Ugrás a tartalomra
Merck
Összes fotó(3)

Fontos dokumentumok

AB9234

Sigma-Aldrich

Anti-Amyloid Oligomer Antibody, αβ, oligomeric

serum, Chemicon®

Szinonimák:

Anti-oligomer

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biológiai forrás

rabbit

Minőségi szint

antitest forma

serum

antitest terméktípus

primary antibodies

klón

polyclonal

faj reaktivitás

rat, eukaryotes, mouse

faj reaktivitás (homológia által előrejelzett)

human

gyártó/kereskedő neve

Chemicon®

technika/technikák

ELISA: suitable
immunofluorescence: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunoprecipitation (IP): suitable
western blot: suitable

NCBI elérési szám

UniProt elérési szám

kiszállítva

dry ice

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... APP(351)

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

Recognizes amyloid oligomer. The antibody recognize all types of amyloid oligomers. The antibody appears to recognize a peptide backbone epitope that is common to amyloid oligomers, but is not found in native proteins, amyloidogenic monomer or mature amyloid fibrils. This antibody has been referred to as A11.

Immunogen

Epitope: Oligomeric

Alkalmazás

Anti-Amyloid Oligomer Antibody, αβ, oligomeric is an antibody against Amyloid Oligomer for use in ELISA, IF, IH, IH(P), IP & WB.
Immunohistochemistry:
A 1:1,000-1:10,000 concentration was used on a previous lot.

Immunoprecipitation:
A 1:1,000 concentration was used on a previous lot. Suggested cell lysis buffer is RIPA. Suggested capture agent is magnetic beads (Dynabeads). Known co-precipitatiing polypeptide: Amyloid beta, alpha synuclein oligomers.

ELISA (direct):
A previous lot of this antibody was used in ELISA.

Optimal working dilutions must be determined by the end user.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

Minőség

Evaluated by Western Blot on mouse brain lysates.

Western Blotting Analysis:
1:500 dilution of this antibody detected AMYLOID OLIGOMER on 10 μg of mouse brain lysates.

Fizikai forma

Rabbit Serum. Contains no preservative.
Unpurified

Tárolás és stabilitás

Stable for 1 year at -20ºC from date of receipt.

Analízis megjegyzés

Control
Brain

Egyéb megjegyzések

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Jogi információk

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Jogi nyilatkozat

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.

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Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


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.

Dokumentumtár megtekintése

Hugo M Botelho et al.
The Journal of biological chemistry, 287(50), 42233-42242 (2012-10-19)
S100A6 is a small EF-hand calcium- and zinc-binding protein involved in the regulation of cell proliferation and cytoskeletal dynamics. It is overexpressed in neurodegenerative disorders and a proposed marker for Amyotrophic Lateral Sclerosis (ALS). Following recent reports of amyloid formation
Sónia S Leal et al.
The Journal of biological chemistry, 288(35), 25219-25228 (2013-07-19)
Imbalance in metal ion homeostasis is a hallmark in neurodegenerative conditions involving protein deposition, and amyotrophic lateral sclerosis (ALS) is no exception. In particular, Ca(2+) dysregulation has been shown to correlate with superoxide dismutase-1 (SOD1) aggregation in a cellular model
Kaolin-induced chronic hydrocephalus accelerates amyloid deposition and vascular disease in transgenic rats expressing high levels of human APP.
Silverberg, GD; Miller, MC; Pascale, CL; Caralopoulos, IN; Agca, Y; Agca, C; Stopa, EG
Fluids and Barriers of the Cns null
Clustering and internalization of toxic amylin oligomers in pancreatic cells require plasma membrane cholesterol.
Trikha, S; Jeremic, AM
The Journal of Biological Chemistry null
Michael H Hayes et al.
Biology open, 5(6), 801-806 (2016-05-25)
A hallmark of Alzheimer's, Huntington's and similar diseases is the assembly of proteins into amyloids rather than folding into their native state. There is an increasing appreciation that amyloids, under specific conditions, may be non-pathogenic. Here we show that amyloids

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