• Purity

  >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by the ability of the immobilized protein to support the adhesion of BCE C/D‑1b bovine corneal endothelial cells. The ED    ₅₀ for this effect is 1.0‑4.0 μg/mL.

• Source

  Chinese Hamster Ovary cell line, CHO-derived Ser60-His585 with a C-terminal 10-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  Ser60 (pro) & Ala287 (mature)

• Predicted Molecular Mass

  60.8 kDa (pro) & 34.9 kDa (mature)

• SDS-PAGE

  40‑60 kDa, reducing conditions

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 PrP  ^C 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).

• References:

1. Sagane, K. et al. (1998) Biochem. J. 334:93.

2. Goldsmith, A.P. et al. (2004) J. Neurosci. Res. 78:647.

3. Sun, Y.P. et al. (2004) Gene 325:171.

4. Cal, S. et al. (2000) Mol. Biol. Cell. 11:1457.

5. Owuor, K. et al. (2009) Mol. Cell. Neurosci. 42:448.

6. Fukata, Y. et al. (2010) Proc. Natl. Acad. Sci. USA 107:3799.

7. Costa, M.D.M. et al. (2009) Neurosci. Lett. 461:16.

8. Sagane, K. et al. (2008) Int. J. Biol. Sci. 4:387.

9. Kim, H.A. et al. (2012) Biochim. Biophys. Acta 1821:914.

10. Hu, C. et al. (2011) Int. J. Exp. Pathol. 92:333.

11. Verbisck, N.V. et al. (2009) Cancer Res. 69:5546.

12. Costa, F.F. et al. (2004) Oncogene 23:1481.

• Long Name:

  A Disintegrin and Metalloproteinase Domain 23

• Entrez Gene IDs:

  8745 (Human); 23792 (Mouse); 301460 (Rat)

• Alternate Names:

  a disintegrin and metalloproteinase domain 23; ADAM metallopeptidase domain 23; ADAM23; disintegrin and metalloproteinase domain-containing protein 23; MDC3; MDC-3; MDC3ADAM 23; MDC-L; Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 3