HT60
Amyloid Stain, Congo Red
Synonym(s):
Puchtler’s Modification for Amyloid
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About This Item
NACRES:
NA.47
UNSPSC Code:
41116121
shelf life
Expiry date on the label.
IVD
for in vitro diagnostic use
dilution
(for histology)
application(s)
hematology
histology
storage temp.
room temp
Quality Level
Biochem/physiol Actions
Amyloid protein is detected in tissue with Congo red, a metachromatic stain. Staining is intensified by pretreatment of tissue with alkaline sodium chloride.
Kit Components Only
Product No.
Description
- Congo Red Solution (kit only) 500 mL
- Sodium Chloride Solution, Alcoholic (kit only) 500 mL
- Sodium Hydroxide Solution (kit only) 2 x 12
signalword
Danger
hcodes
Hazard Classifications
Carc. 1B - Eye Irrit. 2 - Flam. Liq. 2 - Met. Corr. 1 - Skin Irrit. 2
Storage Class
3 - Flammable liquids
flash_point_f
57.2 °F - closed cup
flash_point_c
14.0 °C - closed cup
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J Grayson Richards et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 23(26), 8989-9003 (2003-10-03)
Transgenic mice, expressing mutant beta-amyloid precursor proteins (betaAPPs), have lead to a better understanding of the pathophysiological processes in Alzheimer's disease (AD). In many of these models, however, the temporal development of cognitive decline and the relationship to Abeta deposition
Fubing Ouyang et al.
Brain pathology (Zurich, Switzerland), 30(1), 165-178 (2019-07-07)
Conflicting evidence exists regarding whether focal cerebral infarction contributes to cerebral amyloid-β (Aβ) deposition, as observed in Alzheimer's disease. In this study, we aimed to evaluate the presence of Aβ deposits in the ipsilateral thalamus and hippocampus 12 months post-stroke
Laurence Ozmen et al.
Neuro-degenerative diseases, 2(6), 284-298 (2006-08-16)
Most of the transgenic mice generated to model Alzheimer's disease express human amyloid precursor protein (APP) mutants alone or in conjunction with presenilin mutants. We have generated a mouse model by overexpressing human BACE and human APP with the V717F
Lei Wang et al.
PLoS biology, 6(8), e195-e195 (2008-08-08)
Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can be composed of native globular molecules, such
Antje Willuweit et al.
Frontiers in neuroscience, 15, 699926-699926 (2021-10-22)
Alzheimer's disease (AD) is characterized by formation of amyloid plaques and neurofibrillary tangles in the brain, which can be mimicked by transgenic mouse models. Here, we report on the characterization of amyloid load in the brains of two transgenic amyloidosis
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