Peptides and antibodies that inhibit integrin-ligand binding

Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – 25 or more amino acid residues in defined sequence

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

5303879, 530830, 53038822, 5303887, 5303882, 536 27, 435 691, 435 696, 4351723, 4352201, C07K 700, C07K 1528, C12N 1511, C12N 1500

Patent

active

051497808

ABSTRACT:
Polypeptides which are derived from the Arg-Gly-Asp (RGD) binding portion of an Integrin beta subunit are disclosed as are their use for modulation of Integrin ligand binding. Anti-antibody peptides, hybridomas secreting these antibodies, as well as methods of making any using such antibodies, and recombinant DNA molecules that define the structural gene coding for the polypeptides are also contemplated within the scope of the present invention.

REFERENCES:
Calvete et al., Abstract, (1991), Biochem. J. 274, 457-464.
Alberts et al., "Molecular Biology of the Cell", Garland Publishing, Inc., New York (1983).
Calvete et al. (1988), Tryptic Digestion of Human GPIIIa. Biochem. J. 250, 697-704.
Fitzgerald et al. (1987) Protein Sequence of Endothelial Glycoprotein IIIa Derived from a cDNA clone. J. Biol. Chem. 262, 3936-3939.

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Peptides and antibodies that inhibit integrin-ligand binding does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Peptides and antibodies that inhibit integrin-ligand binding, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Peptides and antibodies that inhibit integrin-ligand binding will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-1069079

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.