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Recombinant Human ADAM15 Protein, CF

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Immobilized RecombinantHuman ADAM15 (Catalog # 9234-AD)supports theadhesion of Jurkat human acute T cell leukemia cells. The ED50 for this effectis 0.5-3 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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Recombinant Human ADAM15 Protein, CF Summary

Details of Functionality
Measured by its ability of the immobilized protein to support the adhesion of Jurkat human acute T cell leukemia cells. The ED50 for this effect is 0.5-3 μg/mL
Source
Chinese Hamster Ovary cell line, CHO-derived human ADAM15 protein
Asp207-Ser693 with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Asp207
Protein/Peptide Type
Recombinant Enzymes
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
53 kDa.
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
67-79 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 MES and NaCl.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in water.

Notes

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

Alternate Names for Recombinant Human ADAM15 Protein, CF

  • ADAM 15
  • ADAM metallopeptidase domain 15
  • ADAM15
  • disintegrin-like, and cysteine-rich protein 15
  • EC 3.4.24
  • MDC15
  • MDC-15
  • Metargidin

Background

A disintegrin and metalloproteinase 15 (ADAM15), also known as MDC15 and Metargin, is an approximately 110 kDa transmembrane member of the M12B family of peptidases (1). Human ADAM15 is synthesized with a 189 amino acid (aa) propeptide that contains a cysteine switch motif. The 75 kDa activated form of human ADAM15 (after removal of the propeptide) consists of a 490 aa extracellular domain (ECD) with a peptidase, disintegrin, cysteine-rich, and EGF-like domain followed by a 21 aa transmembrane segment and a 146 aa cytoplasmic domain (2). Within the ECD, human ADAM15 shares 85% aa sequence identity with mouse and rat ADAM15. Alternative splicing generates multiple additional isoforms with various deletions or substitutions in the cytoplasmic domain, deletion in the propeptide and peptidase domains, or truncation at the beginning of the EGF-like domain (3, 4). ADAM15 is widely expressed, including on colonic epithelial cells, smooth muscle cells, vascular endothelial cells, and it is upregulated during chronic inflammation and tumor progression (5-8). It is also expressed on spermatocytes where both propeptide and the protease domain are cleaved during spermatocyte maturation (9, 10). ADAM15 promotes endothelial permeability, T cell adhesion, MMP-9 production and activation, and tumor cell metastasis (6, 8, 11, 12). It binds to Integrin  alpha V  beta 3 (13) and mediates the proteolytic shedding of cell surface
N-Cadherin, E-Cadherin, MICB, CD23/Fc epsilon  RII, and FGF R2 (IIb) (6, 7, 14-16).
  1. Edwards, D.R. et al. (2008) Mol. Aspects Med. 29:258.
  2. Kratzschmar, J. et al. (1996) J. Biol. Chem. 271:4593.
  3. Kleino, I. et al. (2009) J. Cell. Biochem. 108:877.
  4. Kleino, I. et al. (2007) BMC Mol. Biol. 8:90.
  5. Mosnier, J.F. et al. (2006) Lab. Invest. 86:1064.
  6. Najy, A.J. et al. (2008) Cancer Res. 68:1092.
  7. Duan, X. et al. (2013) Mol. Med. Rep. 7:991.
  8. Dong, D.D. et al. (2015) Oncol. Rep. 34:2451.
  9. Pasten-Hidalgo, K. et al. (2008) Reproduction 136:41.
  10. Pasten, K. et al. (2014) Reproduction 148:623.
  11. Sun, C. et al. (2010) Cardiovasc. Res. 87:348.
  12. Charrier, L. et al. (2007) J. Biol. Chem. 282:16948.
  13. Zhang, X.P. et al. (1998) J. Biol. Chem. 273:7345.
  14. Najy, A.J. et al. (2008) J. Biol. Chem. 283:18393.
  15. Fourie, A.M. et al. (2003) J. Biol. Chem. 278:30469.
  16. Maretzky, T. et al. (2009) Biochem. J. 420:105.

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