G3153
β-Galactosidase from Escherichia coli
lyophilized powder, ≥500 units/mg protein
Synonim(y):
β-D-Galactoside galactohydrolase, Lactase
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5 MG
2790,00 zł
2790,00 zł
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Informacje o tej pozycji
Numer CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-864-1
MDL number:
Specific activity:
≥500 units/mg protein
Recombinant:
expressed in E. coli
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Pozwól nam pomócrecombinant
expressed in E. coli
form
lyophilized powder
specific activity
≥500 units/mg protein
mol wt
465 kDa
storage temp.
−20°C
Quality Level
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1 of 4
Ta pozycja | |||
|---|---|---|---|
| specific activity ≥500 units/mg protein | specific activity ≥500 units/mg protein | specific activity ≥2600 units/g | specific activity ≥0.15 units/mg protein |
| recombinant expressed in E. coli | recombinant - | recombinant - | recombinant - |
| form lyophilized powder | form lyophilized powder | form liquid | form lyophilized powder |
| mol wt 465 kDa | mol wt 465 kDa | mol wt - | mol wt - |
| storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C |
| Quality Level 200 | Quality Level 300 | Quality Level 200 | Quality Level 200 |
General description
Tetramer molecular weight 465 kDa (subunits 116.3 kDa each)
Application
β-Galactosidase from Escherichia coli has been used to produce biocatalytic Ca-alginate beads on a B-390 encapsulator (BUCHI).[3] It has been used to prepare the source droplet solution and also as the cargo for Pep-1 (KETWWETWWTEWSQPKKKRKV-cysteamide).[4]
β-Galactosidase may be used for derivatization, such as an enzyme label for IgG, without prior dialysis or gel filtration.[5]
Biochem/physiol Actions
β-galactosidase cleaves lactose into its monosaccharide components, glucose and galactose. It also catalyses the transglycosylation of glucose into allolactose, the inducer of β-galactosidase, in a feedback loop.
β-galactosidase is considered as a reporter enzyme in applications involving gene expression regulation, analysis of protein function/structure and target gene expression.[6]
Packaging
Package size based on protein content
Physical form
Stabilized with phosphate buffer and sucrose
Other Notes
One unit will hydrolyze 1.0 μmole of o-nitrophenyl β-D-galactopyranoside to o-nitrophenol and D-galactose per min at pH 7.3 at 37 °C.
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Numer produktu
Opis
Cennik
used together
Numer produktu
Opis
Cennik
Klasa składowania
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
M J O'Sullivan et al.
Annals of clinical biochemistry, 16(5), 221-240 (1979-09-01)
In the last few years, the use of enzyme labels in immunoassays has been investigated. The aim of this review is to evaluate critically the role of such labels in clinical biochemistry. Special attention has been given to the problems
Structure of beta-galactosidase at 3.2-AA resolution obtained by cryo-electron microscopy
Bartesaghi A, et al.
Proceedings of the National Academy of Sciences of the USA, 111(32), 11709-11709 (2014)
Peptide-Mediated Membrane Transport of Macromolecular Cargo Driven by Membrane Asymmetry
Li X, et al.
Analytical Chemistry, 89(22), 12369-12374 (2017)
Application of galactose-sensitive E. coli strains as selective hosts for LacZ-plasmids.
Gossen JA, et al.
Nucleic Acids Research, 20(12), 3254-3254 (1992)
Samuel Berhanu et al.
Journal of basic microbiology, 62(6), 669-688 (2022-03-16)
pUC18 and pUC19 are well-known high copy-number plasmid vectors routinely used for DNA cloning purposes. We show here that, in Escherichia coli transformed by native pUC18, the α-complementation of β-galactosidase (i.e., mediated by the peptide LacZα18) is intrinsically weak and
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