MilliporeSigma
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69385

Supelco

Protein Standard Mix 15 - 600 kDa

for size exclusion chromatography

NACRES:
NA.24

Quality Level

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

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P561969149-M32124
Supelco

Supelco

P5619

Protein Standard

mol wt

15-600 kDa

mol wt

-

mol wt

-

mol wt

-

technique(s)

gel permeation chromatography (GPC): suitable

technique(s)

gel permeation chromatography (GPC): suitable

technique(s)

-

technique(s)

HPLC: suitable, gas chromatography (GC): suitable

format

neat

format

neat

format

-

format

multi-component solution

analyte chemical class(es)

amino acids, peptides, proteins

analyte chemical class(es)

amino acids, peptides, proteins

analyte chemical class(es)

-

analyte chemical class(es)

-

application(s)

clinical
food and beverages
pharmaceutical

application(s)

food and beverages

application(s)

-

application(s)

agriculture
cleaning products
cosmetics
food and beverages
personal care

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

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

Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Classifications

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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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
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
Thomas Fricke et al.
Viruses, 14(3) (2022-03-27)
Kaposi's sarcoma herpesvirus (KSHV) is associated with a significant disease burden, in particular in Sub-Sahara Africa. A KSHV vaccine would be highly desirable, but the mechanisms underlying neutralizing antibody responses against KSHV remain largely unexplored. The complex made of glycoproteins
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
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

Articles

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