SEP010
Seppro® IgY14
Spin Columns
Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
About This Item
Codice UNSPSC:
12352200
NACRES:
NA.32
Prodotti consigliati
Capacità
1 mg total protein loading(14 μL of human plasma, average human protein concentration 70 mg/mL)
Temperatura di conservazione
2-8°C
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Descrizione generale
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)
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)
Applicazioni
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]
Note legali
Seppro is a registered trademark of Merck KGaA, Darmstadt, Germany
I componenti del kit sono disponibili anche separatamente
N° Catalogo
Descrizione
SDS
Codice della classe di stoccaggio
10 - Combustible liquids
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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
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
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
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
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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