Detection of Human Iduronate 2‑Sulfatase/IDS by Western Blot.
Western blot shows lysates of human peripheral blood mononuclear cells (PBMCs). PVDF membrane was probed with 1 µg/mL of Goat Anti-Human Iduronate 2‑Sulfatase/IDS Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2449) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for Iduronate 2‑Sulfatase/IDS at approximately 42 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Iduronate 2-Sulfatase/IDS
As a member of the sulfatase family, IDS is required for the lysosomal degradation of the glycosaminoglycans (GAG) heparan sulfate and dermatan sulfate (2, 3). It hydrolyzes the 2‑sulfate group of the L-iduronate 2-sulfate units of the GAG. The IDS deficiency results in mucopolysaccharidosis II (MPS II or Hunter syndrome), an X-linked inborn error leading to lysosomal accumulation of the GAG and its excretion in urine. MPS II has a wide spectrum of clinical manifestations ranging from mild to severe. The deduced amino acid sequence of human IDS consists of a signal peptide (residues 1-25), a pro peptide (residues 26-33) and a mature chain (residues 34-550) that may be further processed into the 42 kDa chain (residues 34-455) and the 14 kDa chain (residues 456-550) (1). Recombinant human IDS corresponds to the single chain and has sulfatase activity described above.
Wilson, P.J. et al. (1990) Proc. Natl. Acad. Sci. USA 87:8531.
Parenti, G. et al. (1997) Curr. Opin. Genet. & Dev. 7:386.
Neufeld, E.F. and J. Muenzer (2001) in The Metabolic and Molecular Basis of Inherited Disease, Scriver, C.R. et al. (eds.) pp. 3421-3452, New York, McGraw-Hill.
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