Human Beta-Amyloid Precursor Protein (APP) Protein

Human Beta-Amyloid Precursor Protein (APP) Protein

Pida mas información

935106861

info@markelab.com

Precio

225€ (10 µg)

proveedor

Abbexa

reference

abx065296

Tested Applications

WB, SDS-PAGE

reactivity

status

RUO

clonality

Descripción

Recombinant Beta-Amyloid Precursor Protein (APP) is a recombinant Human protein produced in E. coli using Prokaryotic expression.

Background

Amyloid precursor protein (APP) is a highly conserved protein. Amyloid precursor-like protein 1 (APLP1) and amyloid precursor-like protein 2 (APLP2) are homologous of APP. APLP1 was the first identified homologue , while APLP2, was later recognized as another homologue of APP . These three proteins share significant sequence similarity and possess conserved domain structures. APLP1, a type I transmembrane protein, plays a crucial role in synaptic adhesion and synaptogenesis. Is actively involved in the formation of protein-protein complexes that serve as bridges between closely adjacent cells, facilitating cell-cell interactions and communication

Características del producto

category

Proteins and Peptides


origin

Human


host

E. coli


immunogen target

Beta-Amyloid Precursor Protein (APP)


host

E. coli


conjugation

Unconjugated


form

Lyophilized


tested applications

WB, SDS-PAGE


size 1

10 µg


size 2

50 µg


size 3

100 µg


size 4

200 µg


size 5

1 mg


expression

Recombinant


purity

> 90%


buffer

Prior to lyophilization: 20 mM Tris, 150 mM NaCl, pH 8.0, containing 1 mM EDTA, 1 mM DTT, 0.01% Sarcosyl, 5% Trehalose and Proclin-300.


storage

Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.


or code

APP


dry ice

No


availability

Shipped within 5-7 working days.


alias

AAA,AD1,PN2,ABPP,APPI,CVAP,ABETA,PN-II,preA4,CTFgamma,alpha-sAPP,Alzheimer disease amyloid protein


note

This product is for research use only. <p></p> Not for human consumption, cosmetic, therapeutic or diagnostic use.


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