10745731001

β-Galactosidase

EIA grade

• 동의어(들): β galactosidase, β-galactosidase
• 효소 위원회 번호: 3.2.1.23 (BRENDA, IUBMB)
• UNSPSC 코드: 12352204

속성

• 생물학적 소스: Escherichia coli
• Quality Level: 100
• 분석: (single peak, HPLC)
• 양식: lyophilized
• 특이 활성도: 750-950 U/mg
• 분자량: 540.000 kDa
• 포장: pkg of 25 mg (approx. 100 mg lyophilizate)
• 제조업체/상표: Roche
• 기술: enzyme immunoassay: suitable
• 색상: white
• pH: 7.3-7.7
• solubility: water: 20 mg/mL
• λmax: 405
• 적합성: suitable for immunoassay
• NCBI 수납 번호: WP_050940144
• UniProt 수납 번호: P00722; ; ; ; P00722
• 응용 분야: life science and biopharma
• 배송 상태: dry ice
• 저장 온도: −20°C (−15°C to −25°C)
• 유전자 정보: Escherichia coli ... lacZ(945006)

설명

일반 설명

β-Galactosidase, EIA grade, is a lyophilizate from E. coli overproducer, consisting of enzyme protein, phosphate buffer, and sucrose. Substances which could interfere with the derivatization of NH₂ or SH groups (e.g., 2-mercaptoethanol, ammonium salts, primary amines etc.) have been removed.

The GLB1 (β-Galactosidase) gene is mapped to human chromosome 3p22.3.[1] The encoded protein belongs to glycosyl hydrolase 35 family and is localized to lysosomes.[2]

애플리케이션

β-Galactosidase has been used as a standard to determine the absolute quantitation of LacZ protein.[3]

β-Galactosidase is used for labeling enzyme immunoassay techniques. β-Galactosidase can be coupled to other proteins via its SH-groups. The reconstituted solution can be used directly for conjugation without prior dialysis or gel permeation chromatography.

생화학적/생리학적 작용

β-Galactosidase catalyzes the hydrolysis of terminal β-galactose residue of ganglioside substrates, such as glycoproteins, sphingolipids, and keratan sulfate and other glycoconjugates.[2][4] This enzyme is associated with the mechanism of cell senescence and carcinogenesis.[2] Mutations in the gene result in gangliosidosis, an autosomal recessive disorder, characterized with defective lysosomal storage due to accumulation of substrates.[5][4] β-Galactosidase deficiency also causes Morquio B syndrome indicating skeletal abnormalities, short stature and increased excretion of keratan sulfate in urine.[4]

품질

Purity: single peak (HPLC)

서열

Free Thiol Groups
The non-denatured, enzymatically-active preparation contains > 12 SH groups per molecule which are not involved in disulfide bridges and are freely accessible to coupling reagents in aqueous media (as assayed with Ellman′s reagent at +37 °C, acc. to Habeeb, 1972).

Absence of Enzyme Aggregates
The preparation contains < 3% dimers (HPLC, area %) and essentially no higher oligomers.

물리적 형태

Lyophilizate, stabilized with phosphate buffer and sucrose. Note: Contains at least 12 free SH-groups/enzyme molecule; 5 mg approximately 20 mg lyophilizate; 25 mg approximately 100 mg lyophilizate.

저장 및 안정성

Store at -15–-25 °C. (sealed under nitrogen)

분석 메모

Specific activity: approximately 750 - 950 U/mg enzyme protein ≅ approximately 150 - 250 U/mg lyophilizate (+37°C, 2-nitrophenyl-β-D-galactoside); approximately 250-400 U/mg enzyme protein ≅ approximately 60-100 U/mg lyophilizate (+37°C, 4-nitrophenyl-β-D-galactoside).

기타 정보

For life science research only. Not for use in diagnostic procedures.

안전성 정보

• Storage Class Code: 11 - Combustible Solids
• WGK: WGK 1
• Flash Point (°F): does not flash
• Flash Point (°C): does not flash