추천 제품
재조합
expressed in E. coli
Quality Level
형태
buffered aqueous solution
특이 활성도
≥6 units/mg protein
포장
vial of 0.06 unit
UniProt 수납 번호
배송 상태
wet ice
저장 온도
2-8°C
유전자 정보
human ... GLB1(2720)
관련 카테고리
일반 설명
β-Galactosidase is present in bacteria, fungi, yeast and animal organs. It is also found in fruits, such as apples, almonds and apricots. β-Galactosidase is a tetramer and is made up of four polypeptide chains consisting of amino acids that assemble to form five structural domains. The domains are jelly roll barrel, a central domain that serves as an active site and the remaining domains are composed of β-sandwich and fibronectin.
애플리케이션
β(1→4)-Galactosidase, positionally specific from Streptococcus pneumonia has been used:
- as a position-specific enzyme to study its effects in the terminal galactosylation with protective efficacy of glycosphingolipid (GSPL) in mice.
- for the digestion of radioactive oligosaccharides.
- as a position-specific enzymeto study its effects on the virulence profile of avirulent Leishmania donovani clone (A-LD).
생화학적/생리학적 작용
β-Galactosidase plays a role in hydrolyzing the D-galactosyl moieties in oligosaccharides, polymers and secondary metabolites. It is widely applicable in the dairy industry to remove lactose from milk and dairy products for the benefit of lactose-intolerant individuals. β-Galactosidase is also applicable in the food industry to improve the sweetness, flavor and solubility.
단위 정의
One unit will hydrolyze 1 μmole of p-nitrophenyl β-D-galactopyranoside per min at pH 5.0 at 37 °C.
물리적 형태
Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
Qayyum Husain
Critical reviews in biotechnology, 30(1), 41-62 (2010-02-11)
Beta galactosidases have been obtained from microorganisms such as fungi, bacteria and yeasts; plants, animals cells, and from recombinant sources. The enzyme has two main applications; the removal of lactose from milk products for lactose intolerant people and the production
TLR4 and NKT cell synergy in immunotherapy against visceral leishmaniasis
Karmakar S, et al.
PLoS Pathogens, 8(4), 79-79 (2012)
S K Bhaumik et al.
Glycoconjugate journal, 25(5), 459-472 (2008-01-17)
Protozoan parasites of the genus Leishmania are the causative agent of leishmaniasis, a disease whose manifestations in humans range from mild cutaneous lesions to fatal visceral infections. Human visceral leishmaniasis is caused by Leishmania donovani. Long-term culture in vitro leads
beta Galactosidases and their potential applications: a review
Husain Q
Critical Reviews in Biotechnology, 30(1), 41-62 (2010)
Andrew J Hanneman et al.
Glycobiology, 16(9), 874-890 (2006-06-14)
Analysis of protein glycosylation within the nematode Caenorhabditis elegans has revealed an abundant and unreported set of core chitobiose modifications (CCMs) to N-linked glycans. With hydrazine release, an array of glycomers and isobars were detected with hexose extensions on the
문서
Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.
자사의 과학자팀은 생명 과학, 재료 과학, 화학 합성, 크로마토그래피, 분석 및 기타 많은 영역을 포함한 모든 과학 분야에 경험이 있습니다..
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