Recombinant GNE antibody

Catalog No. ABIN7880878

The Rabbit Monoclonal anti-GNE antibody (Clone 29G96) (ABIN7880878) specifically detects GNE in WB, IF and ICC. The antibody is reactive with Human samples.

Quick Overview for Recombinant GNE antibody (ABIN7880878)

Target: GNE (Glucosamine (UDP-N-Acetyl)-2-Epimerase/N-Acetylmannosamine Kinase (GNE))

Antibody Type: Recombinant Antibody

Reactivity: Human

Host: Rabbit

Clonality: Monoclonal

Conjugate: This GNE antibody is un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF), Immunocytochemistry (ICC)

Clone: 29G96

Product Details anti-GNE Antibody

Purpose: GNE Antibody / Glucosamine 6 phosphate N acetyltransferase

Purification: Affinity-chromatography

Immunogen: A synthesized peptide derived from human GNE was used as the immunogen for the GNE antibody.

Isotype: IgG

Application Details

Application Notes: Optimal dilution of the GNE antibody should be determined by the researcher.

Restrictions: For Research Use only

Handling

Format: Liquid

Buffer: Rabbit IgG in phosphate buffered saline, pH 7.4, 150 mM NaCl, 0.02 % sodium azide and 50 % glycerol, 0.4-0.5 mg/mL BSA

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: -20 °C

Storage Comment: Store the GNE antibody at -20oC.

Target Details for GNE

Target: GNE (Glucosamine (UDP-N-Acetyl)-2-Epimerase/N-Acetylmannosamine Kinase (GNE))

Alternative Name: GNE

Background: GNE antibody is designed to detect glucosamine 6 phosphate N acetyltransferase, a bifunctional enzyme involved in sialic acid biosynthesis. The GNE protein contains two enzymatic activities, UDP N acetylglucosamine 2 epimerase and N acetylmannosamine kinase. Together, these activities catalyze the first committed steps in the biosynthesis of N acetylneuraminic acid, the most common form of sialic acid in mammals. Sialic acids are critical components of glycoproteins and glycolipids, influencing cell surface interactions, receptor function, and immune regulation.

GNE antibody is widely applied in metabolic, developmental, and neuromuscular research. Mutations in the GNE gene cause GNE myopathy, also known as hereditary inclusion body myopathy. This rare autosomal recessive disorder is characterized by progressive muscle weakness and degeneration. By using GNE antibody, researchers can investigate enzyme expression levels and localization to better understand the molecular basis of this disease.

The antibody is suitable for western blotting, immunohistochemistry, and immunofluorescence. In western blot assays, GNE antibody specifically recognizes the protein across tissue samples, confirming its role in metabolic pathways. Immunohistochemistry highlights expression in muscle and epithelial tissues, while immunofluorescence demonstrates cytoplasmic localization within cultured cells. These approaches provide valuable insight into how GNE supports cellular glycosylation and metabolic balance.

In addition to its relevance in genetic disorders, GNE is important in cancer biology and immunology. Altered sialylation patterns are a hallmark of many cancers, where increased sialic acid residues on tumor cells promote immune evasion and metastasis. By monitoring GNE expression with specific antibodies, scientists can explore how dysregulation of sialic acid biosynthesis contributes to malignant transformation. Similarly, in immunology, GNE activity influences immune recognition, inflammation, and infection responses.

Sialic acids play essential roles in development and signaling. Disruption of GNE function affects not only muscle tissue but also systemic processes, highlighting the importance of reliable antibodies for detection. Using GNE antibody, researchers can explore how this key enzyme contributes to glycosylation pathways and how alterations affect health and disease.

GNE antibody offered by NSJ Bioreagents provides a dependable reagent for studying sialic acid biosynthesis, hereditary myopathy, and glycosylation related disorders. Its proven specificity ensures accurate detection across multiple experimental methods, supporting both basic and translational research.

UniProt: Q9Y223