High Select™ Depletion Spin Columns
High Select™ Depletion Spin Columns
High Select™ Depletion Spin Columns
High Select™ Depletion Spin Columns
Citas y referencias (8)
Thermo Scientific™

High Select™ Depletion Spin Columns

La resina de agotamiento de HSA/inmunoglobulina Thermo Scientific High Select reduce los componentes de albúmina y anticuerpo que abundan enMás información
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Número de catálogoCantidadTipo de productoDiana de purificación
A3637024 columnasColumnaProteína abundante Top14
A363656 columnasColumnaHSA/inmunoglobulina
A3636624 columnasColumnaHSA/inmunoglobulina
A3636710 columnasColumnaHSA/inmunoglobulina
A3636850 mLResinaHSA/inmunoglobulina
A3637110 columnasColumnaProteína abundante Top14
A3637250 mLResinaProteína abundante Top14
A363696 columnasColumnaProteína abundante Top14
Número de catálogo A36370
Precio (USD)
-
Cantidad:
24 columnas
Tipo de producto:
Columna
Diana de purificación:
Proteína abundante Top14
La resina de agotamiento de HSA/inmunoglobulina Thermo Scientific High Select reduce los componentes de albúmina y anticuerpo que abundan en muestras de plasma humano, lo que ayuda a preparar dichas muestras para la espectrometría de masas o la electroforesis 1D o 2D. La resina se proporciona aquí en un formato práctico de minicolumna de centrifugación de un solo uso para el tratamiento de muestras de 10 µl.

Las características de la resina de agotamiento de HSA/IgG incluyen:
• Flexible: el formato de minicolumna se adapta y optimiza para el tratamiento de muestras de plasma humano de 10 µl
• Optimizado: elimina > 95 % de IgG y > 95 % de albúmina
• Rápido: procesa muestras en ∼ 10 minutos
• Económico: el precio de las columnas de centrifugación rentables es por un solo uso
• Variabilidad reducida: el formato de un solo uso evita el arrastre de proteínas y la variabilidad experimental

La resina de agotamiento de HSA/inmunoglobulina High Select utiliza anticuerpos antiHSA y antiinmunoglobulina inmovilizados altamente específicos (IgG, IgA, IgM, IgD e IgE) para eliminar la seroalbúmina humana (HSA) y todas las subclases principales de inmunoglobulinas de suero y plasma. La resina se suministra en un formato de columna de centrifugación económico y práctico diseñado específicamente para el procesamiento en un solo paso y un solo uso.

Los análisis de fluidos humanos suelen complicarse con frecuencia debido a la presencia de altas concentraciones de albúmina e IgG, que pueden alcanzar más del 70 % del total de las proteínas del suero. La extracción de estas proteínas es a menudo esencial para el estudio de proteínas de baja abundancia. La resina de agotamiento de HSA/inmunoglobulina High Select puede reducir más del 95 % de HSA y el 95 % de IgG. Las muestras se cargan en una columna de centrifugación desechable precargada y se procesan en aproximadamente 10 minutos. El agotamiento de proteínas de alta abundancia ayuda a la detección de proteínas de baja abundancia en las muestras y la posterior identificación mediante espectrometría de masas o electroforesis en gel 1D o 2D.

Productos recomendados
Minicolumnas de centrifugación de agotamiento de proteínas de alta abundancia High Select Top14
Resina de agotamiento de proteínas de alta abundancia High Select Top14
Conjunto de reactivos de etiqueta isobárica TMT10plex T, 3 x 0,8 mg
For Research Use Only. Not for use in diagnostic procedures.
Especificaciones
Tipo de producto finalproteína
Para utilizar con (equipo)Espectrómetro de masas
Etiqueta o tinteSin marcar
Diana de purificaciónProteína abundante Top14
Cantidad24 columnas
Condiciones de envíoHielo húmedo
Paso del flujo de trabajoAgotamiento de proteínas
FormatoMinicolumna de centrifugación
Línea de productosHigh Select
Tipo de productoColumna
Material de partidaPlasma, Suero
Unit SizeEach
Contenido y almacenamiento
Almacenar a 2–8 °C.

Preguntas frecuentes

Can I use the High Select Top14 Abundant Protein Depletion Midi Spin Columns to deplete proteins from rodent samples?

The High Select Top14 Abundant Protein Depletion Midi Spin Columns have only been validated for human samples. We do not recommend using them for protein depletion in rodent samples. For protein depletion in rodent samples, we recommend the following multi-species depletion resins:

  • CaptureSelect MultiSpecies Albumin Depletion Product (Cat. No. 191085305)
  • Pierce Albumin Serum Depletion Kits (Cat. No. 89875)


    • Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

After depletion of abundant proteins from my sample, I still see albumin and other abundant proteins after LC-MS analysis. Did the depletion work?

Depletion does not remove all abundant proteins from the sample. Even with 99% depletion of a specific plasma protein, highly abundant proteins will still be the most abundant proteins in the sample detected by MS analysis. However, depletion significantly decreases the most abundant plasma proteins enabling identification of lower abundant proteins.

Find additional tips, troubleshooting help, and resources within our Mass Spectrometry Support Center.

How do I proceed to downstream mass spec sample preparation after abundant plasma protein depletion?

After the depletion, samples are significantly diluted in buffer. Depleted samples should be concentrated by speed vac drying, solvent precipitation, or diafiltration. Samples dried using a speedvac are directly compatible with the EasyPep kit chemistry after resuspension using the Lysis Solution.

Find additional tips, troubleshooting help, and resources within our Mass Spectrometry Support Center.

What is the maximum loading capacity for the High Select Depletion columns?

Mini columns can deplete up to 10 µL (600 µg) of plasma or serum; midi columns can deplete up to 100 µL (6000 µg) of plasma or serum.

Find additional tips, troubleshooting help, and resources within our Mass Spectrometry Support Center.

What is the percentage of albumin that is removed using abundant protein depletion columns?

More than 99% of albumin can be depleted when columns use the recommended sample to resin ratio.

Find additional tips, troubleshooting help, and resources within our Mass Spectrometry Support Center.

View all High Select™ Depletion Spin Columns FAQs

Citations & References (8)

Citations & References
Abstract
Integrated proteomics reveals brain-based cerebrospinal fluid biomarkers in asymptomatic and symptomatic Alzheimer's disease.
Authors:Higginbotham L,Ping L,Dammer EB,Duong DM,Zhou M,Gearing M,Hurst C,Glass JD,Factor SA,Johnson ECB,Hajjar I,Lah JJ,Levey AI,Seyfried NT
Journal:Science advances
PubMed ID:33087358
Alzheimer's disease (AD) lacks protein biomarkers reflective of its diverse underlying pathophysiology, hindering diagnostic and therapeutic advancements. Here, we used integrative proteomics to identify cerebrospinal fluid (CSF) biomarkers representing a wide spectrum of AD pathophysiology. Multiplex mass spectrometry identified ~3500 and ~12,000 proteins in AD CSF and brain, respectively. Network ... More
METTL16 inhibits pancreatic cancer proliferation and metastasis by promoting MROH8 RNA stability and inhibiting CAPN2 expression - experimental studies.
Authors:Yi T,Wang C,Ye X,Lin J,Lin C,Qin F,Yang W,Ye Y,Ning D,Lan J,Li H,Luo C,Ma J,Wei Z
Journal:International journal of surgery (London, England)
PubMed ID:39434688
BACKGROUND: N6-methyladenosine (m6A) modification plays a crucial role in the progression of various cancers, including pancreatic cancer, by regulating gene expression. However, the specific mechanisms by which m6A affects pancreatic cancer metastasis remain unclear. This study aims to elucidate the role of METTL16, an m6A writer gene, in regulating core ... More
Proteomic profiling identifies SPP1 associated with rapidly progressive interstitial lung disease in anti-MDA5-positive dermatomyositis.
Authors:Qiu Y,Feng X,Liu C,Shi Y,Xu L,You H,Wang L,Lv C,Wang F,Tan W
Journal:Arthritis research & therapy
PubMed ID:38167532
BACKGROUND: Anti-melanoma differentiation-associated gene five antibody positive (MDA5(+)) dermatomyositis (DM) is significantly associated with rapidly progressive interstitial lung disease (RP-ILD). Early detection of RP-ILD remains a major challenge. This study aims to identify and validate prognostic factors for RP-ILD in MDA5(+) DM patients. METHODS: Plasma samples from 20 MDA5(+) DM ... More
Enhancing Proteomics Quality Control: Insights from the Visualization Tool QCeltis.
Authors:Vegesna M,Sundararaman N,Bharadwaj A,Washington K,Pandey R,Haghani A,Chazarin B,Binek A,Fu Q,Cheng S,Herrington D,Van Eyk JE
Journal:Journal of proteome research
PubMed ID:39992359
Large-scale mass-spectrometry-based proteomics experiments are complex and prone to analytical variability, requiring rigorous quality checks across each step in the workflow: sample preparation, chromatography, mass spectrometry, and the bioinformatics stages. This includes quality control (QC) measures that address biological and technical variation. Most QC approaches involve detecting sample outliers and ... More
Tandem mass tag-based quantitative proteomic profiling identifies candidate serum biomarkers of drug-induced liver injury in humans.
Authors:Ravindra KC,Vaidya VS,Wang Z,Federspiel JD,Virgen-Slane R,Everley RA,Grove JI,Stephens C,Ocana MF,Robles-Díaz M,Isabel Lucena M,Andrade RJ,Atallah E,Gerbes AL,Weber S,Cortez-Pinto H,Fowell AJ,Hussaini H,Bjornsson ES,Patel J,Stirnimann G,Verma S,Elsharkawy AM,Griffiths WJH,Hyde C,Dear JW,Aithal GP,Ramaiah SK
Journal:Nature communications
PubMed ID:36869085
Diagnosis of drug-induced liver injury (DILI) and its distinction from other liver diseases are significant challenges in drug development and clinical practice. Here, we identify, confirm, and replicate the biomarker performance characteristics of candidate proteins in patients with DILI at onset (DO; n = 133) and follow-up (n = 120), acute non-DILI at onset ... More
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