AB2287
Anti-Amyloid Fibrils LOC Antibody
serum, Chemicon®
Szinonimák:
Amyloid Fibrils, Amyloid Fibrils LOC
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Javasolt termékek
biológiai forrás
rabbit
Minőségi szint
antitest forma
serum
antitest terméktípus
primary antibodies
klón
polyclonal
faj reaktivitás
human
faj reaktivitás (homológia által előrejelzett)
mouse, rat
gyártó/kereskedő neve
Chemicon®
technika/technikák
ELISA: suitable
dot blot: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
izotípus
IgG
NCBI elérési szám
UniProt elérési szám
kiszállítva
wet ice
célzott transzláció utáni módosítás
unmodified
Géninformáció
human ... APP(351)
mouse ... App(11820)
Általános leírás
Amyloid monomeric proteins can sometimes oligomerize into destructive amyloid fibrils. Amyloidogenic conformations of non-disease related proteins can be created by partial protein misfolding or denaturation. In disease state oligomerization, extensive amyloid oligomerization creates plaques in neural tissue that correlates with Alzheimer’s symptomology.
Egyediség
This antibody recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not monomers, prefibrillar oligomers or natively folded proteins.
Immunogen
Fibrils prepared from human islet amyloid polypeptide.
Alkalmazás
Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in fibrils and monomers but not in prefibril oligos. A 1:5,000 dilution, as cited in Glabe C., et al. (2007) Mol Neurodegener 2, 18 shows that the binding with monomers is likely non-specific, and is a possible result of high primary antibody concentration.
This Anti-Amyloid Fibrils LOC Antibody is validated for use in IP, IC, IH, ELISA, WB, DB for the detection of Amyloid Fibrils LOC.
Minőség
Evaluated by Dot Blot in monomers, prefibril oligos, and fibrils.
Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in fibrils and monomers but not in prefibril oligos. A 1:5,000 dilution, as cited in Glabe C., et al. (2007) Mol Neurodegener 2, 18 shows that the binding with monomers is likely non-specific, and is a possible result of high primary antibody concentration.
Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in fibrils and monomers but not in prefibril oligos. A 1:5,000 dilution, as cited in Glabe C., et al. (2007) Mol Neurodegener 2, 18 shows that the binding with monomers is likely non-specific, and is a possible result of high primary antibody concentration.
Tárolás és stabilitás
Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. After thawing, store at 4°C in 0.02% sodium azide.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. After thawing, store at 4°C in 0.02% sodium azide.
Jogi információk
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Tárolási osztály kódja
10 - Combustible liquids
WGK
WGK 1
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.
Elin K Esbjörner et al.
Chemistry & biology, 21(6), 732-742 (2014-05-27)
Insight into how amyloid β (Aβ) aggregation occurs in vivo is vital for understanding the molecular pathways that underlie Alzheimer's disease and requires new techniques that provide detailed kinetic and mechanistic information. Using noninvasive fluorescence lifetime recordings, we imaged the formation
Sahil Chandhok et al.
Scientific reports, 13(1), 14471-14471 (2023-09-03)
The formation of protein aggregates is a hallmark of many neurodegenerative diseases and systemic amyloidoses. These disorders are associated with the fibrillation of a variety of proteins/peptides, which ultimately leads to cell toxicity and tissue damage. Understanding how amyloid aggregation
Thomas Filip et al.
Alzheimer's research & therapy, 13(1), 175-175 (2021-10-18)
To better understand the etiology and pathomechanisms of Alzheimer's disease, several transgenic animal models that overexpress human tau or human amyloid-beta (Aβ) have been developed. In the present study, we generated a novel transgenic rat model by cross-breeding amyloid precursor
Juan Jose Ramos-Rodriguez et al.
Molecular neurobiology, 54(5), 3428-3438 (2016-05-15)
Age remains the main risk factor for developing Alzheimer's disease (AD) although certain metabolic alterations, including prediabetes and type 2 diabetes (T2D), may also increase this risk. In order to understand this relationship, we have studied an AD-prediabetes mouse model
Deanna Price et al.
Biochemistry, 59(21), 1981-2002 (2020-05-10)
It is known that the humanin (HN) peptide binding to amyloid-β (Aβ) protects against its cytotoxic effects, while acetylcholinesterase (AChE) binding to Aβ increases its aggregation and cytotoxicity. HN is also known to bind the insulin-like growth factor binding protein-3
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