Recombinant Human ADAM23 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human ADAM23 Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of BCE C/D‑1b bovine corneal endothelial cells. The ED50 for this effect is 1.0‑4.0 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human ADAM23 protein
Ser60-His585 with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Ser60 (pro) & Ala287 (mature)
Protein/Peptide Type
Recombinant Enzymes
Gene
ADAM23
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
60.8 kDa (pro) & 34.9 kDa (mature).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
40‑60 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris and NaCl.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human ADAM23 Protein, CF

  • 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

Background

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).
  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.

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Bioinformatics

Gene Symbol ADAM23
Uniprot