This is a synthetic peptide designed for use in combination with anti-GLA antibody (Catalog #: ARP54296_P050). It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications.
Each Investigator should determine their own optimal working dilution for specific applications.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Rekonstitution
Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
Konzentration
1 mg/mL
Buffer
Final peptide concentration is 1 mg/mL in PBS.
Handhabung
Avoid repeated freeze-thaw cycles.
Lagerung
-20 °C
Informationen zur Lagerung
For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
Target
GLA
(Galactosidase, alpha (GLA))
Hintergrund
GLA is a homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. This enzyme predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose. A variety of mutations in this gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease, a rare lysosomal storage disorder that results from a failure to catabolize alpha-D-galactosyl glycolipid moieties.This gene encodes a homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. This enzyme predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose. A variety of mutations in this gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease, a rare lysosomal storage disorder that results from a failure to catabolize alpha-D-galactosyl glycolipid moieties. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.