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Merck
CN

TTR002

Amyloid TISSUE-TROL Control Slides

from human heart

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NACRES:
NA.47
UNSPSC Code:
41116121
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biological source

human heart

application(s)

hematology
histology

storage temp.

room temp

General description

Histology control slides are essential tools in supporting formal quality assurance programs within pathology laboratories. Our TISSUE-TROL slides feature paraffin-embedded tissue sections with known characteristics, specifically designed for monitoring staining performance.(a) Amyloid TISSUE-TROL Control Slides are histology slides containing paraffin embedded heart tissue containing amyloid proteins cut at 8 microns. The product comes with one reference slide stained using Congo Red (amyloid stain). Historically, amyloids have been described as fibrillar protein deposits often associated with a disease. Diseases caused by amyloids are referred to as “amyloidosis”. The product comes with one reference slide stained using Congo Red (amyloid stain). Historically, amyloids have been described as fibrillar protein deposits often associated with a disease. Diseases caused by amyloids are referred to as “amyloidosis”.

Application

Amyloid TISSUE-TROL Control Slides is used as a positive control to study pancreatic inflammation, and suitable to study whenther the Serum amyloid A (SAA) is present in human saccular Intracranial aneurysm walls and determine its association with aneurysm rupture.

Other Notes

Box contains 24 unstained slides plus one reference slide stained using Amyloid Stain, Congo Red (Procedure No. HT60).

Legal Information

TISSUE-TROL is a trademark of Sigma-Aldrich Co. LLC

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

高风险级别生物产品--人源产品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Pancreatic inflammation and increased islet macrophages in insulin resistant juvenile primates.
Nicol L, et al.
The Journal of Endocrinology, JOE-J12 (2013)
J C Rochet et al.
Current opinion in structural biology, 10(1), 60-68 (2000-02-19)
Recent progress has improved our knowledge of how proteins form amyloid fibrils. Both 'natively unfolded' and globular proteins have been shown to initiate fibrillization by adopting a partially structured conformation. Oligomeric prefibrillar intermediates have been extensively characterized with respect to
L E Nicol et al.
The Journal of endocrinology, 217(2), 207-213 (2013-02-20)
Chronic high caloric intake has contributed to the increased prevalence of pediatric obesity and related morbidities. Most overweight or obese children, however, do not present with frank metabolic disease but rather insulin resistance or subclinical precursors. The innate immune system

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