enzymatic degradation of poly(l-lactide) film by proteinase k: quartz crystal microbalance and atomic force microscopy study", Biomacromolecules, vol. 6, no. 2, p. 850-857, 2005. https://doi.org/10.1021/bm049395v
[9] G. Fa and G. Hg, "Proteinase k from tritirachium album limber", European Journal of Biochemistry, vol. 179, no. 1, p. 185-194, 1989. https://doi.org/10.1111/j.1432-1033.1989.tb14539.x
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