Anti-VAPA Antibody, clone 7E10.1

Evaluated by Western Blotting in SH-SY5Y cell lysate.

Western Blotting Analysis: 0.2 µg/mL of this antibody detected VAPA in 10 µg of SH-SY5Y cell lysate.

Research Category
Neuroscience

Research Sub Category
Developmental Signaling

This Anti-VAPA Antibody, clone 7E10.1 is validated for use in Western Blotting, Immunohistochemistry (Paraffin) for the detection of VAPA.

Western Blotting Analysis: 0.2 µg/mL from a representative lot detected VAPA in 10 µg of mouse brain tissue lysate.
Immunohistochemistry Analysis: A 1:1,000 dilution from a representative lot detected VAPA in human cerebellum and human testis tissue.

Cross-reactivity to human VAPA spliced isoform 2 is highly expected, but not confirmed.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Vesicle-associated membrane protein-associated protein A (UniProt Q9P0L0; also known as 33 kDa VAMP-associated protein, hVAP-33, VAMP-A, VAMP-associated protein A, VAP-33, VAP-A) is encoded by the VAPA (also known as VAP33) gene (Gene ID 9218) in human. VAMP-associated proteins (VAPs) are type IV membrane proteins that are well conserved among species. There exist three human VAPs encoded by two genes, with VAPA encoding VAP-A and VAPB encoding VAP-B and VAP-C. VAPs generally localize at the endoplasmic reticulum (ER), although they are also reported to localize at other subcellular organelles in some species and cell types. VAP-A contains a major sperm protein (MSP) domain at the N-terminal, followed by a coiled-coil domain, and a transmembrane (TM) domain. VAPs were shown to have important roles in non-vesicular lipid transport, lipid metabolism, the regulation of ER structure, and the unfolded protein response through MSP domain-mediated interaction with FFAT motifs. Oxysterol-binding protein (OSBP) is a cytosolic receptor of cholesterol and oxysterols. OSBP is recruited to the ER by binding to the MSP domain of VAP-A, a process essential for the stimulation of sphingomyelin synthesis by 25-hydroxycholesterol.

~30 kDa observed. Uncharacterized band(s) may appear in some lysates.

Epitope: C-terminal half

GST-tagged recombinant protein corresponding to the C-terminal half of human VAPA.

Concentration: Please refer to lot specific datasheet.

Format: Purified

Protein G Purified

Purified mouse monoclonal IgG1κ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.