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Merck
CN

69385

Protein Standard Mix 15 - 600 kDa

for size exclusion chromatography

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About This Item

NACRES:
NA.24
UNSPSC Code:
85151701

Key Documents

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Product Name

Protein Standard Mix 15 - 600 kDa, for size exclusion chromatography

form

solid

mol wt

15-600 kDa

analyte chemical class(es)

amino acids, peptides, proteins

technique(s)

gel permeation chromatography (GPC): suitable

application(s)

clinical
food and beverages
pharmaceutical

format

neat

storage temp.

−20°C

Quality Level

100

Related Categories

Application

This analytical standard is used for the following:
  • Evaluation of selectivity and separation efficiency of size exclusion chromatography (SEC) to separate intact proteins by varying flow rate, size of silica particles and pore sizes in the column
  • Simultaneous determination of oligomerized and nitrated proteins by size exclusion chromatography-high performance liquid chromatography-diode array detection (SEC-HPLC-DAD)
  • Molecular weight separation of proteins by size-exclusion chromatography, formed upon O3 and NO2 induced oxidation, nitration, and oligomerization of bovine serum albumin (BSA) as a model protein
  • Estimation of molecular masses of two recombinant proteins— TNF fluorescent sensor (BTN-Kat) and fluorescent sensor-inhibitor (ITN-Kat), by size exclusion chromatography (SEC) to evaluate their ability of binding and neutralizing tumor necrosis factor (TNF) in vitro and further serving as imaging labels for non-invasive analysis

General description

The protein standard mix is a calibration standard to test and monitor performance of size exclusion chromatography (SEC) columns. It is a lyophilized mixture of molecular weight markers ranging from 15 kDa to 600 kDa.

Components

Thyroglobulin bovine MW ~ 670 000 Da

γ-globulins from bovine blood MW ~ 150 000 Da

Ovalbumin MW~ 44 300 Da

Ribonuclease A type I-A MW ~ 13 700 Da

p-aminobenzoic acid (pABA) MW ~ 137 Da

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

Acute Tox. 4 Dermal - Acute Tox. 4 Inhalation - Acute Tox. 4 Oral - Aquatic Chronic 3 - Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

监管及禁止进口产品
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Certificates of Analysis (COA)

Lot/Batch Number
BCCP0625
BCCN9919
BCCN0632
BCCM2180
BCCL2045

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Anastasiya Lavell et al.
The Plant journal : for cell and molecular biology, 108(5), 1332-1345 (2021-09-29)
Rhomboid-like proteins are intramembrane proteases with a variety of regulatory roles in cells. Though many rhomboid-like proteins are predicted in plants, their detailed molecular mechanisms or cellular functions are not yet known. Of the 13 predicted rhomboids in Arabidopsis thaliana
Marc D Zack et al.
Scientific reports, 7(1), 11112-11112 (2017-09-13)
In this work, we characterized 2 novel insecticidal proteins; Vip3Ab1 and Vip3Bc1. These proteins display unique insecticidal spectra and have differential rates of processing by lepidopteran digestive enzymes. Furthermore, we have found that both proteins exist as tetramers in their
Yang Wang et al.
Nature communications, 13(1), 4614-4614 (2022-08-09)
Single-chain variable fragments (scFvs), composed of variable domains of heavy and light chains of an antibody joined by a linker, share antigen binding capacity with their parental antibody. Due to intrinsically low solubility and stability, only two Escherichia coli-produced scFvs
Amberley D Stephens et al.
Analytical chemistry, 90(11), 6975-6983 (2018-05-12)
Understanding the mechanisms behind amyloid protein aggregation in diseases, such as Parkinson's and Alzheimer's disease, is often hampered by the reproducibility of in vitro assays. Yet, understanding the basic mechanisms of protein misfolding is essential for the development of novel
Christopher J Kampf et al.
Environmental science & technology, 49(18), 10859-10866 (2015-08-20)
Air pollution is a potential driver for the increasing prevalence of allergic disease, and post-translational modification by air pollutants can enhance the allergenic potential of proteins. Here, the kinetics and mechanism of protein oligomerization upon ozone (O3) exposure were studied
View All Related Papers

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