ARSB Antibodies

Structure of ARSB

Aryl sulfatase B encoded by the ARSB gene is a lysosomal hydrolase with a molecular weight of approximately 58 kDa. This protein is composed of 533 amino acids, and its polypeptide chain folds to form a typical lysosomal enzyme spherical structure, with the active center containing highly conserved cysteine residues. There are subtle differences in the molecular weight of ARSB protein among different mammals, as follows:

The tertiary structure of this enzyme forms stable substrate-binding domains through multiple α -helicles and β -folds, which can specifically recognize and hydrolyze the sulfate ester bonds in heparan sulfate and dermatid sulfate. Its catalytic mechanism relies on the precise spatial conformation within the active center, enabling water molecules to carry out nucleophilic attacks on the substrate and complete the desulfation reaction.

Fig. 1 Three-dimensional structure of ARSB.¹

Key structural properties of ARSB:

• Typical globular folded conformation of lysosomal enzymes
• Catalytic active centers composed of α/β domains
• Highly conserved cysteine residues in the substrate binding pocket

Functions of ARSB

The main function of aryl sulfatase B (ARSB) is to catalyze the hydrolysis of sulfate ester bonds of glycosaminoglycans (GAGs) within lysosomes. In addition, this enzyme is also involved in the regulation of various cellular processes, including extracellular matrix remodeling and signal transduction regulation.

The catalytic efficiency of this enzyme is significantly influenced by the sulfation mode of the substrate and the pH environment of the lysosome. It has the highest activity under the most suitable acidic conditions, demonstrating a high degree of adaptation to the microenvironment of the lysosome.

Applications of ARSB and ARSB Antibody in Literature

1. Bartolomeo, Rosa, et al. "Pharmacological read-through of nonsense ARSB mutations as a potential therapeutic approach for mucopolysaccharidosis VI." Journal of inherited metabolic disease 36.2 (2013): 363-371. https://doi.org/10.1007/s10545-012-9521-y

The article indicates that MPS VI studies targeting nonsense mutations in the ARSB gene show that PTC124 can induce stop codon reading, restore ARSB enzyme activity to 2.5% of the wild type, and reduce lysosomal volume. This result indicates that through-reading therapy is expected to become a potential treatment strategy for such patients.

2. Hosoba, Kosuke. "Generation of a novel disease model mouse for mucopolysaccharidosis type VI via c. 252T> C human ARSB mutation knock-in." Biochemistry and Biophysics Reports 31 (2022): 101321. https://doi.org/10.1016/j.bbrep.2022.101321

Researchers successfully constructed a gene knock-in mouse model carrying the human ARSB Y85H mutation using CRISPR-Cas9 technology. This model exhibits pathological features similar to those of MPS VI patients, including facial abnormalities, mucopolysaccharide accumulation and short stature, providing an ideal tool for studying the relationship between this gene mutation and the severity of the disease.

3. Bhattacharyya, Sumit, et al. "Exogenous recombinant N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB) inhibits progression of B16F10 cutaneous melanomas and modulates cell signaling." Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease 1870.1 (2024): 166913. https://doi.org/10.1016/j.bbadis.2023.166913

The article indicates that in a mouse model of melanoma, exogenous ARSB treatment significantly inhibits tumor growth and prolongs survival by degrading chondroitin sulfate and affecting key signals such as Galectin-3 and SHP2. Studies have shown that ARSB has tumor suppressive functions.

4. Malekpour, Nasrin, Rahim Vakili, and Tayebeh Hamzehloie. "Mutational analysis of ARSB gene in mucopolysaccharidosis type VI: identification of three novel mutations in Iranian patients." Iranian Journal of Basic Medical Sciences 21.9 (2018): 950. https://doi.org/10.22038/IJBMS.2018.27742.6760

In this study, four homozygous mutations of the ARSB gene were identified in six MPS VI patients from Iran and Afghanistan. Among them, three (p.H178N, p.H242R, p.*534W) were novel mutations. All patients showed abnormal excretion of dermatil sulfate in urine and low activity of ARSB enzyme in white blood cells, confirming the association between gene mutation and enzyme deficiency.

5. Al Dhahouri, Nahid, et al. "Case Report: Reinterpretation and Reclassification of ARSB: p. Arg159Cys Variant Identified in an Emirati Patient With Hearing Loss Caused by a Pathogenic Variant in the CDH23 Gene." Frontiers in Pediatrics 9 (2022): 803732. https://doi.org/10.3389/fped.2021.803732

This study reports a suspected case of MPS VI, in which the patient carried the missense variant of ARSB:p.Arg159Cys and had a low activity of blood spot enzymes. However, subsequent biochemical and enzymatic analyses showed that both the GAGs level and the ARSB enzyme activity in fibroblasts were normal. Combined with the clinical manifestations, it was ultimately confirmed that this ARSB variation was benign and did not support the diagnosis of MPS VI.

Creative Biolabs: ARSB Antibodies for Research

Creative Biolabs specializes in the production of high-quality ARSB antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom ARSB Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our ARSB antibodies, custom preparations, or technical support, contact us at email.