AB9890
Anti-AGE (Advanced Glycation End-products) Antibody
serum, Chemicon®
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
klón:
polyclonal
application:
ELISA
WB
WB
faj reaktivitás:
human
technika/technikák:
ELISA: suitable
western blot: suitable
western blot: suitable
citations:
11
Javasolt termékek
biológiai forrás
goat
Minőségi szint
antitest forma
serum
antitest terméktípus
primary antibodies
klón
polyclonal
faj reaktivitás
human
gyártó/kereskedő neve
Chemicon®
technika/technikák
ELISA: suitable
western blot: suitable
kiszállítva
wet ice
célzott transzláció utáni módosítás
unmodified
Egyediség
AGE (Advanced Glycation End-products)
Immunogén
Glycoaldehyde-modified protein.
Alkalmazás
Anti-AGE (Advanced Glycation End-products) Antibody detects level of AGE (Advanced Glycated End-products) & has been published & validated for use in ELISA & WB.
Research Category
Neuroscience
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Oxidative Stress
Neurodegenerative Diseases
Oxidative Stress
Western blot: ≥1:2,000 on AGE-modified proteins.
ELISA: ≥ 1:4,000 against Glycoaldehyde-modified BSA.
Optimal working dilutions must be determined by end user.
ELISA: ≥ 1:4,000 against Glycoaldehyde-modified BSA.
Optimal working dilutions must be determined by end user.
Fizikai forma
Goat antiserum. Liquid with 0.1% SODIUM AZIDE
Serum
Tárolás és stabilitás
Maintain at -20°C in undiluted aliquots for up to 12 months after date of receipt. Avoid repeated freeze/thaw cycles.
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.
Amit Garg et al.
ACS pharmacology & translational science, 6(2), 253-269 (2023-02-18)
Advanced glycation end-products (AGEs) form when glucose reacts non-enzymatically with proteins, leading to abnormal protein function, oxidative stress, and inflammation. AGEs are associated with aging and age-related diseases; their formation is aggravated during diabetes. Therefore, drugs preventing AGE formation can
Ali S Alqahtani et al.
Saudi journal of biological sciences, 28(1), 813-824 (2021-01-12)
Current pre-clinical evidences of Centella focus on its pharmacological effects on normal wound healing but there are limited studies on the bioactivity of Centella in cellular dysfunction associated with diabetic wounds. Hence we planned to examine the potential of Centella
Vassilis L Tzounakas et al.
Frontiers in medicine, 5, 16-16 (2018-02-21)
Transfusion of fresh frozen plasma (FFP) helps in maintaining the coagulation parameters in patients with acquired multiple coagulation factor deficiencies and severe bleeding. However, along with coagulation factors and procoagulant extracellular vesicles (EVs), numerous bioactive and probably donor-related factors (metabolites
Shweta Kishor Sonawane et al.
Oncotarget, 12(11), 1083-1099 (2021-06-05)
Alzheimer's disease is a type of dementia denoted by progressive neuronal death due to the accumulation of proteinaceous aggregates of Tau. Post-translational modifications like hyperphosphorylation, truncation, glycation, etc. play a pivotal role in Tau pathogenesis. Glycation of Tau aids in
Hugo Vicente Miranda et al.
Brain : a journal of neurology, 140(5), 1399-1419 (2017-04-12)
α-Synuclein misfolding and aggregation is a hallmark in Parkinson's disease and in several other neurodegenerative diseases known as synucleinopathies. The toxic properties of α-synuclein are conserved from yeast to man, but the precise underpinnings of the cellular pathologies associated are
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