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	48-602MAG	Buffer Detection Kit for Magnetic Beads	1 Kit

ZipTip^® Pipette Tips

Concentrating and purifying samples for MALDI-ToF MS 더보기

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ZipTip^® Pipette Tips정렬 및 필터링 지우기 Show Filter

ZTC18S008

ZipTip with 0.6 µL C₁₈ resin

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ZTC18S096

ZipTip with 0.6 µL C₁₈ resin

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ZTC18S960

ZipTip with 0.6 µL C₁₈ resin

960

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ZTC04S008

ZipTip with 0.6 µL C₄ resin

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ZTC04S096

ZipTip with 0.6 µL C₄ resin

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ZTC04S960

ZipTip with 0.6 µL C₄ resin

960

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ZTC18M008

ZipTip with 0.2 µL C₁₈ resin

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ZTC18M096

ZipTip with 0.2 µL C₁₈ resin

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ZTC18M960

ZipTip with 0.2 µL C₁₈ resin

960

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ZTSCXS008

ZipTip with 0.6 µL strong cation resin

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ZTSCXS096

ZipTip with 0.6 µL strong cation resin

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Documentation

References

Reference overview	Application	Pub Med ID
A CROSS-SPECIES STUDY OF PI3K PROTEIN-PROTEIN INTERACTIONS REVEALS THE DIRECT INTERACTION OF P85 AND SHP2 Susanne B. Breitkopf, Xuemei Yang, Michael J. Begley, Meghana Kulkarni, Yu-Hsin Chiu, Alexa B. Turke, Jessica Lauriol, Min Yuan, Jie Qi, Jeffrey A. Engelman, Pengyu Hong, Maria I. Kontaridis, Lewis C. Cantley, Norbert Perrimon, John M. Asara Sci Rep. 2016 요약 표시 Using a series of immunoprecipitation (IP)-tandem mass spectrometry (LC-MS/MS) experiments and reciprocal BLAST, we conducted a fly-human cross-species comparison of the phosphoinositide-3-kinase (PI3K) interactome in a drosophila S2R+ cell line and several NSCLC and human multiple myeloma cell lines to identify conserved interacting proteins to PI3K, a critical signaling regulator of the AKT pathway. Using H929 human cancer cells and drosophila S2R+ cells, our data revealed an unexpected direct binding of Corkscrew, the drosophila ortholog of the non-receptor protein tyrosine phosphatase type II (SHP2) to the Pi3k21B (p60) regulatory subunit of PI3K (p50/p85 human ortholog) but no association with Pi3k92e, the human ortholog of the p110 catalytic subunit. The p85-SHP2 association was validated in human cell lines, and formed a ternary regulatory complex with GRB2-associated-binding protein 2 (GAB2). Validation experiments with knockdown of GAB2 and Far-Western blots proved the direct interaction of SHP2 with p85, independent of adaptor proteins and transfected FLAG-p85 provided evidence that SHP2 binding on p85 occurred on the SH2 domains. A disruption of the SHP2-p85 complex took place after insulin/IGF1 stimulation or imatinib treatment, suggesting that the direct SHP2-p85 interaction was both independent of AKT activation and positively regulates the ERK signaling pathway.		26839216
FOOD PEPTIDOMICS OF IN VITRO GASTROINTESTINAL DIGESTIONS OF PARTIALLY PURIFIED BOVINE HEMOGLOBIN: LOW-RESOLUTION VERSUS HIGH-RESOLUTION LC-MS/MS ANALYSES Juliette Caron, Gabrielle Chataigne, Jean-Pascal Gimeno, Nathalie Duhal, Jean-Francois Goossens, Pascal Dhulster, Benoit Cudennec, Rozenn Ravallec, Christophe Flahaut Electrophoresis 2016 요약 표시 Consumers and governments have become aware how the daily diet may affect the human health. All proteins from both plant and animal origins are potential sources of a wide range of bioactive peptides and the large majority of those display health-promoting effects. In the meat production food chain, the slaughterhouse blood is an inevitable co-product and, today, the blood proteins remain underexploited despite their bioactive potentiality. Through a comparative food peptidomics approach we illustrate the impact of resolving power, accuracy, sensitivity, and acquisition speed of low-resolution (LR)- and high-resolution (HR)-LC-ESI-MS/MS on the obtained peptide mappings and discuss the limitations of MS-based peptidomics. From in vitro gastrointestinal digestions of partially purified bovine hemoglobin, we have established the peptide maps of each hemoglobin chain. LR technique (normal bore C18 LC-LR-ESI-MS/MS) allows us to identify without ambiguity 75 unique peptides while the HR approach (nano bore C18 LC-HR-ESI-MS/MS) unambiguously identify more than 950 unique peptides (post-translational modifications included). Herein, the food peptidomics approach using the most performant separation methods and mass spectrometers with high-resolution capabilities appears as a promising source of information to assess the health potentiality of proteins.		26990205
ISOLATION AND IDENTIFICATION OF MEMBRANE VESICLE-ASSOCIATED PROTEINS IN GRAM-POSITIVE BACTERIA AND MYCOBACTERIA Rafael Prados-Rosales, Lisa Brown, Arturo Casadevall, Sandra Montalvo-Quiros, Jose L. Luque-Garcia MethodsX. 2014 요약 표시 Many intracellular bacterial pathogens naturally release membrane vesicles (MVs) under a variety of growth environments. For pathogenic bacteria there are strong evidences that released MVs are a delivery mechanism for the release of immunologically active molecules that contribute to virulence. Identification of membrane vesicle-associated proteins that can act as immunological modulators is crucial for opening up new horizons for understanding the pathogenesis of certain bacteria and for developing novel vaccines. In this protocol, we provide all the details for isolating MVs secreted by either mycobacteria or Gram-positive bacteria and for the subsequent identification of the protein content of the MVs by mass spectrometry. The protocol is adapted from Gram-negative bacteria and involves four main steps: (1) isolation of MVs from the culture media; (2) purification of MVs by density gradient ultrucentrifugation; (3) acetone precipitation of the MVs protein content and in-solution trypsin digestion and (4) mass spectrometry analysis of the generated peptides and protein identification. Our modifications are:<br />• Growing Mycobacteria in a chemically defined media to reduce the number of unrelated bacterial components in the supernatant.<br />• The use of an ultrafiltration system, which allows concentrating larger volumes.<br />• In solution digestion of proteins followed by peptides purification by ziptip.		26150943
Comparative evaluation of peptide desalting methods for salivary proteome analysis. Nico Jehmlich, Claas Golatowski, Annette Murr, Gesell Salazar, Vishnu Mukund Dhople, Elke Hammer, Uwe Volker Clin Chim Acta 2014		24751662
Using theoretical protein isotopic distributions to parse small-mass-difference post-translational modifications via mass spectrometry. Timothy W. Rhoads, Jared R. Williams, Nathan I. Lopez, Jeffrey T. Morre, C. Samuel Bradford, Joseph S. Beckman J Am Soc Mass Spectrom 2013		23247967
DETERMINIG IN VIVO PHOSPHORYLATION SITES USING MASS SPECTROMETRY Susanne B. Breitkopf, John M. Asara Curr Protoc Mol Biol 2012 요약 표시 Phosphorylation is the most studied protein post-translational modification (PTM) in biological systems, since it controls cell growth, proliferation, survival, and other processes. High-resolution/high mass accuracy mass spectrometers are used to identify protein phosphorylation sites due to their speed, sensitivity, selectivity, and throughput. The protocols described here focus on two common strategies: (1) identifying phosphorylation sites from individual proteins and small protein complexes, and (2) identifying global phosphorylation sites from whole-cell and tissue extracts. For the first, endogenous or epitope-tagged proteins are typically immunopurified from cell lysates, purified via gel electrophoresis or precipitation, and enzymatically digested into peptides. Samples can be optionally enriched for phosphopeptides using immobilized metal affinity chromatography (IMAC) or titanium dioxide (TiO(2)) and then analyzed by microcapillary liquid chromatography/tandem mass spectrometry (LC-MS/MS). Global phosphorylation site analyses that capture pSer/pThr/pTyr sites from biological sources sites are more resource and time consuming and involve digesting the whole-cell lysate, followed by peptide fractionation by strong cation-exchange chromatography, phosphopeptide enrichment by IMAC or TiO(2), and LC-MS/MS. Alternatively, the protein lysate can be fractionated by SDS-PAGE, followed by digestion, phosphopeptide enrichment, and LC-MS/MS. One can also immunoprecipitate only phosphotyrosine peptides using a pTyr antibody followed by LC-MS/MS.		22470061
Rapid metabolite identification with sub parts-per-million mass accuracy from biological matrices by direct infusion nanoelectrospray ionization after clean-up on a ZipTip and LTQ/Orbitrap mass spectrometry. John C. L. Erve, William DeMaio, Rasmy E. Talaat Rapid Commun Mass Spectrom 2008 요약 표시 Metabolite identification studies remain an integral part of pre-clinical and clinical drug development programs. Analysis of biological matrices, such as plasma, urine, feces and bile, pose challenges due to the large amounts of endogenous components that can mask a drug and its metabolites. Although direct infusion nanoelectrospray using capillaries has been used routinely for proteomic studies, metabolite identification has traditionally employed liquid chromatographic (LC) separation prior to analysis. A method is described here for rapid metabolite profiling in biological fluids that involves initial sample clean-up using pipette tips packed with reversed-phase material (i.e. ZipTips) to remove matrix components followed by direct infusion nanoelectrospray on an LTQ/Orbitrap mass spectrometer using a protonated polydimethylcyclosiloxane cluster ion for internal calibration. We re-examined samples collected from a prazosin metabolism study in the rat. Results are presented that demonstrate that sub parts-per-million accuracies can be achieved on molecular ions, facilitating identification of metabolites, and on product ions, facilitating structural assignments. The data also show that the high-resolution measurements (R = 100,000 at m/z 400) enable metabolites of interest to be resolved from endogenous components. The extended analysis times available with nanospray enables signal averaging for 1 min or more that is valuable when metabolites are present in low concentrations as encountered here in plasma and brain. Using this approach, the metabolic fate of a drug can be quickly obtained. A limitation of this approach is that metabolites that are structural isomers cannot be distinguished, although such information can be collected by LC/MS during follow-on experiments		18763271
GEL-FREE SAMPLE PREPARATION FOR THE NANOSCALE LC-MS/MS ANALYSIS AND IDENTIFICATION OF LOW-NANOGRAM PROTEIN SAMPLES Marco Gaspari, Vittorio Abbonante, Giovanni Cuda J Sep Sci. 2007 요약 표시 Protein identification at the low nanogram level could in principle be obtained by most nanoscale LC-MS/MS systems. Nevertheless, the complex sample preparation procedures generally required in biological applications, and the consequent high risk of sample losses, very often hamper practical achievement of such low levels. In fact, the minimal amount of protein required for the identification from a gel band or spot, in general, largely exceeds the theoretical limit of identification reachable by nanoscale LC-MS/MS systems. A method for the identification of low levels of purified proteins, allowing limits of identification down to 1 ng when using standard bore, 75 microm id nanoscale LC-MS/MS systems is here reported. The method comprises an offline two-step sample cleanup, subsequent to protein digestion, which is designed to minimize sample losses, allows high flexibility in the choice of digestion conditions and delivers a highly purified peptide mixture even from "real world" digestion conditions, thus allowing the subsequent nanoscale LC-MS/MS analysis to be performed in automated, unattended operation for long series. The method can be applied to the characterization of low levels of affinity purified protei		17763504
COMPARISON OF SDS- AND METHANOL-ASSISTED PROTEIN SOLUBILIZATION AND DIGESTION METHODS FOR ESCHERICHIA COLI MEMBRANE PROTEOME ANALYSIS BY 2-D LC-MS/MS Nan Zhang, Rui Chen, Nelson Young, David Wishart, Philip Winter, Joel H. Weiner, Liang Li Proteomics 2007		17309111
Analysis of modified apolipoprotein B-100 structures formed in oxidized low-density lipoprotein using LC-MS/MS. Takashi Obama, Rina Kato, Yutaka Masuda, Katsuhiko Takahashi, Toshihiro Aiuchi, Hiroyuki Itabe Proteomics 2007 요약 표시 Oxidatively modified low-density lipoprotein (oxLDL) is one of the major factors involved in the development of atherosclerosis. Because of the insolubility of apolipoprotein B-100 (apoB-100) and the heterogeneous nature of oxidative modification, modified structures of apoB-100 in oxLDL are poorly understood. We applied an on-Membrane sample preparation procedure for LC-MS/MS analysis of apoB-100 proteins in native and modified low-density lipoprotein (LDL) samples to eliminate lipid components in the LDLs followed by collection of tryptic digests of apoB-100. Compared with a commonly used in-gel digestion protocol, the sample preparation procedure using PVDF membrane greatly increased the recovery of tryptic peptides and resulted in improved sequence coverage in the final analysis, which lead to the identification of modified amino acid residues in copper-induced oxLDL. A histidine residue modified by 4-hydroxynonenal, a major lipid peroxidation product, as well as oxidized histidine and tryptophan residues were detected. LC-MS/MS in combination with the on-Membrane sample preparation procedure is a useful method to analyze highly hydrophobic proteins such as apoB-100.		17549798

FAQ

Question	Answer
Are ZipTip pipette tips compatible with robotic / automated sample preparation systems?	ZipTipm-C₁₈ compatibility has been demonstarted with the following robotic / automated sample preparation systems: 1. ABI Symbiot™ Sample Workstation for MALDI TOF Biospectrometry™ with Universal Cone for ZipTip (cat. no. GEN602987) and Rack Adapter for the ZipTip box. 2. Bruker Daltonics MAP™ II and MAP™ II/8 MADLI Auto Prep Station 3. Micromass 2700-MS and MassPREP™ Sample Preparation Stations 4. Genomic Solutions ProMS™ Sample Preparation Station 5. Cy-Bio CyBi™ Well 96 automated pipettor 6. Packard BioScrences MultiPROBE 7. Tecan GENESIS Workstation
Can I use ZipTipC₁₈ or ZipTipµ-C₁₈ for amino acids?	ZipTipC₁₈ and ZipTipµ-C₁₈exhibit comparable binding properties to C₁₈ reversed-phase HPLC. As such, lower recoveries will be seen for hydrophilic amino acids. C₁₈ is offered in two bed volumes: ZipTipC₁₈ - a standard bed of 0.6 µL for sample elution in 1 to 4 µL ZipTipµ-C₁₈ - a micro bed of 0.2 µL for sample elution in < 1 µL.
Can ZipTip be reused?	ZipTip is intended for single use.
How are ZipTip pipette tips packaged?	ZipTip pipette tips are available in four pack sizes: 8 Pack Resealable Tray 24 Pack Resealable Tray 96 Pack 96 place tip rack 960 Pack 10 x 96 place tip rack
How can I elute from ZipTip pipette tips directly into a nanospray needle?	We suggest cutting a gel loading tip (Eppendorf 0030 001 222) approximately 2-3 mm above where the tip widens from the capillary end. ZipTip binding, washing and elution are performed utilizing the standard protocols listed in the ZipTip Reversed-Phase Operating Manual. Prior to the final dispense (elution of the peptide or protein) the cut down gel loading tip is pressed on to the end of the ZipTip using a slight twisting motion. The friction fit is tight, allowing sample to be dispensed directly into an nanospray needle. Refer to the ZipTip Reversed-Phase Operators Manual for a detailed diagram demonstrating the above procedure.
How can I improve binding of hydrophilic peptides and proteins to ZipTipC18, ZipTipµ-C18 and ZipTipC4?	Insure that TFA concentration is at least 0.1- 1% with minimal sample dilution. Detergents can interfere with sample binding, (especially with hydrophilic peptides). Dilute detergent to < 0.05%. Alternatively HFBA (heptafluorobutyric acid) may be used as the ion pairing agent. In some cases the peptide may be too hydrophilic for binding to the resin.
How can I improve salt removal with ZipTipC18, ZipTipµ-C18 or ZipTipC4?	Wash ZipTip with 3 to 5 aspirate/dispense cycles of 0.1% TFA (10 ml). If salt contamination persists, consider the following: For Peptides - Try washing peptides with 10% ACN (acetonitrile)/0.1% TFA. For proteins, the above ACN concentration can be increased to 30% Add 100 microliters of additional wash solution to a pipet and slowly push this solution through the Zip Tip. If the problem persists try blotting the Zip Tip on a paper towel to remove the residual wash soulution remainig in the Zip Tip after dispensing the final wash.
How do I process sample volumes larger than 10 ml through a ZipTip?	The entire volume of a sample should be passed through the ZipTip 5 times for sufficient binding. a ZipTip may be utilized on a P-100, P-200, P-500 or P-1000 pipettor by press fitting the ZipTip onto the end of an appropriate pipette tip. Please refer to ZipTip page on the Millipore WEB site.
How many times do I have to cycle the sample through ZipTip to achieve binding to the resin?	The ZipTip Operators Manual recommends to aspirate and dispense samples 3 to 7 cycles for simple mixtures and up to 10 cycles for complex mixtures to achieve maximum binding.
How quickly can I desalt and concentrate peptide, protein or oligonucleotide samples with ZipTip pipette tips?	ZipTip concentrates, and desalts samples in about one minute.

카테고리

Life Science Research > Protein Sample Preparation > Protein Concentration & Dialysis > Protein Concentrators

C5737Concentrating and purifying samples for MALDI-ToF MS

ZipTip Advantages:

Single-step desalting, concentration, and purification
Fractionate complex samples for more meaningful data
Ideal for peptides, proteins, nucleic acids, and more
No dead volume for maximum recovery
Eliminates time-consuming chromatography.

ZipTip is a 10 µL pipette tip with a 0.6 or 0.2 µL bed of chromatography media fixed at its end with no dead volume. It is ideal for concentrating and purifying samples for sensitive downstream analyses.

Examples of analyses enhanced by ZipTip sample preparation:

Mass spectrometry
HPLC (high performance liquid chromatography)
Capillary electrophoresis
Atomic absorption spectroscopy

The ZipTip pipette tip is simple and easy to use.

Place the tip on a single- or multi-channel pipettor, standard 22-gauge blunt-end HPLC needle, or compatible automated liquid handling/sample preparation station.
For sample binding, aspirate and dispense through the media several times.
Similarly, aspirate and dispense appropriate wash solvent to remove contaminants.
The concentrated, purified sample is eluted in 1–4 µL of compatible solvent with direct transfer to a mass spectrometer target, vial, or other analysis step.

For applications requiring smaller elution volumes (e.g., <1 µL), a micro-bed format containing 0.2 µL of media is available.

The ZipTip pipette tip provides a reproducible, high-recovery method for concentrating and purifying femtomoles to picomoles of peptides, proteins and oligonucleotides for improved analytical data. To simplify your analysis even further, you can, fractionate complex peptide mixtures by step elution.

Performance

MALDI MS spectra of a tryptic peptide digest from an in-gel 2D digest. The top spectra represents a contaminated sample prior to sample clean-up. The lower spectra represents the sample after using a ZipTipC18 prior to MALDI TOF MS analysis.

Choose From 3 Different ZipTip Resins:

Resin	Compatible Analytes
C₁₈ Resin (0.6 µL or 0.2 µL bed volumes)	Oligonucleotides or small (<50 kDa) proteins/peptides in aqueous solution
C₄ Resin	Proteins or peptides (3 kDa – 100 kDa) in aqueous solution
Strong cationic resin (SCX)	Peptides in solution with organic solvents or detergents

The ZipTip^® pipette tip is a 10 µL tip with a 0.6 or 0.2 µL bed of chromatography media fixed at its end. It is ideal for concentrating and purifying samples for sensitive analyses such as MALDI-ToF MS. The ZipTip^® pipette tip provides a reproducible, high-recovery method for concentrating and purifying femtomoles to picomoles of peptides, proteins and oligonucleotides for improved analytical data. To simplify your analysis even further, you can fractionate complex peptide mixtures by step elution.

Materials
Pipette Tip	Polypropylene
C₁₈ and µ-C₁₈ Resin	Silica, 15 µm, 200 Å pore size
C₄ Resin	Silica, 15 µm, 300 Å pore size
SCX Resin	Strong cation exchange, 12 µm, 300 Å pore size
Volumes, µL
Pipette tip	10 µL
Resin Bed	0.2 or 0.6
Capacity
ZipTip_C18	Typically 5 µg when used with saturating amounts of analyte
ZipTip_µ-C18	Typically 2.0 µg when used with saturating amounts of analyte
ZipTip_C4	Typically 3.3 µg when used with saturating amounts of analyte
Dimensions
Tip Length	31 mm
Tip ID (top)	3.375 mm
Tip OD (top)	5.8 mm
Temperature, °C	4至70 °C
pH Range	pH1.5 – pH13.5; pH2 – pH12 for 24 hour exposure

Recommended Equipment

Manual Liquid Handling:
ZipTip pipette tips are compatible with most 10 µL single-channel pipettors. The Biohit Proline® electronic multi-channel pipettor is recommended for simultaneously processing eight samples.
Automated Liquid Handling:
ZipTip pipette tips are also proven for use on a variety of automated liquid handling systems including:

ABI SymBiot® Sample Workstations for Biospectrometry™ with universal cone for ZipTip tips (ABI catalogue no. GEN602987) and rack adapter for ZipTip box
Genomic Solutions ProMS™ Sample Preparation Station
Bruker Daltonics MAP™ II and II/8 MALDI AutoPrep Systems with rack adapter for ZipTip box (Millipore catalogue no. ST0B DAP TR)
Tecan GENESIS Workstation
CyBio CyBi™-Well 96 Automated Pipettor

해당 제품은 고객님의 카트에 추가되었습니다.

ZipTip^® Pipette Tips

Concentrating and purifying samples for MALDI-ToF MS 더보기

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개요

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카테고리

ZipTip Advantages:

Examples of analyses enhanced by ZipTip sample preparation:

Performance

Choose From 3 Different ZipTip Resins:

Recommended Equipment

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