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Amyloid beta 1-40 (Abeta 1-40) (Italian Mutant) Peptide

Abeta 1-40 Host: Synthetic Without preservative
Rockland
Catalog No. ABIN6699220
Supplier Product No.: 000-001-k99

Quick Overview for Amyloid beta 1-40 (Abeta 1-40) (Italian Mutant) Peptide (ABIN6699220)

Target

Abeta 1-40 (Amyloid beta 1-40 (Abeta 1-40))

Source

  • 17
Synthetic
  • Protein Region

    Italian Mutant

    Supplier Product No.

    000-001-k99

    Supplier

    Rockland

    Purpose

    Beta Amyloid 40, Italian Mutant

    Purity

    Greater than 95% specific peptide.
  • Application Notes

    Other: Control peptide should be used at 1.0 μg per 1.0 μL of antiserum per assay.

    Application_Note: Beta Amyloid 40, Italian Mutant Control Peptide is suitable for use in ELISA, Western Blot, Dot blot, PCA, and other assays. Control peptide should be used at 1.0 μg per 1.0 μL of antiserum in per assay. Specific conditions for reactivity should be optimized by the end user.

    Comment

    Control peptide should be used at 1.0 μg per 1.0 μl of antiserum per assay.

    Restrictions

    For Research Use only
  • Format

    Lyophilized

    Reconstitution

    Reconstitution_Buffer: Restore with deionized water (or equivalent)

    Reconstitution_Volume: 1.0 mL

    Concentration

    1.0 mg/mL

    Preservative

    Without preservative

    Storage

    4 °C,-20 °C

    Storage Comment

    Store vial at 2 - 8 ° C prior to opening. Aliquot contents and freeze at -20° C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. Dilute only prior to immediate use.

    Expiry Date

    12 months
  • Target

    Abeta 1-40 (Amyloid beta 1-40 (Abeta 1-40))

    Background

    Synonyms: ABPP, APP1, Alzheimer disease amyloid protein, Cerebral vascular amyloid peptide, Protease nexin-II, control peptide, blocking peptide

    Background: Amyloid peptides, derived from amyloid precursor protein (APP), are thought to play a role in the development of the senile plaques associated with Alzheimer's disease. The amyloid hypothesis presupposes that flaws in the processing of APP result in abnormally high levels of the longer, ""stickier"" forms of beta amyloid, known as Aβ42 and Aβ43, leading to aggregation of amyloid in the neuronal cell death and ultimately neuronal death. Mutations in the structure of Aβ40 and related peptides as well as in some of the enzymes involved in the processing of APP have been shown to alter the processing of APP. The sporadic (i.e., non-genetic) form of the disease, however, is far more common, caused by aging in concert with a number of both genetic and environmental risk factors.

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