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RP-HPLC for Protein/Peptide Analysis and Purification The Jupiter HPLC column portfolio, including Jupiter 300 and Jupiter Proteo, offers optimized reversed phase solutions for protein and peptide characterization and purification. With these col-umns, one can identify, purify, and analyze almost any protein.

Jupiter 300 – 300 Å columns designed to analyze and purify intact proteins

For separation of intact proteins > 10,000 MW•

Available with C18, C5, and C4 bonded phases•

1.5 – 10 pH stability for method ruggedness and easy protein removal•

Direct scale-up to preparative and bulk materials•

Jupiter Proteo – 90 Å columns engineered for increased peak capacity and resolution of peptide maps as well as peptide separations

For separation of intact proteins and peptides < 10,000 MW•

Available with novel C12 bonded phase for excellent selectivity•

Identify post-translational modifications•

Capillary columns available for increased sensitivity•

Material Characteristics

Packing Material

ParticleShape/Size

(μm)

PoreSize(Å)

SurfaceArea

(m2/g)

CarbonLoad

%

Calculated Bonded Phase Coverage

(µmole/m2)End

CappingC4 Spher. 5, 10, 15 300 170 5.0 6.30 yesC5 Spher. 5, 10, 15 300 170 5.5 5.30 yesC18 Spher. 3, 5, 10, 15 300 170 13.3 5.50 yesProteo Spher. 4, 10 90 475 15.0 — yes

Dependable Solutions for Protein/Peptide Researchers Jupiter HPLC columns are used throughout the life science industry in a variety of departments. Phenomenex offers support and solutions in all areas of protein research and manufacturing, especially in characterization, purification, and proteomics/biomarker discovery.

Type of Work Key Applications

Protein Characterization•Identifypost-translationalmodifications•Analyzeintactantibodies•StudyPEGylatedproteins

Protein/ Peptide Purification

•Separatetargetcompoundfromimpurities•Purifyantibodies•Separateproteincomponentsfromoneanother•Easy,directscaleuptopreparativeandprocessscales

Proteomics/ Biomarker Discovery•Performpeptidemappingfordifferentialproteomics•Identifylowlevelproteinsutilizingcapillarycolumns•Excellentresinfor2nddimensionof2D-HPLC

(see pp. 182-184 for more information)

Jupiter®

If Jupiter analytical columns do not provide you with at least an equivalent separation as compared to a column of similar phase, particle size and dimension, send in your comparative data within 45 days and keep the Jupiter column for FREE.

179Phenomenex

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Engineered for Robustness, Reproducibility, and Quality It is tough to compete with Jupiter standards. Each column has consistent specifications and thus consistent performance.

pH 1.5-10 stability gives robust, method development •opportunities

Over 25 individual quality control tests performed on •every batch of Jupiter material

Every aspect of column reproducibility is specified, •tested, and reported in Materials Validation Document (MVD)

pH 1.5 – 10 StabilityA wide pH range means more than just longer column life; it means opportunity for method development. Jupiter columns are stable for over 2500 hours at pH extremes. Jupiter 300 and Jupiter Proteo provide excellent separations using various MS compatible buffers and provide good resolution down to 0.01% TFA.

Quality ProvenQuality is carefully maintained and traceability is assured through-out the manufacturing process. A Materials Validation Document (MVD) accompanies every Jupiter column. Each certificate con-tains information on the rigorous testing procedures performed on each batch of Jupiter material to ensure column-to-column and batch-to-batch reproducibility.

Reproducibility AssuredBatch-to-batch and column-to-column is a critical factor in HPLC column performance. Through great advances in silica, bonding, and material characterization technology, Jupiter columns set a new benchmark in reproducibility.

Batch 6

Batch 5

Batch 4

Batch 3

Batch 2

Batch 1

Effect of pH on Bradykinin Separation

pH 9.5

pH 4.0

pH 2.0

Conditions for all separations:

Column: Jupiter 300 5 μm C18 300 Å

Dimensions: 250 x 4.6 mmPart No.: 00G-4053-E0

Flow Rate: 1.0 mL/minDetection: UV @ 215 nm

Sample: 1. Bradykinin 2. Bombesin 3. Neurotensin 4. Eledoisin

pH stabilityEvery batch goes through 1.5 and 10.0 pH testing before release, the results of which are reported on each MVD.

Diagnostic chromatography testsMonitoring chromato-graphic specifications for silanol activity, hydrogen bonding ca-pacity, hydrophobicity and peptide standards.

Silica physical tests and specificationsPore size, particle size and distribution, metal content, surface area, carbon load and surface coverage specifications and results are all reported.

SEM analysisScanning Electron Microscopy (SEM) photos show surface smoothness and particle consistency as well as a visual rep-resentation of particle size distribution.

Stability of Jupiter 300 C18 at pH 1.5 and 10

Hours of ExposureTest Conditions: Column flushed

in 0.1 % TFA (pH 1.5) in Water/Acetonitrile (50:50)

Hours of ExposureTest Conditions: Column flushed

in 20 mM Na2HPO4 (pH 10.0) in Water/Acetonitrile (50:50)

App

ID 8

724

App ID 16658

Column: Jupiter 5 µm C18 300 Å Dimensions: 250 x 4.6 mm

Part No.: 00G-4053-E0Mobile Phase: A: 0.1 % TFA in Water

B: 0.1 % TFA in AcetonitrileGradient: A/B (75:25) to A/B (45:55)

in 15 minFlow Rate: 1.0 mL/minDetection: UV @ 220 nm

Sample: 1. yeast Cytochrome c 2. Equine Cytochrome c 3. Bovine Cytochrome c

Jupiter®

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Jupiter 300 – for Intact Protein Separation and PurificationJupiter 300 has proven its performance to biochromatographers worldwide as a leading 300 Å column in the market.

300 Å column for analysis and purification of proteins •> 10,000 MW

Highly efficient columns with long lifetime due to •super-smooth, high-mechanical-strength 300 Å silica

Excellent column for LC/MS due to low phase bleed and •exceptional performance at low buffer concentrations

Selecting the Appropriate 300 Å PhaseJupiter 300 C4 This low hydrophobicity phase is less likely to cause irreversible adsorption of “sticky” proteins and allows for the use of shallow gradients along with lower concentrations of organic solvent.

For proteins >10,000 Da•

For highly hydrophobic proteins•

Jupiter 300 C5 This bonded phase imparts greater pH stability compared to traditional C4 phase. One can expect longer column lifetimes and more stable, reproducible retention times because of the bonded phase’s increased stability to hydrolysis.

For proteins >10,000 Da•

For highly hydrophobic proteins•

More retentive than C4, offering slightly different selectivity•

Jupiter 300 C18 Excellent for polar as well as non-polar proteins; most retentive of Jupiter 300 phases, allowing one to separate proteins with slight differences in hydrophobicity

For proteins >10,000 Da•

For hydrophilic proteins•

Most retentive phase•

1

2

3

4

Large Proteins on Jupiter 300 C4

Column: Jupiter 300 5 μm C4 300ÅDimensions: 150 x 4.6 mm

Part No.: 00F-4167-E0Mobile Phase: A: 0.1 % TFA in Water

B: 0.08 % TFA in AcetonitrileGradient: A/B (95:5) to A/B (20:80) in 20 minutes

Flow Rate: 1 mL/minTemperature: 22 ˚C

Detection: UV @ 280 nmInj. Volume: 25 μL

Sample: 1. Bovine Serum Albumin2. Glutamic Dehydrogenase3. ß-Galactosidase4. Ovalbumin

App

ID 1

4761

1

0 2 4 6 8 10 12 14 16 18 min

2

3 4

5

0

200

400

800

600

mAU

Separation on Jupiter 300 C18

Column: Jupiter 300 5 µm C18 300 ÅDimensions: 150 x 2.0 mm

Part No.: 00F-4053-B0Mobile Phase: A: 0.1 %TFA/ 95 % Water / 5 % Acetonitrile

B: 0.085 % TFA/ 95 % Acetonitrile/ 5 % WaterGradient: A/B (88:12) to A/B (15:85) in 21 minutes

Flow Rate: 0.2 mL/minDetection: UV @ 220 nm

Sample: 1. Aprotinin2. Ribonuclease3. Lysozyme4. Lactalbumin5. Leptin

App

ID 1

4937

Sharp Peaks and High YieldsUltra-pure silica and dense bonded phase coverage provide sharp peaks for your sample by decreasing the number of non-specific interactions. Sharpened peak symmetry allows for easier quanti-tation, improved resolution, and separation of complex mixtures. High yields result in more material for downstream analysis, de-creased number of purification runs, and lower production costs.

Sharp Peaks for Easy Quantitation

Column: Jupiter 300 5 µm C4 300 ÅDimensions: 50 x 4.6 mm

Part No.: 00B-4167-E0Mobile Phase: A: 0.1% TFA in Water

B: 0.1% TFA in AcetonitrileGradient: A/B (100:0) to A/B (80:20) in 1 min

(20 % B/ min), then to A/B (65:35) in 1.5 min (10 % B/ min), then to A/B (53.5:46.5) in 1.5 min (7.67 % B/ min), hold for 2 min (constant B)

Flow Rate: 1 mL/minDetection: UV @ 220 nm

Sample: 1. Alkaline Phosphatase2. Cyanocobalamin 3. RNase4. Insulin5. Transferrin6. Trypsin Inhibitor

2.5 5 7.5 10 12.5 15 17.5 min

App

ID 5

378

min

Jupiter®

181Phenomenex

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Jupiter Proteo – for Peptide Mapping and Peptide Purification Separating peptide fragments by reversed phase chromatog-raphy is a standard method of protein analysis and is used to develop well-characterized biopharmaceuticals. In an effort to support proteomic research and the growth of the synthetic peptide industry, we have engineered a column with a sorbent and surface chemistry that successfully leverages the physical and chemical properties of polypeptides.

Novel 90 Å, C12 bonded phase optimized for peptide •mapping and the separation of synthetic peptides

Identify oxidation, deamidation, and other post-•translational modifications

Resolve peptides differing in hydrophobicity by one •methyl group

Identify More Peaks in Peptide Maps with Increased Peak Capacity Jupiter Proteo is designed to selectively separate and to op-timize information on peptide fragments obtained in a protein digest. In the example, a Jupiter Proteo column offers better selectivity and resolving power compared with a commercial 300 Å, silica-based C18 reversed phase column.

Method Threshold Peak Width Min Area Min Height

1 1.0 0.1 10.0 20.02 2.0 0.2 10.0 20.03 3.0 0.3 20.0 10.04 3.0 0.3 20.0 50.0

Selectivity to Improve ResolutionJupiter Proteo can be used to resolve peptides of MW < 10,000 Da and often is able to separate peptides of only 1-2 amino acid difference. By comparing the resolution of five peptide standards with amino acid sequences that differ in hydrophobicity by one methyl group each with respect to efficiency, selectivity, and resolution it is evident that Jupiter Proteo fully resolves each peptide.

Determining peak counts - The large number of peaks in a given tryptic digest makes counting peaks visually both inaccurate and subjective. For a more accurate approach, peak counting was performed using Agilent Technologies (HP) ChemStation™ software. Four different integration parameters at different sensitivity settings were used in calculating the number of peaks and an average. The parameters changed within each method were: minimum peak area, minimum peak height, peak width, and threshold. The table below describes the parameters used for each calculation.

Agilent Technologies ZoRbAX® 5 μm Sb-C18 300 Å

Methylene SelectivityConditions for all columns:

Dimensions: 250 x 4.6 mmMobile Phase: A: 0.1 % TFA in Water

B: 0.085 % TFA in AcetonitrileGradient: A/B (95:5) to

A/B (55:45) in 20 minutesFlow Rate: 1 mL/min

Temperature: 22 °CDetection: UV @ 214 nm

Sample: 1. NH2-Arg-Gly-Gly-Ala-Gly-Gly-Leu-Gly-Leu-Gly-Lys-Amide2. Ac-Arg-Gly-Gly-Gly-Gly-Gly-Leu-Gly-Leu-Gly-Lys-Amide3. Ac-Arg-Gly-Ala-Gly-Gly-Gly-Leu-Gly-Leu-Gly-Lys-Amide4. Ac-Arg-Gly-Val-Gly-Gly-Gly-Leu-Gly-Leu-Gly-Lys-Amide5. Ac-Arg-Gly-Val-Val-Gly-Gly-Leu-Gly-Leu-Gly-Lys-Amide

App

ID 1

4427

78 1 2 3 4 Avg.

118 72 71 49 78

78peaks

Agilent Technologies ZoRbAX® 5 μm Sb-C18 300 Å

48peaks

1 2 3 4 Avg.

54 51 50 35 48

App

ID 1

4411

App

ID 1

4408

Jupiter® 4 μm Proteo 90 Å

Alltech Associates Vydac® 5 μm MS54 300 Å

Alltech Associates Vydac® 5 μm TP54 300 ÅJupiter® 4 μm Proteo 90 Å

Conditions for all columns:Dimensions: 250 x 4.6 mm

Mobile Phase: A: 0.012 % TFA in WaterB: 0.01 % TFA in Acetonitrile

Gradient: A/B (95:5) for 5 min, then to A/B (60:40) in 55 minutes

Flow Rate: 1 mL/minTemperature: 22 °C

Detection: UV @ 210 nmSample: Myoglobin Tryptic Digest

Myoglobin Tryptic Digest

Jupiter®

App

ID 1

4428

App

ID 1

4429

App

ID 1

4426

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Protein CharacterizationProtein characterization is essential to fully understand metabolic and disease pathways in order to design therapeutics that are safe and efficacious. Phenomenex has several solutions for research-ers responsible for protein characterization ranging from antibody analysis to post-translational modification (PTM) monitoring.

Successfully analyze intact antibodies and their reduced •forms

Monitor PEGylation forms of protein therapeutics•

Identify unique peptide fragments and PTMs using LC/MS•

App

ID 1

4909

0

14909

2.5 5 7.5 10 12.5 15 17.5 min

Analyze Reduced IgG

Column: Jupiter 300 5 μm C4 300 ÅDimensions: 150 x 2.0 mm

Part No.: 00F-4167-B0Mobile Phase: A: 0.1 % TFA in Water/ Acetonitrile (95:5)

B: 0.085 % TFA in Water/ Acetonitrile/IPA (5:75:20)Gradient: A/B: 80:20 to A/B: 5:95 in 20 minutes

Flow Rate: 0.25 mL/minDetection: UV @ 220 nm

Sample: IgG Dog Reduced

Dog IgG was reduced with DTT and then analyzed using a Jupiter 300 C4 column. Baseline separation is achieved between the heavy and light chains.

Reversed phase separation of PEGylated and native proteins on a Jupiter 300 C4 column. Note the good resolution of multiple PEGylated forms for all proteins tested.

10 15 20

mAU

16191

400

0

800

1200

PEGylated Insulin

Insulin

PEGylated CarbonicAnhydrase II

PEGylated β-Lactoglobin A

β-Lactoglobin A

Carbonic Anhydrase II

min

App

ID 1

6191

Interferon-a must be analyzed for post-translational modifications (PTMs) caused by broken disulfide bonds. Peptide mapping using Jupiter 300 3 µm high efficiency HPLC columns easily identifies peak shifts of disulfide containing peptides which can be verified by MS.

Easily Monitor Post-translational Modifications (PTMs)

Column: Jupiter 4 μm Proteo 90 ÅDimensions: 250 x 4.6 mm

Part No.: 00G-4396-E0Mobile Phase: A: 0.012 % TFA in Water

B: 0.01 % TFA in AcetonitrileGradient: A/B (95:5) for 5 min, then to A/B (60:40) in 55

minutesFlow Rate: 1 mL/min

Temperature: 22 °CDetection: UV @ 210 nm

Sample: Top Chromatogram – ß-Lactoglobulin tryptic digestBottom Chromatogram – Oxidized ß-Lactoglobulintryptic digest

Oxidation is commonly seen with methionine due to its readily oxidized sulfur group. A tryptic digest of ß-Lactoglobulin easily reveals retention time changes due to the oxidation of methionine containing peptides.

10 20 30 40 min

Oxidation of b-Lactoglobulin

Control

OxidationProduct

App ID 14394-95

Disulfide Bridge Analysis of Human Interferon-aColumn: Jupiter 300 3 µm C18 300 Å

Dimensions: 150 x 2.0 mmPart No.: 00F-4263-B0

Mobile Phase: A: .01 % TFA + Acetonitrile in waterB: 0.085 % TFA + 90 % Acetonitrile in water

Gradient: A/B (99:1) in 35 min, then A/B (50:50) in 5 min, then A/B (20:80)

Flow Rate: 0.3 mL/minTemperature: 25 °C

Detection: UV @ 214 nmSample: Reduced Human Interferon-a

Non-reduced Human Interferon-a

min10 15 20 25 30 35

mAU

0

50

100

150

200

250

300

350

400

450

Reduced

Non-Reduced

App

ID 1

8072

Compare PEGylated vs. Native Forms of Proteins

Column: Jupiter 300 5 μm C4 300 ÅDimensions: 150 x 4.6 mm

Part No.: 00F-4167-E0Mobile Phase: A: 2 % Acetonitrile / 0.1 % TFA in Water

B: 70 % Acetonitrile / 20 % IPA / 0.08 % TFA in WaterGradient: A/B (85:15) to A/B (30:70) in 25 min

Flow Rate: 1.0 mL/minTemperature: 45 °C

Detection: UV @ 214 nmSample: PEGylated and Native Proteins

Jupiter®

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Protein/Peptide Purification Achieving adequate separation of proteins is one of the biggest challenges in chromatographic purification. Reversed phase HPLC offers a very high speed, high efficiency, and high resolution solution for protein purification. In addition, scale-up from ana-lytical to prep to process is easy and convenient with the several particle sizes and column dimensions available.

Purify proteins from their degradation produc• ts

Successfully purify target proteins and peptide •therapeutics

Easily scale-up from lab-scale to process-scale •purification

Insulin Purified From Its Degradants

Conditions for all columns:Column: Jupiter 4 μm Proteo 90 Å

Dimensions: 250 x 4.6 mmPart No.: 00G-4396-E0

Mobile Phase: A: 0.1 % TFA in WaterB: 0.085 % TFA in 95:5 Acetonitrile / Water

Gradient: A/B (80:20) to A/B (20:80) in 15 minutesFlow Rate: 1.0 mL/minDetection: UV @ 220 nm (ambient)

Sample: Human Insulin

1

23

2.5 5.0 7.5 10.0 12.5 15.0 17.5 min

0

200

400

600

800

1000

mAU

Separation of Insulin Genetic Variants

Column: Jupiter 300 5 μm C18 300 ÅDimensions: 250 x 4.6 mm

Part No.: 00G-4053-E0Mobile Phase: A: 0.1 % TFA in Water

B: 0.1 % TFA in AcetonitrileGradient: A/B (70:30) to A/B (68:32) in 20 min

Flow Rate: 1.0 mL/minDetection: UV @ 210 nm

Sample: 1. Bovine Insulin 2. Human Insulin 3. Porcine Insulin

Bovine, human, and porcine insulin were purified away from each other due to the strong resolving power of Jupiter 300 C18.

HPLC separations on Jupiter Proteo at different time points of insulin incubated under basic conditions at 60 °C. There was an increase of numerous degradation products with extended exposure at elevated temperature that Jupiter Proteo was able to separate.

Jupiter has excellent resolving power as seen in the above example. Resolution is extremely important, especially when impurities can differ by only a few amino acids.

Separate Key Components

0 2 4 6 8 10 12 14 16 min

0

200

400

mAU

1

23

4

5

Jupiter 300 5 µm C18 300 Å

1

23

4

5

0 2 4 6 8 10 12 14 16 min

0

200

400

mAU

Alltech Associates Vydac® 5 µm C18 300 Å

Purify Key Proteins From One Another

Conditions for all columns:Column: Jupiter 300 5 μm C18 300 Å

Vydac® 5 μm C18 300 Å (238EV52-Everest)Dimensions: 250 x 2.0 mm

Mobile Phase: A: 0.1 %TFA/ 95 % Water/ 5 % AcetonitrileB: 0.085 % TFA/ 95 % Acetonitrile/ 5 % Water

Gradient: A/B (80:20) to A/B (15:85) in 15 minutesFlow Rate: 0.2 mL/minDetection: UV @ 220 nm

Sample: 1. Aprotinin 2. Ribonuclease 3. Acid Glycoprotein 4. Fibrinogen 5. Leptin

2 4 6 8 10 min

0

200

400

mAU

15 min @ 60 ˚C

App

ID 1

4914

App

ID 5

372

App

ID 1

4924

-25

2 4 6 8 10 min

0

200

mAU

30 min @ 60 C˚

App

ID 1

4915

10 min

60 min @ 60 C˚

2

0

200

mAU

4 6 8

App

ID 1

4917

Easy Scale-Up with Prep Columns and Bulk Material Jupiter uses identical bonding and base silica technology in both analytical and preparative materials. Accordingly, Jupiter 300 ma-terial used in analytical separation is available in a 10 µm and 15 µm (Jupiter Proteo is available in 10 µm) version so you can easily scale-up with minimal changes to the separation.

Large loading capacity for higher sample recovery•

Easy material cleaning and regeneration•

Resistance to silica sheering and fine formation at high •packing pressures and flow rates

Jupiter®

10 μm C18 300 Å

Virgin Bulk Media

Jupiter®

10 μm C18 300 Å

After Packing

Jupiter®

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Biomarker discovery and proteomics research requires the right tools to identify promising biomarker candidates and to study proteins in depth. Jupiter materials and formats are reli-able tools for advancing your research.

Perform peptide mapping for differential proteomics•

Identify low level proteins utilizing capillary columns•

Excellent resin for 2nd dimension of 2D-HPLC•

Increase Sensitivity Using Capillary Formats Capillary-LC columns packed with Jupiter 300 and Jupiter Proteo materials provide the same characteristics as their respective analytical-sized columns, but with added sensitivity for microliter sample volumes. The high purity silica combined with proprietary bonding techniques produce dense bonded phase coverage to shield against silanol interaction. With few secondary chromatographic effects, Jupiter capillary-LC columns yield terrific peak shape and are compatible with reduced TFA concentration and other mass spec compatible mobile phase modifiers.

High sensitivity for low volume and mass limited •samples

Consistent performance under LC/MS compatible and •universal conditions

High efficiency 0.30 and 0.50 mm ID glass-lined columns•

App

ID 1

4336

0 10 20 30 40 min

Peak differences between various species and/or various diseased states can be identified using the Jupiter Proteo material.

(Bovine)

(Canine)

Column: Jupiter 4 μm Proteo 90 ÅDimensions: 250 x 4.6 mm

Part No.: 00G-4396-E0Mobile Phase: A: 0.12 % TFA in Water

B: 0.1 % TFA in AcetonitrileGradient: A/B (95:5) to A/B (45:55) in 50 min, then to A/B (5:95) in

5 min, then hold at A/B (5:95) for 5 min, then hold atA/B (95:5) for 5 minutes

Flow Rate: 1 mL/minDetection: UV @ 210 nm

Sample: Tryptic digest of Cytochrome c+ genetic variants – see chromatogram for species

App

ID 1

4682

The 90 Å Jupiter Proteo material gives increased peak capacity for tryptic digests due to its physical and chemical characteristics, which allows identifying more peptides in enzymatic digest samples.

High Peak Capacity for Tryptic Digest Conditions for both columns:

Dimensions: 250 x 4.6 mmMobile Phase: A: 0.012 % TFA in Water

B: 0.01 % TFA in AcetonitrileGradient: A/B (95:5) for 5 min, then to A/B (60:40)

in 55 minutesFlow Rate: 1 mL/min

Temperature: 22 °CDetection: UV @ 210 nm

Sample: Myoglobin Tryptic Digest

64peaks

78peaks

App

ID 1

4408

-09

Jupiter Proteo 4 µm C12 90 Å

Jupiter 300 5 µm C18 300 Å

Differential Proteomics Utilizing Tryptic Maps

Column: Jupiter 4 μm Proteo 90 ÅDimensions: 150 x 0.50 mm

Part No.: 00F-4396-AFMobile Phase: A: 0.01 % TFA in Water

B: 0.008 % TFA in AcetonitrileGradient: A/B (95:5) for 5 min then

A/B (55:45) in 45 min Switch to A/B (95:5) in 1 sec then hold for 10 min

Flow Rate: 15 µL/minTemperature: 40 °C

Detection: UV @ 210 nmSample: a - Chymotrypsin tryptic digest

a-Chymotrypsin Tryptic Digest on Jupiter Proteo

Jupiter®

Proteomics/Biomarker Discovery

185Phenomenex

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For Column Chiller/Heater System (8-70 °C), see p. 343

For Fused Silica Capillary Adapter, see p. 349

4 μm & 5 μm Capillary Columns (mm) Capillary Guard Columns (mm)Phases 50 x 0.30 150 x 0.30 250 x 0.30 50 x 0.50 150 x 0.50 250 x 0.50 20 x 0.30 20 x 0.50

5 μm C4 300 Å 00B-4167-AC 00F-4167-AC 00G-4167-AC 00B-4167-AF 00F-4167-AF — 03M-4167-AC 03M-4167-AF5 μm C18 300 Å 00B-4053-AC 00F-4053-AC 00G-4053-AC 00B-4053-AF 00F-4053-AF 00G-4053-AF 03M-4053-AC 03M-4053-AF4 μm Proteo 90 Å 00B-4396-AC 00F-4396-AC 00G-4396-AC 00B-4396-AF 00F-4396-AF 00G-4396-AF 03M-4396-AC —

Ordering Information

For SecurityGuard Cartridge Holders and Cartridges, see p. 244

Ordering Information

Effectively desalt acidic, basic, and neutral peptides with Strata-X. See p. 32 for more information.

**PREP SecurityGuard™ Cartridges require holder, Part No.: AJ0-8223PREP SecurityGuard™ Cartridges require holder, Part No.: AJ0-8277

*SecurityGuard™ Analytical Cartridges require holder, Part No.: KJ0-4282 ‡SemiPrep SecurityGuard™ Cartridges require holder, Part No.: AJ0-7220

Jupiter®

Bulk Material10 μm Bulk PackingsPhase 100 g 1 kg 5 kg 10 kg 50 kg 100 kg

Inquire Inquire Inquire Inquire Inquire Inquire

C4 300 Å 04G-4168 04K-4168 04L-4168 04M-4168 04N-4168 04P-4168C5 300 Å 04G-4054 04K-4054 04L-4054 04M-4054 04N-4054 04P-4054C18 300 Å 04G-4055 04K-4055 04L-4055 04M-4055 04N-4055 04P-4055Proteo 90 Å 04G-4397 04K-4397 04L-4397 04M-4397 04N-4397 04P-4397

15 μm Bulk PackingsPhases 100 g 1 kg 5 kg 10 kg 50 kg 100 kg

Inquire Inquire Inquire Inquire Inquire InquireC4 300 Å 04G-4169 04K-4169 04L-4169 04M-4169 04N-4169 04P-4169C5 300 Å 04G-4056 04K-4056 04L-4056 04M-4056 04N-4056 04P-4056C18 300 Å 04G-4057 04K-4057 04L-4057 04M-4057 04N-4057 04P-4057

3 μm, 4 μm & 5 μm Microbore and Minibore Columns (mm) SecurityGuard™ Cartridges (mm)Phases 50 x 1.0 150 x 1.0 250 x 1.0 50 x 2.0 150 x 2.0 250 x 2.0 4 x 2.0*

/10pk

5 μm C4 300 Å 00B-4167-A0 00F-4167-A0 00G-4167-A0 00B-4167-B0 00F-4167-B0 00G-4167-B0 AJ0-4329

5 μm C5 300 Å 00B-4052-A0 00F-4052-A0 00G-4052-A0 00B-4052-B0 00F-4052-B0 00G-4052-B0 AJ0-4326

5 μm C18 300 Å 00B-4053-A0 00F-4053-A0 00G-4053-A0 00B-4053-B0 00F-4053-B0 00G-4053-B0 AJ0-4320

4 μm Proteo 90 Å 00B-4396-A0 00F-4396-A0 00G-4396-A0 00B-4396-B0 00F-4396-B0 00G-4396-B0 AJO-6073— — — — /10pk

3 μm C18 300 Å — — — 00B-4263-B0 00F-4263-B0 — AJ0-4320for ID: 2.0-3.0 mm

3 μm, 4 μm & 5 μm Analytical and Preparative Columns (mm) SecurityGuard™ Cartridges (mm)Phases 50 x 4.6 150 x 4.6 250 x 4.6 250 x 10 250 x 21.2 4 x 3.0* 10 x 10‡ 15 x 21.2**

/10pk /3pk /ea5 μm C4 300 Å 00B-4167-E0 00F-4167-E0 00G-4167-E0 00G-4167-N0 00G-4167-P0 AJ0-4330 AJ0-7225 AJ0-72315 μm C5 300 Å 00B-4052-E0 00F-4052-E0 00G-4052-E0 00G-4052-N0 00G-4052-P0 AJ0-4327 AJ0-7371 —5 μm C18 300 Å 00B-4053-E0 00F-4053-E0 00G-4053-E0 00G-4053-N0 00G-4053-P0 AJ0-4321 AJ0-7224 AJ0-72304 μm Proteo 90 Å 00B-4396-E0 00F-4396-E0 00G-4396-E0 00G-4396-N0 00G-4396-P0 AJ0-6074 AJ0-7275 AJ0-7842

— — — /10pk — —

3 μm C18 300 Å — 00F-4263-E0 00G-4263-E0 — — AJ0-4321 — —for ID: 3.2-8.0 mm 9-16 mm 18-29 mm

For Jupiter Proteo Axia Packed Preparative columns, see pp. 310-311

15 μm Analytical and Preparative Columns (mm) SecurityGuard™ Cartridges (mm)Phases 250 x 4.6 250 x 10 250 x 21.2 250 x 30 250 x 50 4 x 3.0* 10 x 10‡ 15 x 21.2** 15 x 30.0♦

Inquire Inquire /10pk /3pk /ea /ea

C4 300 Å 00G-4169-E0 00G-4169-N0 00G-4169-P0 00G-4169-U0 00G-4169-V0 AJ0-4330 AJ0-7225 AJ0-7231 AJ0-8314

C5 300 Å 00G-4056-E0 00G-4056-N0 00G-4056-P0 — 00G-4056-V0 AJ0-4327 AJ0-7371 — —

C18 300 Å 00G-4057-E0 00G-4057-N0 00G-4057-P0 00G-4057-U0 00G-4057-V0 AJ0-4321 AJ0-7224 AJ0-7230 AJ0-8313for ID: 3.2-8.0 mm 9-16 mm 18-29 mm 30-49 mm

10 μm Analytical and Preparative Columns (mm) SecurityGuard™ Cartridges (mm)Phases 250 x 4.6 250 x 10 250 x 21.2 250 x 30 250 x 50 4 x 3.0* 10 x 10 ‡ 15 x 21.2** 15 x 30.0♦

Inquire Inquire /10pk /3pk /ea /eaC4 300 Å 00G-4168-E0 00G-4168-N0 00G-4168-P0 00G-4168-U0 00G-4168-V0 AJ0-4330 AJ0-7225 AJ0-7231 AJ0-8314C5 300 Å 00G-4054-E0 00G-4054-N0 00G-4054-P0 — 00G-4054-V0 AJ0-4327 AJ0-7371 — —C18 300 Å 00G-4055-E0 00G-4055-N0 00G-4055-P0 00G-4055-U0 00G-4055-V0 AJ0-4321 AJ0-7224 AJ0-7230 AJ0-8313Proteo 90 Å 00G-4397-E0 00G-4397-N0 — — — AJ0-6074 AJ0-7275 AJ0-7842 AJ0-8304

for ID: 3.2-8.0 mm 9-16 mm 18-29 mm 30-49 mm

If Jupiter analytical columns do not provide you with at least an equivalent separation as compared to a column of similar phase, particle size and dimension, send in your comparative data within 45 days and keep the Jupiter column for FREE.

Bulk Material10 μm Bulk PackingsPhase 100 g 1 kg 5 kg 10 kg 50 kg 100 kg

C4 300 Å 04G-4168 04K-4168 04L-4168 04M-4168 04N-4168 04P-4168C5 300 Å 04G-4054 04K-4054 04L-4054 04M-4054 04N-4054 04P-4054C18 300 Å 04G-4055 04K-4055 04L-4055 04M-4055 04N-4055 04P-4055Proteo 90 Å 04G-4397 04K-4397 04L-4397 04M-4397 04N-4397 04P-4397

15 μm Bulk PackingsPhases 100 g 1 kg 5 kg 10 kg 50 kg 100 kg

C4 300 Å 04G-4169 04K-4169 04L-4169 04M-4169 04N-4169 04P-4169C5 300 Å 04G-4056 04K-4056 04L-4056 04M-4056 04N-4056 04P-4056C18 300 Å 04G-4057 04K-4057 04L-4057 04M-4057 04N-4057 04P-4057

15 μm Analytical and Preparative Columns (mm) SecurityGuard™ Cartridges (mm)Phases 250 x 4.6 250 x 10 250 x 21.2 250 x 30 250 x 50 4 x 3.0* 10 x 10‡ 15 x 21.2** 15 x 30.0♦

/10pk /3pk /ea /ea

C4 300 Å 00G-4169-E0 00G-4169-N0 00G-4169-P0 00G-4169-U0 00G-4169-V0 AJ0-4330 AJ0-7225 AJ0-7231 AJ0-8314

C5 300 Å 00G-4056-E0 00G-4056-N0 00G-4056-P0 — 00G-4056-V0 AJ0-4327 AJ0-7371 — —

C18 300 Å 00G-4057-E0 00G-4057-N0 00G-4057-P0 00G-4057-U0 00G-4057-V0 AJ0-4321 AJ0-7224 AJ0-7230 AJ0-8313for ID: 3.2-8.0 mm 9-16 mm 18-29 mm 30-49 mm

10 μm Analytical and Preparative Columns (mm) SecurityGuard™ Cartridges (mm)Phases 250 x 4.6 250 x 10 250 x 21.2 250 x 30 250 x 50 4 x 3.0* 10 x 10 ‡ 15 x 21.2** 15 x 30.0♦

/10pk /3pk /ea /eaC4 300 Å 00G-4168-E0 00G-4168-N0 00G-4168-P0 00G-4168-U0 00G-4168-V0 AJ0-4330 AJ0-7225 AJ0-7231 AJ0-8314C5 300 Å 00G-4054-E0 00G-4054-N0 00G-4054-P0 — 00G-4054-V0 AJ0-4327 AJ0-7371 — —C18 300 Å 00G-4055-E0 00G-4055-N0 00G-4055-P0 00G-4055-U0 00G-4055-V0 AJ0-4321 AJ0-7224 AJ0-7230 AJ0-8313Proteo 90 Å 00G-4397-E0 00G-4397-N0 — — — AJ0-6074 AJ0-7275 AJ0-7842 AJ0-8304

for ID: 3.2-8.0 mm 9-16 mm 18-29 mm 30-49 mm