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Mouse Anti-ARSB Recombinant Antibody (1A4) (CBMAB-A0501-LY)

The product is antibody recognizes ARSB. The antibody 1A4 immunoassay techniques such as: WB, ELISA.
See all ARSB antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
1A4
Antibody Isotype
IgG1, κ
Application
WB, ELISA

Basic Information

Immunogen
ARSB (NP_942002, 166 a.a. ~ 265 a.a) partial recombinant protein with GST tag.
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4
Preservative
None
Concentration
Batch dependent
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
arylsulfatase B
Introduction
Arylsulfatase B encoded by this gene belongs to the sulfatase family. The arylsulfatase B homodimer hydrolyzes sulfate groups of N-Acetyl-D-galactosamine, chondriotin sulfate, and dermatan sulfate. The protein is targetted to the lysozyme. Mucopolysaccharidosis type VI is an autosomal recessive lysosomal storage disorder resulting from a deficiency of arylsulfatase B. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq]
Entrez Gene ID
411
UniProt ID
P15848
Alternative Names
ASB; G4S; MPS6
Function
Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (PubMed:19306108).
Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (PubMed:19306108).
In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (By similarity).
Biological Process
Autophagy Source: Ensembl
Central nervous system development Source: Ensembl
Chondroitin sulfate catabolic process Source: Reactome
Colon epithelial cell migration Source: UniProtKB
Lysosomal transport Source: ProtInc
Lysosome organization Source: ProtInc
Neutrophil degranulation Source: Reactome
Positive regulation of neuron projection development Source: UniProtKB
Regulation of epithelial cell migration Source: UniProtKB
Response to estrogen Source: Ensembl
Response to methylmercury Source: Ensembl
Response to nutrient Source: Ensembl
Response to pH Source: Ensembl
Cellular Location
Lysosome; Cell surface
Involvement in disease
Mucopolysaccharidosis 6 (MPS6): An autosomal recessive lysosomal storage disease characterized by intracellular accumulation of dermatan sulfate. Clinical features can include abnormal growth, short stature, stiff joints, skeletal malformations, corneal clouding, hepatosplenomegaly, and cardiac abnormalities. A wide variation in clinical severity is observed.
Multiple sulfatase deficiency (MSD): The protein represented in this entry is involved in disease pathogenesis. Arylsulfatase B activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1. SUMF1 mutations result in defective post-translational modification of ARSB at residue Cys-91 that is not converted to 3-oxoalanine. A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay.
PTM
The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification is severely defective in multiple sulfatase deficiency (MSD).

Bhattacharyya, S., Feferman, L., Han, X., Xia, K., Zhang, F., Linhardt, R. J., & Tobacman, J. K. (2020). Increased CHST15 follows decline in arylsulfatase B (ARSB) and disinhibition of non-canonical WNT signaling: potential impact on epithelial and mesenchymal identity. Oncotarget, 11(24), 2327.

Hendrickx, G., Danyukova, T., Baranowsky, A., Rolvien, T., Angermann, A., Schweizer, M., ... & Schinke, T. (2020). Enzyme replacement therapy in mice lacking arylsulfatase B targets bone-remodeling cells, but not chondrocytes. Human molecular genetics, 29(5), 803-816.

Tobacman, J. K., Bhattacharyya, S., & Feferman, L. (2020). Increased CHST15 expression follows declines in Arylsulfatase B (ARSB) and DKK3 and disinhibition of non-canonical WNT signaling.

Aminzadeh, M., Malekpour, N., & Ghandil, P. (2019). Identification of arylsulfatase B gene mutations and clinical presentations of Iranian patients with Mucopolysaccharidosis VI. Gene, 706, 1-5.

Bhattacharyya, S., Feferman, L., & Tobacman, J. K. (2019). Dihydrotestosterone inhibits arylsulfatase B and Dickkopf Wnt signaling pathway inhibitor (DKK)‐3 leading to enhanced Wnt signaling in prostate epithelium in response to stromal Wnt3A. The Prostate, 79(7), 689-700.

Pohl, S., Angermann, A., Jeschke, A., Hendrickx, G., Yorgan, T. A., Makrypidi‐Fraune, G., ... & Schinke, T. (2018). The lysosomal protein arylsulfatase B is a key enzyme involved in skeletal turnover. Journal of Bone and Mineral Research, 33(12), 2186-2201.

Bhattacharyya, S., Feferman, L., Han, X., Ouyang, Y., Zhang, F., Linhardt, R. J., & Tobacman, J. K. (2018). Decline in arylsulfatase B expression increases EGFR expression by inhibiting the protein-tyrosine phosphatase SHP2 and activating JNK in prostate cells. Journal of Biological Chemistry, 293(28), 11076-11087.

Essawi, M. L., Elbagoury, N. M., Sayed, O. M., Aglan, M. S., Ibrahim, M. M., Soliman, H. N., & Fateen, E. M. (2018). Mutation analysis of the arylsulfatase B gene among Egyptian patients with Maroteaux–Lamy disorder. Middle East Journal of Medical Genetics, 7(2), 96.

Zhang, J., Liang, H., Zhu, L., Gan, W., Tang, C., Li, J., & Xu, R. (2018). Expression and distribution of Arylsulfatase B are closely associated with neuron death in SOD1 G93A transgenic mice. Molecular neurobiology, 55(2), 1323-1337.

Bhattacharyya, S., Feferman, L., Terai, K., Dudek, A. Z., & Tobacman, J. K. (2017). Decline in arylsulfatase B leads to increased invasiveness of melanoma cells. Oncotarget, 8(3), 4169.

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For research use only. Not intended for any clinical use.

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