APP Human

Amyloid beta (A4) Precursor Protein Human Recombinant
Cat. No.
BT24843
Source
Escherichia Coli.
Synonyms
Amyloid beta A4 protein, ABPP, APPI, APP, Alzheimer disease amyloid protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II, APP, A4, AD1, AAA, PN2, ABETA, CTFgamma.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

APP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (18-289 a.a) and having a molecular mass of 34.7kDa (Molecular size on SDS-PAGE will appear higher).
APP is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Amyloid beta A4 protein (APP) is a multifunctional protein that acts as a cell surface receptor and a transmembrane precursor. It undergoes cleavage by secretases, resulting in various peptides. Some of these peptides are secreted and can interact with the acetyltransferase complex APBB1/TIP60 to enhance transcriptional activation. In contrast, other peptides aggregate to form amyloid plaques, a hallmark of Alzheimer's disease, in the brain. Mutations in the APP gene are linked to autosomal dominant Alzheimer's disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy).
Description
Recombinant Human APP, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 308 amino acids (18-289 a.a). It has a molecular mass of 34.7 kDa. Note: The molecular size observed on SDS-PAGE will be higher due to the presence of a 36 amino acid His-tag at the N-terminus. The protein is purified using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered colorless solution.
Formulation
The APP protein solution (0.5 mg/ml) is supplied in a buffer containing 20 mM Tris-HCl (pH 8.0), 20% glycerol, 0.1 M NaCl, and 1 mM DTT.
Stability
For short-term storage (up to 2-4 weeks), store the product at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Minimize repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 85.0% by SDS-PAGE analysis.
Synonyms
Amyloid beta A4 protein, ABPP, APPI, APP, Alzheimer disease amyloid protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II, APP, A4, AD1, AAA, PN2, ABETA, CTFgamma.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSLEVP TDGNAGLLAE PQIAMFCGRL NMHMNVQNGK WDSDPSGTKT CIDTKEGILQ YCQEVYPELQ ITNVVEANQP VTIQNWCKRG RKQCKTHPHF VIPYRCLVGE FVSDALLVPD KCKFLHQERM DVCETHLHWH TVAKETCSEK STNLHDYGML LPCGIDKFRG VEFVCCPLAE ESDNVDSADA EEDDSDVWWG GADTDYADGS EDKVVEVAEE EEVAEVEEEE ADDDEDDEDG DEVEEEAEEP YEEATERTTS IATTTTTTTE SVEEVVRE.

Product Science Overview

Introduction

Amyloid beta (A4) precursor protein (APP) is a transmembrane protein that plays a crucial role in the development and function of the nervous system. It is widely expressed in various tissues, with higher concentrations found in the brain . The human recombinant form of this protein is used extensively in research to understand its structure, function, and role in diseases, particularly Alzheimer’s disease.

Structure and Function

APP is a cell surface receptor that performs several physiological functions on the surface of neurons. These functions include neurite growth, neuronal adhesion, and axonogenesis . The protein undergoes sequential proteolytic processing by enzymes known as secretases, leading to the generation of amyloid-beta (Aβ) peptides of different lengths .

Proteolytic Processing

The proteolytic processing of APP involves two main pathways: the non-amyloidogenic pathway and the amyloidogenic pathway. In the non-amyloidogenic pathway, APP is cleaved by α-secretase, resulting in the release of a soluble APP fragment (sAPPα) and a membrane-bound C-terminal fragment (CTFα). This pathway precludes the formation of Aβ peptides.

In the amyloidogenic pathway, APP is first cleaved by β-secretase, producing a soluble APP fragment (sAPPβ) and a membrane-bound C-terminal fragment (CTFβ). The CTFβ is then further cleaved by γ-secretase, resulting in the release of Aβ peptides . These Aβ peptides can aggregate to form amyloid plaques, which are a hallmark of Alzheimer’s disease .

Role in Alzheimer’s Disease

Aβ peptides are the major component of amyloid plaques found in the brains of Alzheimer’s patients . The aggregation of these peptides is believed to play a central role in the pathogenesis of Alzheimer’s disease. Mutations in the APP gene have been implicated in autosomal dominant Alzheimer’s disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy) .

Research and Applications

Human recombinant APP is used in various research applications to study its structure, function, and role in disease. It is also used to develop therapeutic strategies aimed at modulating APP processing and reducing Aβ peptide formation. Understanding the mechanisms underlying APP processing and Aβ aggregation is crucial for developing effective treatments for Alzheimer’s disease.

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