LongLife™ Zymolyase® (19 Citations)
Catalog
Description
Size
Price(USD)
Qty
Catalog
786-036
786-036
Description
LongLife™ Zymolyase® [1.5U/µl]
LongLife™ Zymolyase® [1.5U/µl]
Size
2 x 0.5ml
2 x 0.5ml
$110.00
$110.00
Catalog
786-914
786-914
Description
LongLife™ Zymolyase® [1.5U/µl]
LongLife™ Zymolyase® [1.5U/µl]
Size
5ml
5ml
$436.00
$436.00
Enzymes regularly used in laboratory applications often require preparation of fresh solution before each use. Making fresh enzyme solution for each application is time consuming and wasteful. G-Biosciences offers a wide variety of fresh, ready-to-use enzyme preparations.
Our high performance LongLife™ Zymolyase® preparation contains high yeast lytic activity with low non-specific activity. This ready-to-use solution has been stabilized and can be stored at -20ºC.
LongLife™ Zymolyase® is suitable for spheroplast preparation, yeast plasmid isolation (lysis of yeast cells and further extraction of soluble protein from them), glucan hydrolysis and more. The size of the supplied Longlife™ Zymolyase® is one mL (two 0.5mL vials included) in a concentration of 1,500 units per milliliter.
All LongLife™ Enzymes Available:
LongLife™ Zymolyase® for digestion of yeast & fungal cell walls
LongLife™ Lysozyme for digestion of bacterial cell walls
LongLife™ Proteinase K for digestion of proteins in nucleic acid preparations
LongLife™ Nuclease for removal of nucleic acids
LongLife™ RNase for digestion of RNA
LongLife™ DNase for digestion of DNA
LongLife™ PE LB Lysozyme for digestion of bacterial cell walls & reduction of viscosity build-up due to
presence of nucleases (fully compatible with our PE LB™Systems)
Features
- Ready-to-use enzyme prepartion
- High yeast lytic activity & low non-specific activity
Applications
- Spheroplast preparation
- Yeast plasmid isolation
- Lysis and extraction of protein from yeast cells
Protocol | |
786-036 | |
786-914 |
Material Safety Data Sheet | |
786-036 | |
786-914 |
Technical Literature | |
Increased stability of LongLife Zymolyase | |
Molecular Biology Handbook | A guide to our products for DNA and RNA. |
Protease & Phosphatase Inhibitors & Proteases Handbook | A handbook & selection guide for inhibitors of protease & phosphatases & for proteases & assays |
Sample Preparation Handbook | For Lysis Buffers, Fractionation, Dialysis, Protein Concentration and Enrichment |
Certificate Of Analysis | |
786-036 |
- Dipayan, Akhuli et al (2022) ALIBY: ALFA nanobody-based toolkit for imaging and biochemistry in yeast. MSPHERE. https://doi.org/10.1128/msphere.00333-22
- Hatano, Tomoyuki et al (2022) mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells. J CELL SCI. https://doi.org/10.1242/jcs.260288
- Bhardwaj, Vaibhav et al (2021) Deletion of the non-essential Rpb9 subunit of RNA polymerase II results in pleiotropic phenotypes in Schizosaccharomyces pombe. BIOCHIM BIOPHYS ACTA. https://doi.org/10.1016/j.bbapap.2021.140654
- Gupta, Aditi et al (2021) Characterization of the transactivation and nuclear localization functions of Pichia pastoris zinc finger transcription factor Mxr1p. J BIOL CHEM. https://doi.org/10.1016/j.jbc.2021.101247
- Kojima, Atsushi (2021) Validation of the usefulness of 265 rDNA D1/D2, internal transcribed spacer, and intergenic spacer 1 for molecular epidemiological analysis of Macrorhabdus ornithogaster. JSTAGE.
- Anderson, MZ. et al (2019) A ‘parameiosis’ drives depolyploidization and homologous recombination in Candida albicans. NAT COMMUN. 10:4388
- Rather, G.A. et al(2019) Molecular characterization and overexpression analyses of secologanin synthase to understand the regulation of camptothecin biosynthesis in Nothapodytes nimmoniana (Graham.) Mabb.
- Chew, T.G. et al (2017) Actin turnover maintains actin filament homeostasis during cytokinetic ring contraction. J Cell Biol.DOI: 10.1083/jcb.201701104
- Funk, I. et al (2017) Production of dodecanedioic acid via biotransformation of low cost plant-oil derivatives using Candida tropicalis. J Ind Microbiol Biotechnol. https://doi.org/10.1007/s10295-017-1972-6
- Pombejra, s. et al (2017) The Metalloprotease, Mpr1, Engages AnnexinA2 to Promote the Transcytosis of Fungal Cells across the Blood-Brain Barrier. Front Cell Infect Microbiol. https://doi.org/10.3389/fcimb.2017.00296
- Sahu, U. et al (2017) Methionine synthase is localized to the nucleus in Pichia pastoris and Candida albicans and to the cytoplasm in Saccharomyces cerevisiae. J Biol Chem. doi: 10.1074/jbc.M117.783019
- Bilyk, O. et al (2016) Cloning and Heterologous Expression of the Grecocycline Biosynthetic Gene Cluster. PLOS One. doi:10.1371/journal.pone.0158682
- Bilyk, O. (2015) Exploring chemical diversity of angucycline antibiotics: molecular basis of simocyclinone and grecocycline biosynthesis.
- Perlin et al. BMC Genomics (2015) 16:461
- Sahoo, A. et al (2015) Residue proximity information and protein model discrimination using saturation-suppressor mutagenesis. eLife 2015;10.7554/eLife.09532
- Muzny, C.A. et al (2014) Sex Transm. Unfect. doi:10.1136/sextrans-2013-051361
- Yu, X et al (2014) Appl. Microbiol. Biotechnol. Doi: 10.1007/s00253-014-5589-7
- Tashiro, R. et al (2010) Crop Sci. 50:1260
- Voth, D. et al (2004) Infect Immunol. 72: 3366