69385
Protein Standard Mix 15 - 600 kDa
for size exclusion chromatography
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About This Item
NACRES:
NA.24
UNSPSC Code:
85151701
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
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
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
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
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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
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
Different Structural Conformers of Monomeric α-Synuclein Identified after Lyophilizing and Freezing.
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
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