Application

Immunohistochemistry Analysis: A 1:5,000 dilution from a representative lot detected Semaphorin 3A in human cerebellum, human cerebral cortex, rat cerebral cortex, and rat kidney tissues.

Immunohistochemistry Analysis: A representative lot detected Semaphorin 3A in Immunohistochemistry applications (Rosenzweig, S., et. al. (2010). Graefes Arch Clin Exp Opthalmol. 248(10):1423-35).

Immunofluorescence Analysis: A representative lot detected Semaphorin 3A in Immunofluorescence applications (Nitzan, A., et. al. (2006). Glia. 54(6):545-56; Baranes, K., et. al. (2009). Exp Neurol. 218(1):24-32).

Western Blotting Analysis: A representative lot detected Semaphorin 3A in Western Blotting applications (Nitzan, A., et. al. (2006). Glia. 54(6):545-56; Rosenzweig, S., et. al. (2010). Graefes Arch Clin Exp Opthalmol. 248(10):1423-35).

Research CategoryNeuroscience

Anti-Semaphorin 3A Antibody, clone Sema-3A, Cat. No. MABN783, is a highly specific mouse monoclonal antibody that targets Semaphorin 3A and has been tested in Immunofluorescence, Immunohistochemistry (Paraffin), and Western Blotting.

Disclaimer

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.

General description

Semaphorin-3A (UniProt: Q90607, also known as Collapsin-1, COLL-1) is encoded by the SEMA3A (also known as COLL1) gene (gene ID: 395825) in chicken. Semaphorin-3A is a secreted protein that is synthesized with a 22 amino acid signal peptide. It is a member of a family of proteins that are involved in cell migration and axonal growth cone guidance. Semaphorin-3A has an Ig-like C2-type (immunoglobulin-like) domain, a PSI domain, and a Sema domain of 500 amino acids. It strongly binds to neuropilin via its carboxy third sequence and competes with semaphorin dimerization. It is expressed at relatively high levels in brain and muscle and at moderate levels in lung, bursa, and heart. It is not found in the liver. Semaphorin-3A can function as either a chemorepulsive agent, inhibiting axonal outgrowth, or as a chemoattractive agent, stimulating the growth of apical dendrites. It induces the collapse and paralysis of neuronal growth cones and could serve as a ligand that guides specific growth cones by a motility-inhibiting mechanism. Increased expression of Semaphorin-3A is associated with schizophrenia and it is seen in a variety of human tumor cell lines. Additionally, aberrant release of this protein is associated with the progression of Alzheimer′s disease. Semaphorin-3A is also reported to exert an osteoprotective effect by both suppressing osteoclastic bone resorption and increasing osteoblastic bone formation. The downregulation of Semaphorin-3A expression is shown to cause ischemia, degenerative diseases, and multiple sclerosis. (Ref.: Hayashi, M et al. (2012). Nature. 485(7396):69-74).

Immunogen

KLH-conjugated linear peptide corresponding to 18 amino acids from the N-terminal half of Chicken Semaphorin-3A.

Epitope: unknown

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Protein G purified

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Format: Purified

Quality

Evaluated by Western Blotting in HEK293 cell culture enriched with Semaphorin 3A.

Western Blotting Analysis: 0.01 µg/mL of this antibody detected Semaphorin 3A in 23 µL of enriched culture supernatant from HEK293 cells.

Specificity

Clone Sema-3A specifically targets Semaphorin 3A in multiple species. It targets a sequence of 18 amino acids within the N-terminal half of Semaphorin 3A.

Storage and Stability

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

Target description

~95 kDa observed; 88.87 kDa calculated. Uncharacterized bands may be observed in some lysate(s).