AnaSpec Introduces Nine New Catalog Peptides

September 26, 2007 – San Jose, CA - Today AnaSpec, one of the world’s largest providers of custom and catalog peptides, introduced nine (9) new peptides for drug discovery research.

Rat Renin FRET Substrate (5-FAM/QXL™520) - Cat# 62334
This renin FRET peptide is a specific substrate for rat renin. Aspartyl protease cleaves angiotensinogen to yield angiotensin I; which is further converted to angiotensin II. The renin-angiotensin system is a coordinated hormonal cascade in the control of cardiovascular; renal; and adrenal function. It governs body fluid and electrolyte balance; as well as arterial pressure. Since an overactive renin-angiotensin system leads to hypertension; renin is an attractive target for the treatment of this disease. This renin peptide substrate may be used for screening renin inhibitors. In the FRET peptide; the fluorescence of 5-FAM is quenched by QXL™ 520. Upon cleavage into two separate fragments by rat renin; the fluorescence of 5-FAM is recovered; and can be monitored at excitation/emission = 490/520 nm. The SensoLyte™ 520 Renin Assay Kit (cat # 72040) contains the human renin FRET substrate.

Peptide Substrate for Renin 520 Assay kit - Cat# 61872-01
This FRET peptide is a specific substrate for renin. Aspartyl protease cleaves angiotensinogen to yield angiotensin I; which is further converted to angiotensin II. The renin-angiotensin system is a coordinated hormonal cascade in the control of cardiovascular; renal; and adrenal function. It governs body fluid and electrolyte balance; as well as arterial pressure. Since an overactive renin-angiotensin system leads to hypertension; renin is an attractive target for the treatment of this disease. This renin peptide substrate may be used for screening of renin inhibitors. In the FRET peptide; the fluorescence of 5-FAM is quenched by QXL™ 520. Upon cleavage into two separate fragments by renin; the fluorescence of 5-FAM is recovered; and can be monitored at excitation/emission = 490/520 nm. This substrate is employed in the SensoLyte™ 520 Renin Assay Kit; cat # 72040.

Rat Renin FRET Substrate (5-FAM/QXL™520) - Cat# 62334-01
This renin FRET peptide is a specific substrate for rat renin. Aspartyl protease cleaves angiotensinogen to yield angiotensin I; which is further converted to angiotensin II. The renin-angiotensin system is a coordinated hormonal cascade in the control of cardiovascular; renal; and adrenal function. It governs body fluid and electrolyte balance; as well as arterial pressure. Since an overactive renin-angiotensin system leads to hypertension; renin is an attractive target for the treatment of this disease. This renin peptide substrate may be used for screening renin inhibitors. In the FRET peptide; the fluorescence of 5-FAM is quenched by QXL™ 520. Upon cleavage into two separate fragments by rat renin; the fluorescence of 5-FAM is recovered; and can be monitored at excitation/emission = 490/520 nm. The SensoLyte™ 520 Renin Assay Kit (cat # 72040) contains the human renin FRET substrate.

[Glu1]-Fibrinopeptide B - Cat# 60501-1
Sequence: EGVNDNEEGFFSAR

Cyclo[-RGDyK(HiLyte Fluor™ 750)-] - Cat# 62333-1
Sequence: Cyclo[-RGDy-K(Hilyte Fluor 750)-]

Cyclo[-RGDyK(HiLyte Fluor™ 750)-] - Cat# 62333-01
Sequence: Cyclo[-RGDy-K(Hilyte Fluor 750)-]

Beta-Amyloid (1-42); Scrambled; 5-FAM labeled - Cat# 60892
Sequence: 5-FAM-AIAEGDSHVLKEGAYMEIFDVQGHVFGGKIFRVVDLGSHNVA

BPE-Conjugated-beta-Amyloid(1-40) - Cat# 60496
Sequence: B-Phycoerythrin-Conjugated-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV

MAPS; Core; 8-Branch - Cat# 21006
Sequence: K4K2KA-NH2

Company Info
AnaSpec, Inc. is a leading provider of integrated proteomics solutions to pharmaceutical, biotech, and academic research institutions throughout the world. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents, and combinatorial chemistry. Established in 1993, AnaSpec's headquarters and manufacturing facilities are located in San Jose, CA.

For more information visit www.anaspec.com