Recombinant Human ADAM23 Protein, CF Summary
Product Specifications
Ser60-His585 with a C-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
4974-AD
Formulation | Lyophilized from a 0.2 μm filtered solution in Tris and NaCl. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: ADAM23
ADAM23 (a disintegrin and metalloprotease domain 23; also MDC3) is a member of the M12B peptidase family of enzymes. It is synthesized as an approximately 100 kDa glycosylated proprotein that consists of a 227 amino acid (aa) propeptide, a 506 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 19 aa cytoplasmic domain (1, 2). The ECD contains a nonfunctional metalloprotease domain, an integrin‑binding disintegrin domain, and a cysteine‑rich region. Proteolytic removal of the propeptide generates an approximately 70 kDa mature protein (2). Within the propeptide, peptidase, and disintegrin domains (aa 60‑585), human ADAM23 shares 93% aa sequence identity with mouse and rat ADAM23. Alternative splicing of human ADAM23 yields additional isoforms (including a potentially secreted molecule) by substitution of the transmembrane and cytoplasmic regions (3). ADAM23 is expressed in the brain, notably on pyramidal cells of the cerebral cortex and hippocampus and on cerebellar Purkinje and granule cells (1, 2, 4‑6). ADAM23 binds the prion protein PrPC and the leucine‑rich glioma inactivated proteins LGI1 and LGI4 (7, 8). Its interaction with LGI1 promotes neurite outgrowth and dendrite arborization on pyramidal neurons (5). LGI1 appears to function as a trans‑synaptic bridge between ADAM23 and ADAM22 (6). In adipose tissue, the binding of ADAM23 to LGI3 inhibits adipocyte differentiation and lipid accumulation (9). ADAM23 is also expressed on bronchial epithelial cells (10). It serves as a counter‑receptor for Integrin alpha V beta 3 and can limit integrin activation and adhesion to alpha V beta 3 ligands (4, 11). ADAM23 expression is down‑regulated in some breast and non‑small cell lung carcinomas (10, 12).
- Sagane, K. et al. (1998) Biochem. J. 334:93.
- Goldsmith, A.P. et al. (2004) J. Neurosci. Res. 78:647.
- Sun, Y.P. et al. (2004) Gene 325:171.
- Cal, S. et al. (2000) Mol. Biol. Cell. 11:1457.
- Owuor, K. et al. (2009) Mol. Cell. Neurosci. 42:448.
- Fukata, Y. et al. (2010) Proc. Natl. Acad. Sci. USA 107:3799.
- Costa, M.D.M. et al. (2009) Neurosci. Lett. 461:16.
- Sagane, K. et al. (2008) Int. J. Biol. Sci. 4:387.
- Kim, H.A. et al. (2012) Biochim. Biophys. Acta 1821:914.
- Hu, C. et al. (2011) Int. J. Exp. Pathol. 92:333.
- Verbisck, N.V. et al. (2009) Cancer Res. 69:5546.
- Costa, F.F. et al. (2004) Oncogene 23:1481.
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