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PP69 β-Amyloid Peptide (1-42), Human

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PP69
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Overview

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PP69-.25MG
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      Glass bottle .25 mg
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      PP69-5MG
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          Plastic ampoule 5 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
          PP69-5MG 04055977227062

          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.