MABN2421
Anti-Beta (β)-Amyloid antibody
mouse monoclonal, Mhj7.4
Synonym(s):
Ab42, Amyloid peptide 1-42
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
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Product Name
Anti-Amyloid β 1-42 Antibody, clone mHJ7.4, clone mHJ7.4
biological source
mouse
Quality Level
antibody form
purified antibody
clone
mHJ7.4, monoclonal
mol wt
4.51 kDa (for Amyloid 1-42 peptide; 86.94 kDa calculated for Amyloid Precursor Protein.)
purified by
using protein G
species reactivity
human
isotype
IgG2bκ
accession no.
NP_000475
UniProt accession no.
General description
Amyloid-beta A4 protein (UniProt: P05067; also known as ABPP, APPI, APP, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II) is encoded by the APP (also known as A4, AD1) gene (Gene ID: 351) in human. Deposition of Aβ peptides is an early event in the pathogenesis of Alzheimer s disease (AD) that precedes the formation of Tau-positive paired helical filaments (PHFs) in NFTs. AD is also characterized by a progressive deposition of the Aβ peptide in senile plaques. Aβ peptides originate from the proteolytic cleavage of the amyloid precursor protein (APP).
Processing of APP occurs by two major pathways cleavage of APP by a-secretase is a non-amyloidogenic pathway and does not produce Aβ peptides. Cleavage of APP at the N-terminus of the Aβ region by β-secretase and at the C-terminus by g-secretase represents the amyloidogenic pathway. The β-secretase cleaves APP between residues Met671 and Asp672 and yields sAPPβ and C99. Following the β-secretase cleavage, a second cleavage occurs at the C-terminus of Aβ peptide that releases Aβ from C99. This cleavage occurs in the vicinity of residue 712 of the C-terminus. The g-secretase can cleave the C-terminal region at either Val711 or Ile713 to produce the shorter Aβ peptide (Aβ1-40) or the longer Aβ peptide (Aβ1-42), respectively.
The predominant form of Aβ found in the cerebrospinal fluid is the shorter Aβ1-40 peptide. Despite its lower rate of synthesis, Aβ1-42 is the peptide that is initially deposited within the extracellular plaques of AD patients. In addition, Aβ1-42 is more hydrophobic and aggregates at much lower concentration than the Aβ1-40 form. The abnormal accumulation of Aβ peptides can result in neuronal damage and loss by increasing free radical production and activation of inflammatory pathways by enhancing microglial secretion of inflammatory cytokines. Interaction between Aβ and ApoE3 or E4 is also an important determinant of amyloidosis. ApoE3 is shown to inhibit Aβ aggregation in vitro by decreasing Aβ multimers, whereas ApoE4 is reported to accelerate the rate of amyloid fibril formation.
Processing of APP occurs by two major pathways cleavage of APP by a-secretase is a non-amyloidogenic pathway and does not produce Aβ peptides. Cleavage of APP at the N-terminus of the Aβ region by β-secretase and at the C-terminus by g-secretase represents the amyloidogenic pathway. The β-secretase cleaves APP between residues Met671 and Asp672 and yields sAPPβ and C99. Following the β-secretase cleavage, a second cleavage occurs at the C-terminus of Aβ peptide that releases Aβ from C99. This cleavage occurs in the vicinity of residue 712 of the C-terminus. The g-secretase can cleave the C-terminal region at either Val711 or Ile713 to produce the shorter Aβ peptide (Aβ1-40) or the longer Aβ peptide (Aβ1-42), respectively.
The predominant form of Aβ found in the cerebrospinal fluid is the shorter Aβ1-40 peptide. Despite its lower rate of synthesis, Aβ1-42 is the peptide that is initially deposited within the extracellular plaques of AD patients. In addition, Aβ1-42 is more hydrophobic and aggregates at much lower concentration than the Aβ1-40 form. The abnormal accumulation of Aβ peptides can result in neuronal damage and loss by increasing free radical production and activation of inflammatory pathways by enhancing microglial secretion of inflammatory cytokines. Interaction between Aβ and ApoE3 or E4 is also an important determinant of amyloidosis. ApoE3 is shown to inhibit Aβ aggregation in vitro by decreasing Aβ multimers, whereas ApoE4 is reported to accelerate the rate of amyloid fibril formation.
Specificity
Clone mHJ7.4 is a mouse monoclonal antibody that detects Amyloid β 1-42 peptide. It targets an epitope within 6 amino acids from the C-terminal region of the peptide.
Immunogen
A linear peptide corresponding to six amino acids (37-42) from the C-terminal region of human Amyloid β1-42 peptide.
Application
ELISA Analysis: A representative lot detected Amyloid β 1-42 in ELISA applications
Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user
Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user
Quality
Evaluated by ELISA using human Amyloid β 1- 42 peptide.
Reconstitution
1.0 mg/mL. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.
Storage and Stability
Stable for 1 year at +2°C to +8°C from date of receipt.
Other Notes
Purified mouse monoclonal antibody IgG2b in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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