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C0356

Protein Extraction Reagent Type 4

Name: Protein Extraction Reagent Type 4
Brand: SIGMA

Synonym(s):

Protein extraction solution

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About This Item

NACRES:

NA.56

UNSPSC Code:

41116012

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form

solid

Quality Level

200

solubility

deionized water: 13.6 g /15 ml at 25 °C, clear to hazy

General description

Protein Extraction Reagent Type 4, is a highly premixed, prequalified and effective protein solubilization and extraction reagent composed of urea, thiourea, Trizma^®, and detergent C7BzO (C0856).

Application

Protein extraction reagent type 4 is optimized for proteomic studies. Cellular and organelle membrane solubilizing reagent is ideal for protein extraction prior to isoelectric focusing and 2D electrophoresis. Reducing and alkylating reagents TBP (T7567) and iodoacetamide (A3221) are recommended for use with this reagent. Protein extraction reagent type 4 is also available as a component of the ProteoPrep^® Sample.

Other Notes

Contains urea, thiourea, Trizma^®, and detergent C7BzO (C0856).

Legal Information

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

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

pictograms

GHS08,GHS07,GHS09

signalword

Warning

hcodes

H302,H351,H361fd,H411

pcodes

P202 - P264 - P273 - P280 - P301 + P312 - P308 + P313

Hazard Classifications

Acute Tox. 4 Oral - Aquatic Chronic 2 - Carc. 2 - Repr. 2

Storage Class

11 - Combustible Solids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

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Comparative profiling of highly enriched 22L and Chandler mouse scrapie prion protein preparations.

Roger A Moore et al.

Proteomics, 10(15), 2858-2869 (2010-06-03)

Transmissible spongiform encephalopathies (TSEs) or prion diseases are characterized by the accumulation of an aggregated isoform of the prion protein (PrP). This pathological isoform, termed PrP(Sc), appears to be the primary component of the TSE infectious agent or prion. However

Age- and sex-dependent differences in extracellular matrix metabolism associate with cardiac functional and structural changes.

Gabriel A Grilo et al.

Journal of molecular and cellular cardiology, 139, 62-74 (2020-01-25)

Age-related remodeling of the heart causes structural and functional changes in the left ventricle (LV) that are associated with a high index of morbidities and mortality worldwide. Some cardiac pathologies in the elderly population vary between genders revealing that cardiac

Comparative analysis of hemolymph proteome maps in diapausing and non-diapausing larvae of Sesamia nonagrioides.

Meritxell Pérez-Hedo et al.

Proteome science, 10(1), 58-58 (2012-10-02)

Sesamia nonagrioides is a noctuid that feeds on maize, sugar cane and sorghum in North Africa and Southern Europe. Larvae reared under long day conditions pupate after 5 or 6 larval instars, whereas larvae reared under short day conditions enter

Carbamylation of proteins in 2-D electrophoresis--myth or reality?

John McCarthy et al.

Journal of proteome research, 2(3), 239-242 (2003-06-20)

Carbamylation is widely quoted as being a problem in 2-D gel analysis and the associated sample preparation steps. This modification occurs when iso-cyanate, a urea break-down product, covalently modifies lysine residues, thus inducing a change in isoelectric point. Urea is

VIP36 protein is a target of ectodomain shedding and regulates phagocytosis in macrophage Raw 264.7 cells.

Kyoko Shirakabe et al.

The Journal of biological chemistry, 286(50), 43154-43163 (2011-10-22)

Ectodomain shedding is a posttranslational modification mechanism, which liberates extracellular domains of membrane proteins through juxtamembrane processing executed mainly by the ADAM (a disintegrin and metalloprotease) family of metalloproteases. Shedding is a unique and effective mechanism for inducing multifaceted effects

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Global Trade Item Number

SKU	GTIN
C0356-4BTL	04061833450505
C0356-1BTL	04061821194404

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