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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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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
Laurence Ozmen et al.
Neuro-degenerative diseases, 6(1-2), 29-36 (2008-12-11)
Alzheimer's disease is the most common cause of dementia occurring in the elderly. The identification of the genetic factors in the familial forms of the disease enabled the generation of transgenic animals which reproduce an essential part of its pathology.
Samir K Maji et al.
PLoS biology, 6(2), e17-e17 (2008-02-08)
Amyloids are highly organized protein aggregates that are associated with both neurodegenerative diseases such as Alzheimer disease and benign functions like skin pigmentation. Amyloids self-polymerize in a nucleation-dependent manner by recruiting their soluble protein/peptide counterpart and are stable against harsh
Brian O'Nuallain et al.
The Journal of biological chemistry, 279(17), 17490-17499 (2004-01-31)
Over residues 15-36, which comprise the H-bonded core of the amyloid fibrils it forms, the Alzheimer's disease plaque peptide amyloid beta (Abeta) possesses a very similar sequence to that of another short, amyloidogenic peptide, islet amyloid polypeptide (IAPP). Using elongation
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