|Description||Semaphorins are a large group of structurally related secreted, GPI-anchored and transmembrane cell signaling molecules. There are 8 major classifications (1-7) of Semaphorins characterized by the existence of a conserved 500 amino acid SEMA domain at the amino terminus. Classes 3,4,6, and 7 are found in vertebrates only, whilst class 5 is found in both vertebrates and invertebrates. Each class is then divided into additional subgroups based on shared structural characteristics. Semaphorins primarily function as axon growth cone guidance factors during neuronal development. Semaphorin 3A acts as a chemo-repellent to axons, and an inhibitor of the growth of axons by signaling through receptors, Neuropilin-1and Plexin-A. Recombinant human Semaphorin 3A is a 751 amino acid protein containing the SEMA domain, an immunoglobulin c2-like domain and a basic domain (Arg/Lys rich) near the C-terminus.|
|BiologicalActivity||Determined by its ability to bind recombinant rat Neuropilin-1 Fc Chimera in a functional ELISA assay.|
|Authenticity||Verified by N-terminal and Mass Spectrometry analyses (when applicable).|
|Endotoxin||Endotoxin level is <0.1 ng/ µg of protein (<1EU/ µg).|
|Protein Content||Verified by UV Spectroscopy and/or SDS-PAGE gel.|
|Precautions||Recombinant Human Semaphorin 3A is for research use only and not for use in diagnostic or therapeutic procedures.|
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