Product Name: ALG6 Antibody
Species Reactivity: Human, Mouse, Rat
Tested Applications: ELISA, WB
Applications: ALG6 antibody can be used for detection of ALG6 by ELISA at 1:62500. ALG6 antibody can be used for detection of ALG6 by western blot at 1 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 – 100,000.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 58 kDa
Immunogen: Antibody produced in rabbits immunized with a synthetic peptide corresponding a region of human ALG6.
Host Species: Rabbit
Purification: Antibody is purified by peptide affinity chromatography method.
Physical State: Lyophilized
CAS NO.: 139504-50-0
Product: Mertansine
Buffer: Antibody is lyophilized in PBS buffer with 2% sucrose. Add 50 μL of distilled water. Final antibody concentration is 1 mg/mL.
Concentration: 1 mg/ml
Storage Conditions: For short periods of storage (days) store at 4˚C. For longer periods of storage, store ALG6 antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: ALG6, CDG1C
Accession NO.: NP_037471
Protein Ino: 38026892
Official Symbol: ALG6
Geneid: 29929
Background: ALG6 is a member of the ALG6/ALG8 glucosyltransferase family. It catalyzes the addition of the first glucose residue to the growing lipid-linked oligosaccharide precursor of N-linked glycosylation. Mutations in this gene encoding ALG6 are associated with congenital disorders of glycosylation type Ic.This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the first glucose residue to the growing lipid-linked oligosaccharide precursor of N-linked glycosylation. Mutations in this gene are associated with congenital disorders of glycosylation type Ic. 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.
PubMed ID:http://aac.asm.org/content/52/9/3180.abstract