High Select™ Depletion Spin Columns
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High Select™ Depletion Spin Columns
High Select™ Depletion Spin Columns
High Select™ Depletion Spin Columns
Thermo Scientific™

High Select™ Depletion Spin Columns

Decrease albumin, immunoglobulins, and other high-abundance proteins from human serum or plasma in preparation for mass spectrometry analysis, or 1D and 2D gel electrophoresis using High Select depletion spin columns or resin.
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Catalog NumberQuantityProduct TypePurification Target
A3637024 ColumnsMini Spin ColumnTop14 Abundant Protein
A363656 ColumnsMini Spin ColumnHSA/Immunoglobulin
A3636624 ColumnsMini Spin ColumnHSA/Immunoglobulin
A3636710 ColumnsMidi Spin ColumnHSA/Immunoglobulin
A3636850 mLResinHSA/Immunoglobulin
A3637110 ColumnsMidi Spin ColumnTop14 Abundant Protein
A3637250 mLResinTop14 Abundant Protein
A363696 ColumnsMini Spin ColumnTop14 Abundant Protein
Catalog number A36370
Price (CNY)
7,263.00
飞享价
Ends: 31-Dec-2025
9,404.00
Save 2,141.00 (23%)
Each
Add to cart
Quantity:
24 Columns
Product Type:
Mini Spin Column
Purification Target:
Top14 Abundant Protein
Price (CNY)
7,263.00
飞享价
Ends: 31-Dec-2025
9,404.00
Save 2,141.00 (23%)
Each
Add to cart
Analysis of human fluids is often complicated by the presence of high concentrations of serum proteins, including albumin and IgG that can make up more than 70% of total serum protein. Removal of albumin, immunoglobulins, and other abundant proteins is essential for the study of low-abundance proteins. Thermo Scientific High Select HSA/Immunoglobulin and Top 14 Abundant Protein depletion spin columns and resins enable depletion of the most abundant proteins in human serum and plasma for improved detection of low-abundance proteins using mass spectrometry analysis or 1D or 2D gel electrophoresis.
Flexible—resin provided in mini and midi column formats as well as bulk for custom filling options
Optimized—removes >95% of IgG and >95% of albumin (HSA/Immunoglobulin); removes >95% of IgG and >95% of albumin, plus 12 other abundant proteins (Top 14)
Fast—process samples in ∼10 minutes
Economical—cost-effective spin columns are priced for single use
Reduced carry-over—one-time use prevents protein carryover and experimental variability

High Select HSA/Immunoglobulin Depletion Resin uses highly specific, immobilized anti-HSA and anti-immuoglobulin antibodies (IgG, IgA, IgM, IgD, and IgE) to remove human serum albumin (HSA) and all major subclasses of immunoglobulins from serum and plasma. High Select Top14 Abundant Protein Depletion Resin uses highly specific immobilized antibodies to remove human serum albumin (HSA), albumin, IgG, IgA, IgM, IgD, IgE, kappa and lambda light chains, alpha-1-acidglycoprotein, alpha-1-antitrypsin, alpha-2-macroglobulin, apolipoprotein A1, fibrinogen, haptoglobin, and transferrin from serum, plasma, or spinal fluids. The resins are provided in an economical and convenient spin column format specifically designed for one-step processing and single use or bulk format for custom filling.

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Final Product TypeProtein
For Use With (Equipment)Mass Spectrometer
Label or DyeUnlabeled
Purification TargetTop14 Abundant Protein
Quantity24 Columns
Shipping ConditionWet Ice
Workflow StepProtein Depletion
FormatMini Spin Column
Product LineHigh Select
Product TypeMini Spin Column
Starting MaterialPlasma, Serum
Unit SizeEach
Contents & Storage
Store at 2–8°C.

Frequently asked questions (FAQs)

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.

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