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Abeta 1-42 Protein (AA 672-713) (His-GST)

This Recombinant Abeta 1-42 protein is expressed in Escherichia coli (E. coli).
Catalog No. ABIN7317786
$1,029.34
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100 μg
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Quick Overview for Abeta 1-42 Protein (AA 672-713) (His-GST) (ABIN7317786)

Target

Abeta 1-42 (Amyloid beta 1-42 (Abeta 1-42))

Protein Type

Recombinant

Origin

Human

Source

  • 1
Escherichia coli (E. coli)

Purity

> 80 % as determined by reducing SDS-PAGE.
  • Protein Characteristics

    AA 672-713

    Purification tag / Conjugate

    This Abeta 1-42 protein is labelled with His-GST.

    Purpose

    Recombinant Human Beta-amyloid 42/Beta-APP42 Protein (His & GST Tag)

    Sequence

    Asp672-Ala713

    Characteristics

    A DNA sequence encoding the amino acids (Asp672-Ala713) of human Amyloid beta A4 protein (APP770) (P05067-1), corresponding to the Beta-amyloid protein 42, was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

    Sterility

    0.2 μm filtered

    Biological Activity Comment

    Not validated for activity
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  • Restrictions

    For Research Use only
  • Format

    Lyophilized

    Buffer

    Lyophilized from sterile PBS, 10 % glycerol, pH 7.4
    Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween 80 are added as protectants before lyophilization.

    Storage

    4 °C,-20 °C,-80 °C

    Storage Comment

    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

    Expiry Date

    12 months
  • Target

    Abeta 1-42 (Amyloid beta 1-42 (Abeta 1-42))

    Alternative Name

    Beta-amyloid 42

    Background

    AAA,ABETA,ABPP,AD1,APPI,CTFgamma,CVAP,PN-II,PN2,Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer's disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies.

    Molecular Weight

    Calculated MW: 32.4 kDa

    Observed MW: 34 kDa

    Gene ID

    351

    UniProt

    P05067
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