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)
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
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
TLR4 and NKT cell synergy in immunotherapy against visceral leishmaniasis
Karmakar S, et al.
PLoS Pathogens, 8(4), 79-79 (2012)
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
beta Galactosidases and their potential applications: a review
Husain Q
Critical Reviews in Biotechnology, 30(1), 41-62 (2010)
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
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..
고객지원팀으로 연락바랍니다.