98% Purity Beta-Amyloid (1-42) Human for Pathology of Alzheimer CAS 107761-42

Details:

Quick Detail: 

Product Name: Beta-Amyloid (1-42), Ultra Pure, HFIP 
Sequence: Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala- Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala 
Storage: -20° 
Molecular Mass: 4514.1 4 
Peptide Purity: 98% 
Counter Ion: HFIP treated 
Supplied As: No salt, as HFIP desalts the sample. 
Recombinant. A DNA sequence encoding the human beta-amyloid (1-42)sequence was expressed in E. Coli. 

Description: 

Beta-amyloid peptide (Abeta), the major constituent of amyloid plaques in the brains of Alzheimer's patients, is thought to be the cause of Alzheimer's Disease (AD)1-3. AD is the most common neurodegenerative disease and afflicts about 10% of the population over 60 4. The abeta, HFIP is described in Stine, et. Al. 3. 
1) Yankner, BA, et. Al., (1990) Science, 250: 279-282 
2) Selkoe, D. J., (2001) Physiol. Rev, 81: 741-766 
3) Stine, W. B. Et. Al., (2003) J. Biol. Chem, 278: 11612-11622 
4) Frank, R. A., et. Al., (2003) Neurobiology of Aging, 24: 521-536 

HPLC REPORT: 
Product Name: Beta-Amyloid(1-42), HFIP 
Column: 4.6*250mm, SP-300-5-C4-BIO 
Solvent A: 0.1%Trifluoroacetic in 100% Acetonirile 
Solvent B: 0.1%Trifluoroacetic in 100% Water 
Flow rate: 1.0ml/min 
Wavelength: 220nm 

RankTimeNameConc. Area 
18.000 0.3194914 
29.959 1.07116490 
310.519 98.231514485 
411.018 0.27914298 
Total 1001540187 

Notes: 

This product is a chemically-modified β -amyloid (1-42) precursor, which belongs to GenScript's click peptides. The click peptides; Are best described by the following key features: 
1. Enhanced Stability— The O-acyl moiety within the click peptide is stable even under acidic pH. 
2. Convenient and quick process— The click peptides can be easily converted to native peptide at pH 7.4 or above. 
3. No by-product formation in the conversion process. 
4. Superior quality— After the click, the aggregative property of the peptides is significantly minimized compared to its native format