Sephadex G 200 is a hydrophilic gel that could be utilized as gel filtration packing (particle size range: 40-120 μm; globular protein separation range: 5k-600k Da).

Physicochemical Properties

Exact Mass	2251.65
CAS #	9041-36-5
Related CAS #	Sephadex G 50;9048-71-9;Sephadex G 100;9050-94-6;Sephadex G 15;11081-40-6;Sephadex G 10;9050-68-4;Sephadex G 150;12774-36-6
PubChem CID	168010037
Appearance	White to off-white solid powder
Hydrogen Bond Donor Count	5
Hydrogen Bond Acceptor Count	36
Rotatable Bond Count	5
Heavy Atom Count	163
Complexity	2630
Defined Atom Stereocenter Count	0
InChi Key	XDTNUBTXHWPZST-UHFFFAOYSA-N
InChi Code	InChI=1S/2C24H20ClN3O4.C24H20F2N4O3.2C24H19F2N3O4/c2*25-18-10-6-9-17-20(16-7-2-1-3-8-16)28-15-26(12-4-5-14-32-23(17)18)24(31)21-22(30)19(29)11-13-27(21)28;25-17-8-4-7-16-15(17)6-2-1-3-12-28-14-30(21(16)18-9-5-10-20(26)27-18)29-13-11-19(31)23(32)22(29)24(28)33;2*25-17-9-8-16-20(15-6-2-1-3-7-15)29-14-27(11-4-5-13-33-23(16)19(17)26)24(32)21-22(31)18(30)10-12-28(21)29/h2*1-11,13,20,30H,12,14-15H2;1,3-5,7-11,13,21,32H,2,6,12,14H2;2*1-10,12,20,31H,11,13-14H2
Chemical Name	7-chloro-17-hydroxy-2-phenyl-9-oxa-1,14,21-triazatetracyclo[12.7.1.03,8.016,21]docosa-3(8),4,6,11,16,19-hexaene-15,18-dione;6,7-difluoro-17-hydroxy-2-phenyl-9-oxa-1,14,21-triazatetracyclo[12.7.1.03,8.016,21]docosa-3(8),4,6,11,16,19-hexaene-15,18-dione;7-fluoro-2-(6-fluoropyridin-2-yl)-17-hydroxy-1,14,21-triazatetracyclo[12.7.1.03,8.016,21]docosa-3(8),4,6,11,16,19-hexaene-15,18-dione
HS Tariff Code	2934.99.9001
Storage	Powder-20°C 3 years 4°C 2 years In solvent -80°C 6 months -20°C 1 month Note: Please store this product in a sealed and protected environment, avoid exposure to moisture.
Shipping Condition	Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)

Biological Activity

References	[1]. Ogston AG, et al. The thermodynamics of interaction between Sephadex and penetrating solutes. Biochem J. 1970 Jan;116(2):171-5.
Additional Infomation	See also: Oils, Osmanthus fragrans (annotation moved to).

Solubility Data

Solubility (In Vitro)

May dissolve in DMSO (in most cases), if not, try other solvents such as H2O, Ethanol, or DMF with a minute amount of products to avoid loss of samples

Solubility (In Vivo)

Dextran Gel G Series Instructions for Use 1. Chemical and Physical Properties Dextran Gel is a beaded gel containing a large number of hydroxyl groups, allowing it to swell readily in water and electrolyte solutions. The hydrophilic matrix minimizes non-specific adsorption and provides high recovery rates during biomolecule separation. G-type Dextran Gels have varying degrees of cross-linking, resulting in different swelling degrees and fractionation ranges. The swelling degree of Dextran Gel is essentially unaffected by the presence of salts or detergents. 2. Product Specifications Product Name Globular Protein Separation Range Applications Max Pressure Resistance (MPa) Dextran Gel G-10 <700 Buffer exchange, desalting, separation of small molecules, removal of small molecules 0.15 Dextran Gel G-15 <1500 Buffer exchange, desalting, separation of small molecules, removal of small molecules 0.15 Dextran Gel G-25 1000-5000 Industrial desalting and buffer exchange 0.15 Dextran Gel G-50 1000-30000 Peptide separation, desalting, purification of biological extracts, molecular weight determination 0.10 Dextran Gel G-75 2000-70000 Protein separation and purification, molecular weight determination, equilibrium constant determination 0.016 Dextran Gel G-100 2000-120000 Protein separation and purification, molecular weight determination, equilibrium constant determination 0.0096 Dextran Gel G-150 5000-300000 Protein separation and purification, molecular weight determination, equilibrium constant determination 0.0096 Dextran Gel G-200 5000-600000 Protein separation and purification, molecular weight determination, equilibrium constant determination 0.0096 3. Usage Instructions Sephadex series products are supplied as dry powders and must be swollen before use. Avoid excessive stirring during swelling as it may damage the packing material. Do not use magnetic stirrers. 3.1 Packing Material Preparation (1) Swell the packing material in an excess of deionized water or buffer at room temperature for 24 hours, or in hot water for 1 hour (Not in a water bath!). The elution buffer should not contain high-viscosity reagents. If floating matter appears on the upper layer during swelling, remove it. (2) Equilibrate the swollen packing material and all buffers to the experimental operating temperature. Degas all buffers. 3.2 Column Packing (1) Inspect all column components, especially the filter screen, sealing ring, and screw plug for tightness. Ensure the glass tube is clean and intact. (2) Wet the column interior and bottom end with water or buffer, maintaining a small liquid level. Ensure no air bubbles are present at the bottom. (3) Use a glass rod to guide the slurry into the column along the inner wall in one continuous pour, avoiding bubble formation. Open the column outlet to allow the gel to settle freely within the column. Connect the top column end fitting securely. (4) Start the peristaltic pump and allow buffer to flow through the column at 1.33 times the operating flow rate to stabilize the bed (Ensure pressure does not exceed the maximum pressure resistance of the packing material). 3.3 Equilibration Equilibrate the column with at least 5-10 column volumes (CV) of buffer before sample application until the recorder baseline stabilizes (i.e., the pH and conductivity of the effluent equal those of the application buffer). 3.4 Sample Application Samples must be centrifuged or filtered (0.45 µm filter) before application. For gel filtration, the sample volume is generally no more than 5% of the bed volume. For initial runs, it is recommended to load 1-2% of the bed volume and adjust based on separation results. For desalting, sample volumes up to 20% of the bed volume can be applied. Column height also affects separation; taller columns provide better resolution but cause higher backpressure and should be avoided if possible. Challenging separations require adequate column height and flow rate control. For desalting, a height-to-diameter ratio of 5:1 is sufficient. 3.5 Elution Method Elution can be performed using salt-free water or the buffer used during column packing. 3.8 Cleaning In Place (CIP) Perform CIP after every ten uses to remove precipitated and stubbornly adsorbed proteins. Method: Wash with 0.1 M NaOH for 2 column volumes (CV), followed by regeneration with at least 10 CV of equilibration buffer. 4. Storage Untreated Packing Material:Store sealed at room temperature. Used Packing Material:Thoroughly rinse out salts with pure water. Finally, store in 20% ethanol at 4°C. 5. Precautions a) Before sample application, samples must be membrane-filtered and decolorized. Otherwise, impurities and pigments may adsorb onto the packing material, affecting its performance. All buffers must be filtered through a 0.45 µm filter. b) Avoid using high concentrations of strong acids or bases during operation. Acid and alkali concentrations should be below 0.1 M. Alkali solutions can reduce flow rates. c) Adsorption and elution methods differ for different samples. Consult relevant literature for specific protocols. 6. Particle Size Specifications Fine Particles:Slow flow rate, optimal separation resolution. Coarse Particles:Fast flow rate, reduced separation resolution. Medium Particles:Moderate flow rate, moderate separation resolution. This type is most commonly selected by customers.  (Please use freshly prepared in vivo formulations for optimal results.)