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Merck
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SEP010

Millipore

Seppro® IgY14

Spin Columns

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About This Item

Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Capacité

1 mg total protein loading(14 μL of human plasma, average human protein concentration 70 mg/mL)

Température de stockage

2-8°C

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Description générale

Seppro® IgY14 columns allow users to separate 14 highly abundant proteins (HAP) from plasma protein mixtures. The Avian polyclonal IgY (Immunoglobulin Yolk) antibodies, have a distinct, highly specific partitioning advantage over competing products, allowing the researcher to look at a much cleaner human protein mixture. Seppro® columns make further proteomics analysis into the plasma proteome much easier and provide cleaner results.

Proteins Depleted:

Albumin
IgG
α1-Antitrypsin
IgA
IgM
Transferrin
Haptoglobin
α2-Macroglobulin
Fibrinogen
Complement C3
α1-Acid Glycoprotein (Orosomucoid)
HDL (Apolipoproteins A-I and A-II)
LDL (mainly Apolipoprotein B)

Application

Seppro® IgY14, spin columns (capacity: 15-20μl) is designed for use as a plasma/serum protein removal tool base upon immune affinity removal of 14 highly abundant proteins (HAP) from human plasma protein mixtures via liquid chromatography. Seppro® IgY14 is used to support the analysis of low abundance human serum/plasma proteins.[1][2]

Informations légales

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

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Description
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Code de la classe de stockage

10 - Combustible liquids

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Certificats d'analyse (COA)

Lot/Batch Number
SLCD9598
SLCD2893
SLCC1883
SLCB3766
SLBZ9708

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Maneesh Bhargava et al.
PloS one, 9(10), e109713-e109713 (2014-10-08)
Acute Respiratory Distress Syndrome (ARDS) continues to have a high mortality. Currently, there are no biomarkers that provide reliable prognostic information to guide clinical management or stratify risk among clinical trial participants. The objective of this study was to probe
Hoi Pang Low et al.
Genomics, proteomics & bioinformatics, 11(6), 335-344 (2013-12-04)
Preeclampsia, a complication of pregnancy characterized by hypertension and proteinuria, has been found to reduce the subsequent risk for breast cancer in female offspring. As this protective effect could be due to exposure to preeclampsia-specific proteins during intrauterine life, the
Chien-Lun Chen et al.
Journal of proteomics, 85, 28-43 (2013-05-02)
In this study, we evaluated the reproducibility of abundant urine protein depletion by hexapeptide-based library beads and an antibody-based affinity column using the iTRAQ technique. The antibody-based affinity-depletion approach, which proved superior, was then applied in conjunction with iTRAQ to
Inmaculada Lopez-Font et al.
Molecular neurobiology, 56(12), 8603-8616 (2019-07-11)
The β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the main brain β-secretase responsible for the amyloidogenic processing of the amyloid precursor protein (APP). Previous studies have suggested that cerebrospinal fluid (CSF) β-secretase activity may be a candidate diagnostic
Majlinda Kullolli et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 939, 10-16 (2013-10-05)
Human plasma is a commonly used diagnostic fluid in clinical chemistry. In-depth plasma proteomic analysis is performed to search for disease biomarkers, however the large dynamic range of protein abundance in plasma presents a substantial analytical challenge. Removal of abundant
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