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171590 β-Amyloid Peptide (1-40, Gln¹¹), Human

171590
  
Purchase on Sigma-Aldrich

Přehled

Replacement Information
Description
Overview

This product has been discontinued.





β-Amyloid protein has both neurotrophic and neurotoxic effects depending upon the neuronal age and concentration of β-protein. A major component of senile and Alzheimer’s plaques. Promotes the down-regulation of Bcl-2 and enhances the phosphorylation of Tau protein.
Catalogue Number171590
Brand Family Calbiochem®
References
ReferencesChauhan, A., et al. 1998. J. Neurol. Sci. 154, 159.
Aksenov, M.Y., et al. 1996. J. Neurochem. 66, 2050.
Naiki, H., and Nakakuki, K. 1996. Lab Invest. 74, 374.
Paradis, E., et al. 1996. J. Neurosci. 16, 7533.
Terzi, E., et al. 1995. J. Mol. Biol. 252, 633.
Askenov, M.Y., et al. 1995. J. Neurochem. 65, 1899.
Klegeris, A., et al. 1994. Biochem. Biophys. Res. Commun. 199, 984.
Kowalska, M.A., and Badellino, K. 1994. Biochem. Biophys. Res. Commun. 205, 1829.
Yankner, B.A., et al. 1990. Science 250, 279.
Product Information
CAS number131438-79-4
FormWhite solid
FormulationSupplied as a trifluoroacetate salt.
Hill FormulaC₁₉₄H₂₉₆N₅₄O₅₇S
Chemical formulaC₁₉₄H₂₉₆N₅₄O₅₇S
Hygroscopic Hygroscopic
Applications
Biological Information
Purity≥95% by HPLC
Physicochemical Information
Peptide SequenceH-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Gln-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-OH
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage -20°C
Hygroscopic Hygroscopic
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution aliquot and freeze at-20°C. Stock solutions are stable for up to 2 weeks at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications

Documentation

β-Amyloid Peptide (1-40, Gln¹¹), Human Certificates of Analysis

TitleLot Number
171590

References

Přehled odkazů
Chauhan, A., et al. 1998. J. Neurol. Sci. 154, 159.
Aksenov, M.Y., et al. 1996. J. Neurochem. 66, 2050.
Naiki, H., and Nakakuki, K. 1996. Lab Invest. 74, 374.
Paradis, E., et al. 1996. J. Neurosci. 16, 7533.
Terzi, E., et al. 1995. J. Mol. Biol. 252, 633.
Askenov, M.Y., et al. 1995. J. Neurochem. 65, 1899.
Klegeris, A., et al. 1994. Biochem. Biophys. Res. Commun. 199, 984.
Kowalska, M.A., and Badellino, K. 1994. Biochem. Biophys. Res. Commun. 205, 1829.
Yankner, B.A., et al. 1990. Science 250, 279.

Brochure

Title
Alzheimer's Disease Brochure & Technical Guide
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision06-September-2007 RFH
Descriptionβ-Amyloid Peptide (Aβ) is the main constituent in both senile plaques and diffuse deposits in Alzheimer's diseased brains. Under appropriate conditions the soluble amyloid peptides aggregate into the fibrils associated with the disease state. It has been proposed that Aβ peptide may increase the sensitivity of neurons to oxidative damage by downregulating bcl-2 and/or inactivating glutamine synthetase.
FormWhite solid
FormulationSupplied as a trifluoroacetate salt.
CAS number131438-79-4
Chemical formulaC₁₉₄H₂₉₆N₅₄O₅₇S
Peptide SequenceH-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Gln-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-OH
Purity≥95% by HPLC
Solubility5% Acetic acid (2 mg/ml)
Storage -20°C
Hygroscopic
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution aliquot and freeze at-20°C. Stock solutions are stable for up to 2 weeks at -20°C.
Toxicity Standard Handling
ReferencesChauhan, A., et al. 1998. J. Neurol. Sci. 154, 159.
Aksenov, M.Y., et al. 1996. J. Neurochem. 66, 2050.
Naiki, H., and Nakakuki, K. 1996. Lab Invest. 74, 374.
Paradis, E., et al. 1996. J. Neurosci. 16, 7533.
Terzi, E., et al. 1995. J. Mol. Biol. 252, 633.
Askenov, M.Y., et al. 1995. J. Neurochem. 65, 1899.
Klegeris, A., et al. 1994. Biochem. Biophys. Res. Commun. 199, 984.
Kowalska, M.A., and Badellino, K. 1994. Biochem. Biophys. Res. Commun. 205, 1829.
Yankner, B.A., et al. 1990. Science 250, 279.