|Application ||WB, IF, ICC, E|
|Other Accession||NP_000207, 119395746|
|Calculated MW||76112 Da|
|Application Notes||Anosmin antibody can be used for detection of Anosmin by Western blot at 1 µg/mL. Antibody can also be used for immunocytochemistry starting at 5 µg/mL. For immunofluorescence start at 20 µg/mL.|
|Reconstitution & Storage||Anosmin antibody can be stored at 4 ℃, stable for one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||Anosmin Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Has a dual branch-promoting and guidance activity, which may play an important role in the patterning of mitral and tufted cell collaterals to the olfactory cortex (By similarity). Chemoattractant for fetal olfactory epithelial cells.|
|Cellular Location||Cell membrane; Peripheral membrane protein. Secreted. Note=Proteolytic cleavage may release it from the cell surface into the extracellular space|
|Tissue Location||Expressed in the cerebellum (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
Anosmin Antibody: Mutations in Anosmin-1, an extracellular matrix-associated glycosylated protein, have been linked with Kallmann Syndrome (KS), an X-linked genetic disorder characterized by loss of smell caused by abnormal olfactory bulb development and delayed puberty caused by disrupted migration of the gonadotropin-releasing hormone neuron. Anosmin-1 has been shown to directly bind FGFR1 via its N-terminal cysteine-rich domain, whey-acidic protein-like domain, and its first FnIII repeat with the D2 and D3 ectodomains of FGFR1. It is thought that Anosmin-1 can modulate FGFR1 signaling and have opposing effects on the formation and activation of FGF2-FGFR1-heparing complex.
Franco B, Guioli S, Pragliola A, et al. A gene deleted in Kallmann’s syndrome shares homology with neural cell adhesion and axonal path-finding molecules. Nature 1991; 353:529-36.
Soussi-Yanicostas N, Hardelin JP, Arroyo-Jimenez MM, et al. Initial characterization of anosmin-1, a putative extracellular matrix protein synthesized by definite neuronal cell populations in the central nervous system. J. Cell Sci. 1996; 109:1749-57.
Hu Y, Guimond SE, Travers P, et al. Novel mechanisms of fibroblast growth factor receptor 1 regulation by extracellular matrix protein Anosmin-1. J. Biol. Chem. 2009; 284:29905-20
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