High Select™ Depletion Spin Columns

Citations & References (8)

Thermo Scientific™

High Select™ Depletion Spin Columns

Name: High Select™ Depletion Spin Columns
SKU: A36370

Thermo Scientific High Select HSA/Immunoglobulin Depletion Resinは、ヒト血漿サンプル中に高量に存在するアルブミンおよび抗体成分を低減し、これらのサンプルを質量分析または1D／2D電気泳動用に調製するのに役立ちます。このレジンは詳細を見る

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製品番号（カタログ番号）	数量	製品タイプ	精製標的
A36370	24カラム	スピンカラム	Top14 Abundant Protein
A36365	6カラム	スピンカラム	HSA/Immunoglobulin
A36366	24カラム	スピンカラム	HSA/Immunoglobulin
A36367	10 Columns	スピンカラム	HSA/Immunoglobulin
A36368	50 mL	樹脂	HSA/Immunoglobulin
A36371	10 Columns	スピンカラム	Top14 Abundant Protein
A36372	50 mL	樹脂	Top14 Abundant Protein
A36369	6カラム	スピンカラム	Top14 Abundant Protein

8 オプション

製品番号（カタログ番号） A36370

価格（JPY）

163,600

Each

お問い合わせください ›

数量:

24カラム

製品タイプ:

スピンカラム

精製標的:

Top14 Abundant Protein

Thermo Scientific High Select HSA/Immunoglobulin Depletion Resinは、ヒト血漿サンプル中に高量に存在するアルブミンおよび抗体成分を低減し、これらのサンプルを質量分析または1D／2D電気泳動用に調製するのに役立ちます。このレジンは、10 µLのサンプルの処理に便利なシングルユースミニスピンカラムフォーマットで提供されます。

HSA/IgG除去レジンの特長：
•柔軟—ミニカラムフォーマットは、10 µLのヒト血漿サンプルを処理するようにサイズ調整および最適化済み
• 最適化済み—95%超のIgGと、95%超のアルブミンを除去
• 高速 —サンプルを約10分で処理
• 経済的—シングルユース向けに価格設定されたコスト効率の高いスピンカラム
• ばらつきの低減—1回限りの使用であるため、タンパク質のキャリーオーバーや実験間のばらつきを防止

High Select HSA/Immunoglobulin Depletion Resinは、特異性の高い固定化抗HSAおよび抗イムノグロブリン抗体（IgG、IgA、IgM、IgD、およびIgE）を使用しており、血清および血漿からヒト血清アルブミン（HSA）やイムノグロブリンのすべての主要サブクラスを除去します。この樹脂は、ワンステップ処理とシングルユース用に特別に設計された経済的で便利なスピンカラムフォーマットで提供されています。

ヒトの体液の分析は、総血清タンパク質の70%強を占める高濃度のアルブミンおよびIgGの存在により複雑になることがよくあります。少量タンパク質の研究では多くの場合、このようなタンパク質の除去が不可欠です。High Select HSA/Immunoglobulin Depletion Resinは、HSAを95%超、IgGを95%超除去できます。サンプルを充填済みのディスポーザブルスピンカラムにロードすると、約10分で処理されます。多量のタンパク質を除去することで、サンプル中の微量タンパク質の検出や、質量分析または1D／2Dゲル電気泳動による同定が可能になります。

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For Research Use Only. Not for use in diagnostic procedures.

仕様

最終産物タイプタンパク質

使用対象 (装置)質量分析計

標識または色素非標識

精製標的Top14 Abundant Protein

数量24カラム

出荷条件湿氷

ワークフローステップProtein Depletion

フォーマットMini Spin Column

製品ラインHigh Select

製品タイプスピンカラム

原料Plasma, Serum

Unit SizeEach

組成および保存条件

2～8℃で保存してください。

よくあるご質問（FAQ）

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)

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

引用および参考文献 (8)

引用および参考文献

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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