Abeta 1-40 Protein (His-GST)

Catalog No. ABIN7317787

This Recombinant Abeta 1-40 protein is produced in Escherichia coli (E. coli).

Quick Overview for Abeta 1-40 Protein (His-GST) (ABIN7317787)

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

Protein Type: Recombinant

Biological Activity: Active

Origin: Human

Source: Escherichia coli (E. coli)

Application: ELISA

Purity: > 92 % as determined by reducing SDS-PAGE.

Product Details

Purification tag / Conjugate: This Abeta 1-40 protein is labelled with His-GST.

Purpose: Recombinant Human Beta-amyloid 40/Beta-APP40 Protein (His&GST Tag)

Sequence: Asp 672-Val 711

Characteristics: A DNA sequence encoding the amino acids (Asp 672-Val 711) of human Amyloid beta A4 protein (APP770) (P05067-1), corresponding to the Beta-amyloid protein 40, was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

Sterility: 0.2 μm filtered

Biological Activity Comment: Measured by its ability to bind biotinylated recombinant human AGER in a functional ELISA.

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Restrictions: For Research Use only

Handling

Format: Lyophilized

Buffer: Lyophilized from sterile 50 mM Tris, 500 mM NaCl, pH 7.5
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 Details

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

Alternative Name: Beta-amyloid 40

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: 31.8 kDa

Observed MW: 33 kDa

Gene ID: 351

UniProt: P05067