Recombinant Human ADAM28 Protein, CF

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Recombinant Human ADAM28 (Catalog #9325-AD) inducesadhesion of Jurkat human acute T cell leukemia cells. The ED50 for this effectis 0.2-1 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human ADAM28 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 0.2-1 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human ADAM28 protein
Leu72 & Leu191-Ala623, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Leu72 & Leu191
Protein/Peptide Type
Recombinant Enzymes
Purity
>70%, 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

Theoretical MW
49 & 62 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
59-80 kDa, reducing conditions
Reviewed Applications
Read 1 Review rated 5
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9325-AD in the following application:

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
>70%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 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 ADAM28 Protein, CF

  • a disintegrin and metalloproteinase domain 28
  • ADAM metallopeptidase domain 28
  • ADAM23MDC-L
  • ADAM28
  • disintegrin and metalloproteinase domain-containing protein 28
  • Dtgn1
  • EC 3.4.24
  • EC 3.4.24.-
  • eMDC II
  • eMDCII
  • Epididymial metalloproteinase-like, disintegrin-like, and cysteine-rich proteinII
  • MDCL
  • MDCLADAM 28
  • MDC-Lm
  • MDC-Ls
  • Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L
  • metalloproteinase-like, disintegrin-like, and cysteine-rich protein-L
  • Protein-L

Background

A distintegrin and metalloprotease domain-containing protein 28 (ADAM28), also known as MDC-L, is a member of the M12B peptidase family of enzymes. It is synthesized as an approximately 80-90 kDa glycosylated proprotein that is processed to a mature form later in the secretory pathway (1-3). After the removal of the propeptide that contains a cysteine switch motif, the activated form of ADAM28 consists of a 467 amino acid (aa) extracellular domain (ECD) which contains a peptidase, disintegrin, cysteine-rich and EGF-like domains, followed by a 21 aa transmembrane segment and an 89 aa cytoplasmic domain (3). Alternative splicing generates additional isoforms with a variety of substitutions and deletions in the cysteine-rich and EGF-like domains (1). Within the ECD, human ADAM28 shares 73% aa sequence identity with mouse and rat ADAM28 (3).  ADAM28 is a cell surface protein that is involved in a variety of cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis (4-6), and exhibits catalytic activity to insulin-like growth factor binding protein-3 (7). Like many members of the ADAM proteins, the disintegrin domain of ADAM28 interacts with integrin to influence cell adhesion and cell-cell interaction (8). ADAM28 can mediate the adhesion of the Jurkat cells, T-lymphoma cell line, through integrin alpha 4b1(9). 
  1. Roberts, C.M. et al. (1999) J. Biol. Chem. 274:29251.
  2. McGinn, O.J. et al. (2011) Cell Biol. Int. 35:1043.
  3. Howard, L. et al. (2000) Biochem. J. 348:21.
  4. Mochizuki, S. and Okada Y, (2007) Cancer Sci. 98:621.
  5. Schlondorff, J. et al. (1999) J. Cell Sci. 112:3603.
  6. Blobel, C.P. (1997) Cell 90:589.
  7. Mochizuki S. and Okada Y. (2009) Curr. Pharm. Des. 15:2349.
  8. Edwards, L. et al. (2008) Molecular Aspects of Medicine 29:258.
  9. Bridges, L. et al. (2002) J. Biol. Chem. 277:3784.

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Review for ADAM28 (9325-AD) (1) 51

Average Rating: 5
(Based on 1 review)

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