Alpha Galactosidase

Cat. No.: A489917
주문 가능
GRADE & PURITY Specific Activity >30 U/mg;Activity 80 U/ml
Bioactivity
400 U/ml
★
Size
USA
독일 (EU)*
Price
Qty
20μl
A489917-20μl
US 주문제작 · 2–4주 ·
—
US$999.90
60μl
A489917-60μl
US 주문제작 · 2–4주 ·
—
US$2,199.90
Enter a quantity for the sizes you want to add.
🧪

Why this grade

Specific Activity >30 U/mg;Activity 80 U/ml for sensitive chromatographic and analytical workflows requiring minimal baseline interference.

🌡

Storage & shipping

Store at 2-8°C Ships Wet ice Check lot-specific COA for exact specifications.

📋

Quality documents

SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.

📚

Literature proof

Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.

개요

Product Description

Alpha Galactosidase from E. coli cleaves α(1-3)- and α(1-6)-linked, non-reducing terminal galactose from complex carbohydrates and glycoproteins. There is no activity on α(1-4) linked galactose. It is particularly efficient for removing α-linked galactose under conditions where the pH must be neutral or above, for example, with living cells.


Molecular Weight

~80,000 daltons


Contents

Alpha galactosidase in 50 mM sodium phosphate, pH 7.5

included with 20 µL and 60 µl pack sizes:

Reaction buffer - 250mM Sodium phosphate, pH 6.5


Specificity

Non-reducing terminal alpha-(1-3)- and alpha-(1-6)- galactose. There is no activity on alpha-(1-4)-galactose.


Stability

Stable at least 12 months when stored properly. Several days exposure to ambient temperatures will not reduce activity.


Specific Activity

One unit of alpha-(1-3,6) Galactosidase is defined as the amount of enzyme required to produce 1 µmole of p-nitrophenol (pNP) in 1 minute at 25°C pH 6.5 from p-nitrophenyl-alpha-D-galactopyranoside.


Purity

α(1-3,6) galactosidase is tested for contaminating protease as follows; 10 μg of denatured BSA is incubated for 24 hours at 37°C with 2 μL of enzyme. SDS-PAGE analysis of the treated BSA shows no evidence of degradation.

The production host strain has been extensively tested and does not produce any detectable glycosidases.of the BSA band after SDS-PAGE should show no evidence of degradation.


Directions for use

1. Add up to 100 µg of asialoglycoprotein or 1 nmol of oligosaccharide to tube.

2. Add water to 13 µl and 4 µl 5X Reaction Buffer.

3. Add 2 µl alpha-(1-3,6)-Galactosidase.

4. Incubate at 37°C for 1 hour. Longer incubations are necessary if fucose is present on the penultimate sugar.


Applications

Structural analysis of oligosaccharides

Xenograft transplantation studies

Removing heterogeneity from glycoproteins

Specifications

Product Name
Alpha Galactosidase
동의어
α-D-galactoside galactohydrolase, melibiase
사양 및 순도
Specific Activity >30 U/mg;Activity 80 U/ml
생체 활성
400 U/ml
효소 커미션 번호
3.2.1.22
분자 유형
Enzyme
보관 및 배송
집중력
Specific Activity >30 U/mg;Activity 80 U/ml
보관 조건
Store at 2-8°C
배송
Wet ice

Documentation

📋 Safety Data Sheet (SDS)

Comprehensive hazard, handling, storage, and regulatory compliance document.

Download SDS →

✅ Certificate of Analysis (COA)

Lot-specific quality data. Enter your lot number to retrieve the exact COA.

Look up COA →

📊 Datasheet

Quick-reference summary of product specifications and applications.

View datasheet →

🔬 Specification Sheet

Full quality attributes and acceptance criteria for this grade.

View spec sheet →

Advanced Data

인증서(CoA, COO, BSE/TSE 및 분석 차트)
C of A & Other Certificates(BSE/TSE, COO):
Analytical Chart:
솔루션 계산기
리뷰

고객 리뷰

자주 묻는 질문

How should this product be stored?
Store at 2–8 °C. Refrigerated storage is required to maintain the specified shelf life.
How is this product shipped?
This product ships chilled on wet ice. Unpack on arrival and transfer it to the storage condition stated above.
What documentation is provided?
Available product documentation, including Certificates of Analysis (COA), Safety Data Sheets (SDS), and specification sheets, is shown in the product document area. Document availability and access follow the current site policy.

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