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PP69 β-Amyloid Peptide (1-42), Human

β-Amyloid Peptide (1-42), Human MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

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PP69
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PP69-.25MG
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      		 Glass bottle .25 mg
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      Description
      OverviewWild-type, human Aβ1-42 peptide. This product is supplied in a form that is not neurotoxic prior to a pre-incubation step. The level of toxicity has been shown to correlate to the extent of β sheet structure.
      Catalogue NumberPP69
      Brand Family Calbiochem®
      SynonymsDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
      References
      ReferencesCitron, M., et al. 1997. Nature Med. 3, 67.
      Hardy, J. 1997. Trends in Neurosci. 20, 154.
      Solomon, B., et al. 1997. Proc. Natl. Acad. Sci. USA 94, 4109.
      Duff, K., et al. 1996. Nature 383, 710.
      Iwatsubo, T., et al. 1994. Neuron 13, 45.
      Suzuki, N., et al. 1994. Science 264, 133.
      Simmons, L.K., et al. 1994. Mol. Pharmacol. 45, 373.
      Product Information
      FormLyophilized
      FormulationSupplied as a chloride salt.
      Hill FormulaC₂₀₃H₃₁₂N₅₆O₅₉S
      Chemical formulaC₂₀₃H₃₁₂N₅₆O₅₉S
      Hygroscopic Hygroscopic
      PreservativeNone
      RegionSynthetic peptide corresponding to amino acid residues 1 - 42 of the processed human β-amyloid peptide.
      Quality LevelMQ100
      Applications
      Key Applications Substrate Cleavage Assay
      Application NotesSubstrate Cleavage Assays (30-100 μg/ml)
      Application Comments
      Biological Information
      ImmunogenHuman
      Purity≥95% by HPLC
      Physicochemical Information
      Peptide SequenceH-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-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 InstructionsReconstitute just prior to use. Do not store following reconstitution, as aggregation may occur.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      PP69-.25MG 07790788059842

      Documentation

      β-Amyloid Peptide (1-42), Human SDS

      Title

      Safety Data Sheet (SDS) 

      β-Amyloid Peptide (1-42), Human Certificates of Analysis

      TitleLot Number
      PP69

      References

      Reference overview
      Citron, M., et al. 1997. Nature Med. 3, 67.
      Hardy, J. 1997. Trends in Neurosci. 20, 154.
      Solomon, B., et al. 1997. Proc. Natl. Acad. Sci. USA 94, 4109.
      Duff, K., et al. 1996. Nature 383, 710.
      Iwatsubo, T., et al. 1994. Neuron 13, 45.
      Suzuki, N., et al. 1994. Science 264, 133.
      Simmons, L.K., et al. 1994. Mol. Pharmacol. 45, 373.
      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.

      Revision26-October-2007 JSW
      SynonymsDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
      ApplicationSubstrate Cleavage Assays (30-100 μg/ml)
      DescriptionWild-type, human Aβ1-42 peptide. A number of mutations, identified in the gene encoding the β-amyloid precursor protein (βAPP), have been linked to early-onset Familial Alzheimer’s Disease. Mutations in the genes encoding presenilin 1 and presenilin 2 have also been shown to alter the processing of βAPP, resulting in increased extracellular concentration of β-amyloid peptide Aβ1-42(43) relative to Aβ1-40. Biophysical and biochemical experiments suggest that Aβ1-42(43) may serve as a catalyst for the aggregation and deposition of β-amyloid peptide (Aβ) leading to neurotoxic effects associated with senile plaque formation. Furthermore, antibodies recog-nizing Aβ1-42 revealed that the long form of the peptide is increased in presenilin and βAPP mutants, while other studies have used Aβ specific antibodies to prevent the in vitro fibrillar aggregation of Aβ. Amino acid sequence verified by amino acid analysis or sequencing. This product is supplied in a form that is not neurotoxic prior to a preincubation step. The appearance of toxicity has recently been shown to correlate to the extent of β sheet structure. Useful for neurotoxicity studies and substrate cleavage assays.
      Immunogen speciesHuman
      FormLyophilized
      FormulationSupplied as a chloride salt.
      Recommended reaction conditionsDissolve the lyophilized peptide at 1 mg/ml in 50 mM Tris-HCl, pH ≥9.0. Dilute peptide to an appropriate concentration with calcium, magnesium-free PBS and incubate at 37°C for 24-48 h prior to neurotoxicity studies. Suggested neurotoxic concentration is 30-100 µg/ml.
      Chemical formulaC₂₀₃H₃₁₂N₅₆O₅₉S
      Peptide SequenceH-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-OH
      Purity≥95% by HPLC
      Solubility50 mM Tris•HCl, pH >9.0 (≤1 mg/ml)
      PreservativeNone
      Comments
      Storage -20°C
      Hygroscopic
      Do Not Freeze Ok to freeze
      Special InstructionsReconstitute just prior to use. Do not store following reconstitution, as aggregation may occur.
      Toxicity Standard Handling
      ReferencesCitron, M., et al. 1997. Nature Med. 3, 67.
      Hardy, J. 1997. Trends in Neurosci. 20, 154.
      Solomon, B., et al. 1997. Proc. Natl. Acad. Sci. USA 94, 4109.
      Duff, K., et al. 1996. Nature 383, 710.
      Iwatsubo, T., et al. 1994. Neuron 13, 45.
      Suzuki, N., et al. 1994. Science 264, 133.
      Simmons, L.K., et al. 1994. Mol. Pharmacol. 45, 373.