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GE17-5079-02

HiTrap® rProtein A Fast Flow

Cytiva 17-5079-02, pack of 2 × 1 mL

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About This Item

UNSPSC Code:
23151816
NACRES:
NA.56

ligand

recombinant protein A (E. coli)

packaging

pack of 2 × 1 mL

manufacturer/tradename

Cytiva 17-5079-02

storage condition

(20% Ehtanol)
(20% Ethanol)

parameter

<4 mL/min flow rate
42 psi

bed size

7 mm × 25 mm

bed volume

1 mL

column I.D.

7 mm

matrix

4% cross-linked agarose

particle size

60-165 μm

average diameter

90 μm (d50v)

cleaning

2-11

working range

3-10

capacity

~50 mg binding capacity (human lgG/ml medium)

suitability

suitable for bioprocess medium

storage temp.

2-8°C

Related Categories

General description

Capacity of HiTrap rProtein A for some monoclonal antibodies. Running conditions: Binding buffer: 20 mM sodium phosphate (incl. 3 M NaCl for IgG), pH 7.0. Elution buffer: 0.1 M sodium citrate, pH 3.0.
HiTrap® rProtein A FF columns are prepacked with rProtein A Sepharose Fast FLow for purification and fractionation of IgG subclasses and IgG from different sources, including cell supernatants and ascites.
pH below 3 is sometimes required to elute strongly bound IgG species. However, protein ligands may hydrolyze at very low pH.

Application

The recombinant Protein A ligand (produced in E. coli) is coupled to Sepharose Fast FLow by a technique which generates a stable thioether linkage between rProtein A and the base matrix. The coupling technique is optimized to give high binding capacity for IgG.

Features and Benefits

  • Quick, convenient preparative purification of monoclonal antibodies.
  • Well-established Protein A-based medium used in many approved MAb processes.
  • Recombinant Protein A exhibits similar Fc region specificity to that of native Protein A but shows enhanced binding capacity and fewer regulatory concerns due to the total absence of mammalian culture in the ligand production and purification.
  • Simple operations with a syringe, pump, or high-performance chromatography system, such as ÄKTA® design.

Storage and Stability

Please be aware this product may be shipped 90 days before the expiration date. For more information on the batch specific expiration date, please contact technical service.

Analysis Note

To view the Certificate of Analysis for this product, please visit www.cytiva.com.

Other Notes

The pressure over the packed bed varies depending on a range of parameters such as the characteristics of the chromatography medium and the column tubing used.

Legal Information

HiTrap is a registered trademark of Cytiva
Sepharose is a trademark of Cytiva
ÄKTA is a registered trademark of Cytiva

Pictograms

Flame

Signal Word

Warning

Hazard Statements

Storage Class Code

3 - Flammable liquids


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Articles

This page shows how to purify IgM antibodies by affinity chromatography using HiTrap™ IgM Purification HP.

This page shows how to separate IgG antibodies by affinity chromatography using HiTrap® Protein G HP columns from Cytiva.

This page shows various purification options for Protein A Sepharose chromatography media and describes typical binding and elution conditions for Protein A Sepharose chromatography media.

This page shows how to solve practical problems that may occur when running an affinity chromatography column.

Protocols

Protein A is derived from a strain of Staphylococcus aureus and contains five regions that bind to the Fc region of IgG. As an affinity ligand, protein A is coupled to Sepharose so that these regions are free to bind IgG.

This page shows how to convert between linear flow and volumetric flow rates in affinity chromatography.

How to perform buffer exchange and desalting with Sephadex G-25, HiTrap Desalting columns, or ÄKTAprime plus.

This page shows how to perform column packing and preparation for affinity chromatography when using Tricorn™ or XK columns available from Cytiva.

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