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Thermo Fisher Scientific BACE1 Polyclonal Antibody
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Thermo Fisher Scientific BACE1 Polyclonal Antibody

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Rabbit polyclonal antibody targeting human BACE1, validated for WB and ICC/IF. Detects ~70 kDa band in human brain lysate. Useful for Alzheimer’s disease research. Supplied as liquid, 1 mg/mL, store at -20°C.

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Thermo Fisher Scientific PA112529 BACE1 Polyclonal Antibody 100 ug pk판매 단위 pk ·
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Thermo Fisher Scientific · Thermo Fisher Scientific BACE1 Polyclonal Antibody

Applications and Tested Dilution

Application Tested Dilution
Western Blot (WB) 0.5–1 µg/mL
Immunocytochemistry (ICC/IF) 1:100

Product Specifications

Specification Description
Host / Isotype Rabbit / IgG
Class Polyclonal
Type Antibody
Immunogen Synthetic peptide corresponding to residues 485–501 of human BACE1
Conjugate Unconjugated
Form Liquid
Concentration 1 mg/mL
Storage Conditions -20°C, Avoid Freeze/Thaw Cycles
Shipping Conditions Wet ice
RRID AB_1070542

Product Specific Information

In Western blot, this antibody detects a ~70 kDa band in human brain lysate.

Target Information

BACE1 (beta-secretase) is a key enzyme involved in the production of amyloid beta-peptides (Abeta) found in extracellular amyloid plaques of Alzheimer’s disease (AD). In some cases, early-onset familial AD can be attributed to a “Swedish” mutation in the amyloid precursor protein (APP), which enhances cleavage by BACE1. This has led to therapeutic approaches focused on inhibiting BACE1 and other APP-cleaving enzymes such as gamma-secretase. APP is first cleaved by beta-secretase, producing a soluble derivative and a membrane-anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment is then processed by gamma-secretase to generate the 4 kDa amyloid-beta peptide, which accumulates in the brains of Alzheimer’s disease patients. BACE1, also known as beta-site APP cleaving enzyme or Asp2, is a transmembrane aspartic protease that colocalizes with APP.


For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

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