VAMP (Vesicle-Associated Membrane Protein)-Associated Protein B and C (VAPB) (Cytoplasmic Domain) antibody

Antigen: VAMP (Vesicle-Associated Membrane Protein)-Associated Protein B and C (VAPB)

Synonyms: ALS8, VAP-B, VAP-C, VAMP-B, VAMP-C

Binding Site: Cytoplasmic Domain

Clonality: Polyclonal

Host: Rabbit

Reactivity: Please enquire

Conjugate: Un-conjugated

Application: Immunohistochemistry (IHC), Western Blotting (WB)

Catalog no.: ABIN351367

Additional Information

Alternative name: Vesicle-associated membrane protein-associated protein B (VAMP-B)

UniProt: O95292

Immunogen: A synthetic peptide from a cytoplasmic part of Vesicle-associated membrane protein-associated protein B (VAMP-B) conjugated to an immunogenic carrier protein was used as the immunogen. The peptide is homologous in many species including human, rat, mouse, zebra fish, bovine, xenopus and chicken.

Format: Lyophilized

Description: FUNCTION: May play a role in vesicle trafficking. SUBUNIT: Homodimer, and heterodimer with VAPA. Interacts with VAMP1 and VAMP2. SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane protein. Intracytoplasmic membrane; Single-pass type IV membrane protein. Note: Present in the plasma membrane and in intracellular vesicles. TISSUE SPECIFICITY: Ubiquitous. Isoform 1 predominates. DISEASE: Defects in VAPB are the cause of amyotrophic lateral sclerosis type 8 (ALS8). ALS8 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms. DISEASE: Defects in VAPB are a cause of proximal adult autosomal dominant spinal muscular atrophy; also called late-onset spinal muscular atrophy Finkel type. Spinal muscular atrophies are neurodegenerative disorders characterized by degeneration of lower motor neurons, leading to progressive paralysis muscular atrophy. This form is a late- adult-onset form of the disease (after age 20 years). The patients show a benign course, most of them remaining ambulatory 10 to 40 years after clinical onset. Also known as: VAMP-associated protein B, VAMP-B, VAP-B, Vesicle-associated membrane protein-associated protein B/C, VAMP-associated protein B/C, VAMP-B/VAMP-C, VAP-B/VAP-C, VAPB.

Specificity: Appears to be specific for VAMP-B.

Application Details

Application Notes: IHC, WB. A dilution of 1 : 300 to 1 : 2000 is recommended. The optimal dilution should be determined by the end user. Not yet tested in other applications.

Purity: whole serum

Storage: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Restrictions: For Research Use only

Images

IHC on rat spinal cord using Rabbit antibody to a cytoplasmic part of Vesicle-associated membrane protein-associated protein B (VAMP-B): whole serum (ABIN351367) at 1 : 2000 dilution. Pre-absorption of the antibody with the immunising peptide completely abolishes the immunostaining (not shown).

IHC on rat spinal cord using Rabbit antibody to a cytoplasmic part of Vesicle-associated membrane protein-associated protein B (VAMP-B): whole serum (ABIN351367) at 1 : 2000 dilution. Pre-absorption of the antibody with the immunising peptide completely abolishes the immunostaining (not shown).

IHC on rat spinal cord using Rabbit antibody to a cytoplasmic part of Vesicle-associated membrane protein-associated protein B (VAMP-B): whole serum (ABIN351367) at 1 : 2000 dilution. Pre-absorption of the antibody with the immunising peptide completely abolishes the immunostaining (not shown).

Publications

Nishimura, Hayashi, Inada et al.: "Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins." in: Biochemical and biophysical research communications, Vol. 254, Issue 1, pp. 21-6, 1999 (PubMed).

Hu, Han, Song et al.: "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 97, Issue 17, pp. 9543-8, 2000 (PubMed).

Deloukas, Matthews, Ashurst et al.: "The DNA sequence and comparative analysis of human chromosome 20." in: Nature, Vol. 414, Issue 6866, pp. 865-71, 2002 (PubMed).

Gevaert, Goethals, Martens et al.: "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." in: Nature biotechnology, Vol. 21, Issue 5, pp. 566-9, 2003 (PubMed).

Clark, Gurney, Abaya et al.: "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." in: Genome research, Vol. 13, Issue 10, pp. 2265-70, 2003 (PubMed).

Nousiainen, Silljé, Sauer et al.: "Phosphoproteome analysis of the human mitotic spindle." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, Issue 14, pp. 5391-6, 2006 (PubMed).

Olsen, Blagoev, Gnad et al.: "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." in: Cell, Vol. 127, Issue 3, pp. 635-48, 2006 (PubMed).