GLA Human

Alpha-Galactosidase Human Recombinant

GLA, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain consisting of 406 amino acids (specifically, amino acids 32 to 429). With a molecular mass of 46.4 kDa, this GLA protein is expressed with an 8 amino acid His tag at the C-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21148
Source
Sf9, Baculovirus cells.
Appearance
The product is a sterile, colorless solution that has been filtered for sterility.

GLB1 E.Coli

Galactosidase-Beta 1 E.coli Recombinant

Originating from E. coli, the recombinant Beta-galactosidase protein (114 kDa) is characterized by its enzymatic inactivity and lack of reactivity with human serum.
Shipped with Ice Packs
Cat. No.
BT21262
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered for sterility.

GLB1 Human

Galactosidase-Beta 1 Human Recombinant

Recombinant human GLB1, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. It comprises 662 amino acids (with a sequence spanning from amino acid 24 to 677) and has a molecular weight of 74.6 kDa.
For purification and detection purposes, the GLB1 protein contains an 8-amino acid Histidine tag fused at its C-terminus. The protein has been purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT21327
Source

Sf9, Baculovirus cells.

Appearance
A clear, colorless solution that has been sterilized by filtration.

melA E. coli

Alpha-Galactosidase E.coli Recombinant

Recombinant melA from E. coli, produced in E. coli, is a single polypeptide chain comprising 474 amino acids (residues 1-451) with a molecular mass of 53.0 kDa. The protein consists of the melA sequence fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21411
Source
E.coli.
Appearance
A sterile, colorless solution.

NAGA Human

N-Acetylgalactosaminidase Alpha Human Recombinant

Recombinant human NAGA, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. It consists of 400 amino acids (residues 18-411), resulting in a molecular mass of 45.5 kDa. However, on SDS-PAGE analysis, the apparent molecular size ranges from 40 to 57 kDa. The protein incorporates a C-terminal 6-amino acid His-tag and undergoes purification via proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT21505
Source
Sf9, Baculovirus cells.
Appearance
The product is a clear solution that has been sterilized by filtration.
Definition and Classification

Galactosidases are enzymes (glycoside hydrolases) that catalyze the hydrolysis of galactosides into monosaccharides . They are classified into two main types based on the glycosidic linkage they hydrolyze: alpha-galactosidase and beta-galactosidase . Alpha-galactosidase hydrolyzes substrates containing α-galactosidic residues, such as glycosphingolipids or glycoproteins . Beta-galactosidase, on the other hand, breaks down the disaccharide lactose into glucose and galactose .

Biological Properties

Key Biological Properties: Galactosidases possess both hydrolytic and transgalactosylation properties . They are essential for the breakdown of complex carbohydrates into simpler sugars.

Expression Patterns and Tissue Distribution: Beta-galactosidase is widely expressed in various tissues, including the liver, kidneys, and intestines . Alpha-galactosidase is predominantly found in lysosomes and is encoded by the GLA gene .

Biological Functions

Primary Biological Functions: Galactosidases play a crucial role in carbohydrate metabolism by breaking down galactosides into monosaccharides . This process is vital for energy production and carbon sourcing.

Role in Immune Responses and Pathogen Recognition: Galactosidases are involved in the degradation of glycoproteins and glycolipids, which can influence immune responses and pathogen recognition .

Modes of Action

Mechanisms with Other Molecules and Cells: Galactosidases catalyze the hydrolysis of glycosidic bonds through a double-displacement mechanism . This involves the transfer of a sugar residue from a glycosyl donor to an acceptor.

Binding Partners and Downstream Signaling Cascades: Beta-galactosidase interacts with various substrates, including lactose, ganglioside GM1, and lactosylceramides . These interactions can trigger downstream signaling cascades that regulate metabolic processes.

Regulatory Mechanisms

Transcriptional Regulation: The expression of beta-galactosidase is regulated by the lac operon in bacteria, which is activated in the presence of lactose and repressed when glucose levels are sufficient .

Post-Translational Modifications: Galactosidases undergo various post-translational modifications, including glycosylation, which can affect their stability and activity .

Applications

Biomedical Research: Galactosidases are used as biomarkers in gene expression studies and enzyme-linked immunosorbent assays (ELISAs) .

Diagnostic Tools: Beta-galactosidase is employed in diagnostic assays for lactose intolerance and other metabolic disorders .

Therapeutic Strategies: Alpha-galactosidase is used in enzyme replacement therapy for Fabry disease, a genetic disorder caused by the deficiency of this enzyme .

Role in the Life Cycle

Development to Aging and Disease: Galactosidases play a significant role throughout the life cycle. During development, they are involved in the breakdown of maternal milk lactose in infants . In adults, they aid in the digestion of dietary lactose and other galactosides . Deficiencies in galactosidase activity can lead to metabolic disorders such as galactosialidosis and Morquio B syndrome .

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