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일반 설명
β-galactosidase is a 465 kDa tetrameric protein. It is coded by the LacZ gene.
애플리케이션
β-Galactosidase from Escherichia coli has been used to produce biocatalytic Ca-alginate beads on a B-390 encapsulator (BUCHI). It has been used to prepare the source droplet solution and also as the cargo for Pep-1 (KETWWETWWTEWSQPKKKRKV-cysteamide).
β-Galactosidase may be used for derivatization, such as an enzyme label for IgG, without prior dialysis or gel filtration.
생화학적/생리학적 작용
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.
포장
Package size based on protein content
물리적 특성
Tetramer molecular weight 465 kDa (subunits 116.3 kDa each)
단위 정의
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.
물리적 형태
Stabilized with phosphate buffer and sucrose
기질
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
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시험 성적서(COA)
Lot/Batch Number
이미 열람한 고객
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)
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
Bi-Enzymatic Embolization Beads for Two-Armed Enzyme-Prodrug Therapy
Olesen MTJ, et al.
Advances in Therapy, 1(4), 1800023-1800023 (2018)
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