ARSA Mouse

Arylsulfatase A Mouse Recombinant

Recombinant ARSA Mouse, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain consisting of 498 amino acids (specifically, amino acids 18-506). It has a molecular mass of 53.2kDa. However, on SDS-PAGE, the molecular size appears to be between 50-70kDa. This ARSA protein is expressed with a 6 amino acid His tag at its C-Terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22821
Source
Sf9, Baculovirus cells.
Appearance
A clear solution that has been sterilized by filtration.

ARSA Mouse, Active

Arylsulfatase A Mouse Recombinant, Active

Recombinant ARSA Mouse protein, expressed in Sf9 cells, is a single, glycosylated polypeptide chain consisting of 498 amino acids (positions 18-506), with a molecular mass of 53.2 kDa. It's important to note that on SDS-PAGE, the apparent molecular size might range from 50 to 70 kDa. The ARSA Mouse protein includes a 9-amino acid His-Tag fused at its C-terminus and is purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT22917
Source
Sf9, Baculovirus cells.
Appearance
The product appears as a clear solution that has been sterilized through filtration.

ARSG Human

Arylsulfatase G Human Recombinant

Recombinant human ARSG, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 532 amino acids (17-525) with a molecular weight of 57kDa. For purification, it is tagged with a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23003
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

IDS Human

Iduronate 2-Sulfatase Human Recombinant

Recombinant human IDS, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 533 amino acids (26-550a.a) with a molecular mass of 60.3 kDa. (Molecular size on SDS-PAGE will appear at approximately 35-70 kDa). IDS is fused to an 8 amino acid His-tag at the C-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23094
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered, clear solution.

SUMF1 Human

Sulfatase Modifying Factor 1 Human Recombinant

This product consists of the recombinant human SUMF1 protein, produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 304 amino acids (specifically, amino acids 91 to 374) with a molecular weight of 34.1 kDa. The protein is engineered with a 20 amino acid His-tag at the N-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23181
Source
E.coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.

ARSA Human, SF9

Arylsulfatase A Human Recombinant, Sf9

Produced in Sf9 insect cells using a baculovirus expression system, ARSA is a single, glycosylated polypeptide chain. It consists of 498 amino acids (with a sequence spanning from amino acid 21 to 509) and has a molecular weight of 53.0 kDa. On SDS-PAGE, its apparent molecular size will be approximately 50-70 kDa. This ARSA protein is engineered with a 9 amino acid His tag at its C-terminus to facilitate purification, which is carried out using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT22644
Source

Sf9, Baculovirus cells.

Appearance
A clear solution that has been sterilized by filtration.

ARSA Human

Arylsulfatase A Human Recombinant

Recombinant human ARSA, produced in E.coli, is a single, non-glycosylated polypeptide chain consisting of 512 amino acids (21-509) with a molecular weight of 54.3kDa. It is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT22725
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

SUMF1 Human, Sf9

Sulfatase Modifying Factor 1 Human Recombinant, Sf9

SUMF1, produced in Sf9 insect cells, is a single, glycosylated polypeptide chain with a molecular weight of 38.1 kDa. The recombinant protein encompasses amino acids 34 to 374 and includes a 6-amino acid His tag at the C-terminus. Its apparent molecular size on SDS-PAGE is approximately 40-57 kDa. SUMF1 is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23260
Source

Sf9, Insect cells.

Appearance
Sterile Filtered colorless solution.
Definition and Classification

Sulfatases are a class of enzymes that catalyze the hydrolysis of sulfate esters into an alcohol and a bisulfate . These enzymes are crucial in the metabolism of sulfate esters, which are found in a variety of biological molecules including steroids, carbohydrates, and proteins . Sulfatases are classified into four main families based on sequence homology:

  • S1 Family: Formylglycine-dependent sulfatases
  • S2 Family: Alkylsulfodioxygenases
  • S3 Family: Alkylsulfohydrolases
  • S4 Family: Arylsulfohydrolases .
Biological Properties

Sulfatases are expressed in various cellular compartments such as the lysosome, endoplasmic reticulum, and Golgi apparatus . They are activated by the unusual amino acid formylglycine, which is formed from cysteine at the catalytic center . These enzymes are extensively glycosylated and follow specific trafficking pathways through cells . Sulfatases are distributed in a wide range of tissues, including the central and peripheral nervous systems, connective tissues, liver, placenta, and skin .

Biological Functions

Sulfatases play a pivotal role in the regulation of cell metabolism and developmental cell signaling . They cleave sulfate groups from sulfate esters contained in hormones, proteins, and complex macromolecules . This activity is essential for the homeostasis of the body, maintaining neuronal function, chondrogenesis, detoxification, steroid hormone inactivation, and skin humidification . Sulfatases are also involved in immune responses and pathogen recognition .

Modes of Action

Sulfatases operate by hydrolyzing sulfate esters through a highly conserved cysteine in their active site, which is post-translationally converted into formylglycine . This post-translational modification activates all sulfatases . They interact with various molecules and cells, including proteoglycans, glycoproteins, and glycolipids, modulating specific signaling pathways and cell metabolism . Sulfatases also play a role in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome .

Regulatory Mechanisms

The expression and activity of sulfatases are regulated by various mechanisms, including transcriptional regulation and post-translational modifications . Cytokines, growth factors, and steroids can influence sulfatase activity . The formylglycine-generating enzyme encoded by SUMF1 is crucial for the activation of sulfatases through post-translational modification . Additionally, sulfatases are extensively glycosylated, which affects their trafficking and function within cells .

Applications

Sulfatases have significant applications in biomedical research, diagnostic tools, and therapeutic strategies . They are used in the study of metabolic disorders, lysosomal storage diseases, and hormone-dependent cancers . Sulfatases are also employed in the development of enzyme replacement therapies and gene therapies . In addition, they have potential applications in biocatalysis for the production of novel sulfated oligomers used in pharmaceuticals and cosmetics .

Role in the Life Cycle

Sulfatases play a crucial role throughout the life cycle, from development to aging and disease . During development, they are involved in the regulation of cell signaling and metabolism . In adulthood, sulfatases maintain homeostasis and are essential for various physiological processes . In aging and disease, defects in sulfatase activity can lead to lysosomal storage disorders and other metabolic conditions . Sulfatases are also implicated in the immune response and cognitive function .

© Copyright 2024 Thebiotek. All Rights Reserved.