GCS1 Polyklonale Antilichaam, FITC-vervoeging

Glycosylation of asparagine residues in Asn-X-Ser/Thr motifs in proteins commonly occur in the lumen of the endoplasmic reticulum (ER) . Glucosidase I catalyzes the first step in the N-linked oligosaccharide processing pathway. It specifically removes the distal alpha 1,2-linked glucose residue from the Glc3-Man9-GlcNAc2 oligosaccharide precursor. Glucosidase I contains a short cytosolic tail, a single pass transmembrane domain and a large C-terminal catalytic domain located on the luminal side of the ER. Mutations in the gene encoding Glucosidase I result in the congenital disorder glycosylation (CDG-IIb), which is characterized by generalized hypotonia, dysmorphic features, hepatomegaly, hypoventilation, feeding problems, seizures and death. Two point mutations in the Glucosidase I gene have been identified and result in amino acid substitutions, namely Arg486Thr and Phe652Leu, that affect polypeptide folding and active site formation.

EC 3.2.1.106; glucosidase I; Mannosyl oligosaccharide glucosidase; Mannosyl-oligosaccharide glucosidase; Mogs; MOGS_HUMAN; Processing A glucosidase I; Processing A-glucosidase I.

7841

Cytoplasm, Cell membrane

51-150/837

GCS1

FITC

KLH conjugated synthetic peptide derived from human GCS1

WB, IF (IHC-P), IF (IHC-F), IF (ICC)

Purified by Protein A.

494nm/518nm

1µg/µl

WB (1:300-5000), IF (IHC-P) (1:50-200), IF (IHC-F) (1:50-200), IF (ICC) (1:50-200)

Aqueous buffered solution containing 0.01M TBS (pH 7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Unmodified

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

7841

Human, Mouse, Rat, Dog