Rabbit Anti-beta Amyloid 1-42 Polyclonal Antibody #abs119700

abs119700-50ul

In Stock

201

abs119700-100ul

In Stock

301

Other names

Beta Amyloid (1-42), also known as beta Amyloid 1-42 or beta-Amyloid 1-42, is a protein implicated in Alzheimer's Disease. It is also referred to as P3(42), A4, AAA, ABETA, ABPP, AD1, or Alzheimers Disease Amyloid Protein. Another name for it is Amyloid B or Amyloid Beta A4 Protein Precursor. This protein, commonly found in the brains of individuals with Alzheimer's Disease, is associated with the formation of amyloid plaques. These plaques are a hallmark characteristic of Alzheimer's and contribute to the degeneration of brain cells. The protein is derived from the Amyloid Beta precursor protein (APP), also known as APPI or Beta APP. It is produced through the proteolytic cleavage of APP by various enzymes. Other names for the protein include Cerebral Vascular Amyloid Peptide, CTFgamma, CVAP, PN II, PN2, PreA4, or Protease nexin II. Its official gene symbol is A beta, and in humans, it is coded by the A4_HUMAN gene. Understanding the role of Beta-amyloid protein 42 is crucial in unraveling the mechanisms behind Alzheimer's Disease pathology.

Source

Rabbit

Specificity

beta Amyloid 1-42

Species Reactivity

Human;Mouse;Rat;Chicken;Dog;Pig;Cow;Rabbit;

Application

The suggested dilutions for ELISA are 1:500-1000, for IHC-P are 1:400-800, for IHC-F are 1:400-800, for Flow-Cyt are 1μg/Test, for ICC are 1:100-500, and for IF are 1:100-500 (Antigen retrieval is required for paraffin section). Please note that the rearrangement of the original content is as follows but with a different viewpoint:
For ELISA, it is recommended to use dilutions of 1:500-1000. In the case of IHC-P and IHC-F, the suggested dilutions are 1:400-800. For Flow-Cyt, 1μg of the sample per test is ideal. In the case of ICC and IF, dilutions of 1:100-500 are suitable, but please remember that antigen retrieval is necessary for paraffin section.

Immunogen

A synthetic peptide of human beta-Amyloid: 1-42/42 has been conjugated with KLH. To create content that is highly similar to this original text, the following rephrased version can be generated: KLH has been combined with a synthetic peptide of human beta-Amyloid: 1-42/42.

Properties

Concentration

1mg/ml

Purification

affinity purified by Protein A

Clonality

Polyclonal Antibody

Isotype

IgG

Stability & Storage

To ensure optimal storage conditions, it is recommended to keep the product at a temperature of -20 °C for a duration of one year. It is important to note that repeated freeze/thaw cycles should be avoided at all costs. Taking these precautions will help maintain the product's integrity and efficacy over time.

Storage buffer

TBS (pH 7.4) with 0.01M concentration is supplemented with 1% Bovine Serum Albumin (BSA), 0.03% Proclin300, and 50% Glycerol.

Research area

Alzheimer's disease is a neurological disorder that affects millions of people worldwide. It is characterized by the gradual deterioration of brain cells, leading to memory loss, confusion, and other cognitive impairments. In order to understand the mechanisms behind this disease, scientists have turned to the fields of cell biology, immunology, and neurobiology.
Cell biology is the study of how cells function at the molecular level. Researchers who study Alzheimer's disease in this field focus on the structure and function of brain cells and how they are affected by the disease. They investigate how the accumulation of beta-amyloid protein plaques and neurofibrillary tangles within brain cells contribute to cell death and cognitive decline.
Immunology is the study of the immune system, which plays a critical role in protecting the body from infections and other diseases. Researchers studying Alzheimer's disease in this field investigate how immune cells in the brain, called microglia, respond to the accumulation of beta-amyloid plaques. They also explore how inflammation in the brain can contribute to the progression of the disease.
Neurobiology is the study of the nervous system and how it controls and regulates behavior and cognition. Researchers studying Alzheimer's disease in this field investigate how the degeneration of brain cells in certain regions of the brain contributes to cognitive decline. They also explore how neurotransmitters, such as acetylcholine, are affected in Alzheimer's disease and how this may contribute to the cognitive symptoms of the disease.
Together, these fields of research provide a comprehensive understanding of Alzheimer's disease and the mechanisms that underlie its progression. By investigating the complex interplay between cell biology, immunology, and neurobiology, scientists hope to develop new treatments and interventions for this devastating disease.

Target

Background

Alzheimer's disease is characterized by the presence of cerebral and vascular plaques composed mainly of Amyloid beta peptides. These peptides are derived from the cleavage of the Amyloid precursor protein and can range from 39 to 43 amino acids in length. Specifically, beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are formed after cleavage occurs at residues 40, 42, and 43 during the last processing step of the Amyloid precursor protein by gamma-secretase.
The accumulation of beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides is closely linked to the formation of plaques and tangles in Alzheimer's disease. To better understand the biology of this disease, researchers have developed beta Amyloid antibodies and peptides as useful tools.
To summarize, the involvement of Amyloid beta peptides in the pathology of Alzheimer's disease is significant, and beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles associated with this devastating illness. The use of beta Amyloid antibodies and peptides is an important avenue of investigation for further understanding this disease and potentially developing effective treatments.

Celluar localization

Cytoplasm cell membrane extracellular matrix

UniPort

P05067