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171596 β-Amyloid Peptide (1-42), Rat

171596
Purchase on Sigma-Aldrich

Panoramica

Replacement Information

Products

Numero di catalogoConfezionamento Qtà/conf
171596-250UG Fiala di plastica 250 μg
Description
OverviewPredominant peptide found in the brain of patients with Alzheimer’s Disease and Down’s Syndrome. Promotes down-regulation of Bcl-2 and upregulation of Bax expression in neurons.
Catalogue Number171596
Brand Family Calbiochem®
SynonymsDAEFGHDSGFEVRHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
References
ReferencesParadis, E., et al. 1996. J. Neurosci. 16, 7533.
Roher, A.E., et al. 1996. J. Biol. Chem. 271, 20631.
Soto, C., and Castano, E.M. 1996. Biochem. J. 314, 701.
Murrell, J., et al. 1991. Science 254, 97.
Goldgaber, D., et al. 1987. Science 235, 877.
Kang, J., et al. 1987. Nature 325, 733.
Product Information
CAS number107761-42-2
FormLyophilized
FormulationSupplied as a trifluoroacetate salt.
Hill FormulaC₁₉₉H₃₀₇N₅₃O₅₉S
Chemical formulaC₁₉₉H₃₀₇N₅₃O₅₉S
Hygroscopic Hygroscopic
Quality LevelMQ100
Applications
Biological Information
Purity≥80% by HPLC
Physicochemical Information
Peptide SequenceH-Asp-Ala-Glu-Phe-Gly-His-Asp-Ser-Gly-Phe-Glu-Val-Arg-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-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 (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Numero di catalogo GTIN
171596-250UG 04055977207286

Documentation

β-Amyloid Peptide (1-42), Rat MSDS

Titolo

Scheda di sicurezza (MSDS) 

β-Amyloid Peptide (1-42), Rat Certificati d'Analisi

TitoloNumero di lotto
171596

Riferimenti bibliografici

Panoramica delle referenze
Paradis, E., et al. 1996. J. Neurosci. 16, 7533.
Roher, A.E., et al. 1996. J. Biol. Chem. 271, 20631.
Soto, C., and Castano, E.M. 1996. Biochem. J. 314, 701.
Murrell, J., et al. 1991. Science 254, 97.
Goldgaber, D., et al. 1987. Science 235, 877.
Kang, J., et al. 1987. Nature 325, 733.

Brochure

Titolo
Alzheimer's Disease Brochure & Technical Guide
Scheda tecnica

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.

Revision14-April-2008 RFH
SynonymsDAEFGHDSGFEVRHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
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 proposed that Aβ peptide may increase the sensitivity of neurons to oxidative damage by downregulating expression of bcl-2, a key anti-apoptotic protein and upregulating of bax expression, a protein known to induce cell death.
FormLyophilized
FormulationSupplied as a trifluoroacetate salt.
CAS number107761-42-2
Chemical formulaC₁₉₉H₃₀₇N₅₃O₅₉S
Peptide SequenceH-Asp-Ala-Glu-Phe-Gly-His-Asp-Ser-Gly-Phe-Glu-Val-Arg-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-OH
Purity≥80% by HPLC
Solubility5% Acetic Acid (1 mg/ml)
Storage -20°C
Hygroscopic
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Toxicity Standard Handling
ReferencesParadis, E., et al. 1996. J. Neurosci. 16, 7533.
Roher, A.E., et al. 1996. J. Biol. Chem. 271, 20631.
Soto, C., and Castano, E.M. 1996. Biochem. J. 314, 701.
Murrell, J., et al. 1991. Science 254, 97.
Goldgaber, D., et al. 1987. Science 235, 877.
Kang, J., et al. 1987. Nature 325, 733.