accessibility menu, dialog, popup

UserName
Viewing profile as user:

Miscellaneous Immobilized Affinity Ligands

Agarose beads and other resins bound to specialized immobilized ligands for use in diverse affinity procedures; ligands may include biotin, poly(e-lysine), lectins, metal ions, ribonucleotides, heparin, etc.; suitable for target molecule purification.
Product Line 
  • (22)
  • (6)
  • (1)
  • (30)
Type 
  • (6)
  • (6)
  • (2)
  • (4)
  • (31)
  • (10)
Capacity (Metric) 
  • (2)
  • (2)
  • (4)
  • (22)
  • (16)
Form 
  • (20)
  • (23)
  • (2)

Filtered Search Results

Products from some of our suppliers do not display in filtered search results. Please clear all filters to see these products.

Narrow Results

Narrow Results

No results found within this category. Try removing some selected filters and try again.

category

brands

  • (1)
  • (2)
  • (1)
  • (4)
  • (2)
  • (3)
  • (22)
  • (1)
  • (4)
  • (1)
  • (4)
  • (7)
  • (4)
  • (1)
  • (13)
  • (36)

special interests

  • (2)
  • (8)
  • (22)
  • (35)

special offers

  • (29)
  • (29)

Product Line

  • (22)
  • (6)
  • (1)
  • (30)

Type

  • (6)
  • (6)
  • (2)
  • (4)
  • (31)
  • (10)

Capacity (Metric)

  • (2)
  • (2)
  • (4)
  • (22)
  • (16)

Form

  • (20)
  • (23)
  • (2)
16 – 30 of 105 results
16
Promotions Available

Invitrogen™ EK-Away™ Resin

Specifically designed for removal of EKMaxor other enterokinase enzymes following cleavage of proteins containing the enterokinase cleavage site

ENCOMPASS_PREFERRED
Stationary Phase Enterokinase
Type Resin
Content And Storage EK-Away™ is provided as a 50% ethanol slurry and should be stored at +4°C. 10X binding and 10X stripping buffers are included. 7.5 ml resin will remove 250 units of enterokinase; 30 ml will remove 1000 units of EKMax™. All reagents are guaranteed stable for 6 months when stored properly.
Form Liquid Suspension
Column Type Affinity
Product Line EK-Away™
17

Thermo Scientific™ Detoxi-Gel™ Endotoxin Removing Columns, 1 mL

Bind and extract endotoxins (lipopolysaccharides or LPS) from antibody or protein samples using bulk resin or columns of immobilized Polymixin B ligand.

18

Promega HaloTag™ PEG-Biotin Ligand

The HaloTag™ Technology enables covalent protein labeling and immobilization in vivo and in vitro.

19

Promega HaloTag™ NanoBRET™ 618 Ligand

NanoBRET Transcriptional Protein Assays are sensitive, reproducible live-cell assays designed for monitoring or screening the interaction of proteins involved in transcriptional regulation.

20

Promega HaloTag™ Coumarin Ligand

The HaloTag™ Technology enables covalent protein labeling and immobilization in vivo and in vitro.

21

Promega HaloTag™ Biotin Ligand

The HaloTag™ Technology enables covalent protein labeling and immobilization in vivo and in vitro.

22

G-Biosciences Immobilized L-Lysine
SCI_ED

Immobilized L-Lysine Resin Column is used for purification of amino acid binding proteins.

23

G-Biosciences Immobilized D-Alanine
SCI_ED

Immobilized D-Alanine Resin Column is used for purification of amino acid binding proteins.

24

G-Biosciences Immobilized L-Glycine
SCI_ED

Immobilized L-Glycine Resin Column is used for purification of amino acid binding proteins.

25

G-Biosciences Immobilized L-Glutamic Acid
SCI_ED

Immobilized L-Glutamic Acid Resin Column is used for purification of amino acid binding proteins.

26

G-Biosciences Immobilized L-Serine
SCI_ED

Immobilized L-Serine Resin Column is used for purification of amino acid binding proteins.

27

G-Biosciences Immobilized L-Tyrosine
SCI_ED

Immobilized L-Tyrosine Resin Column is used for purification of amino acid binding proteins.

28

G-Biosciences Immobilized Poly-L-Lysine
SCI_ED

Immobilized Poly-L-Lysine Resin Column is used for purification of amino acid binding proteins.

29

G-Biosciences Immobilized L-Asparagine
SCI_ED

Immobilized L-Asparagine Resin Column is used for purification of amino acid binding proteins.

30

G-Biosciences Immobilized L-Leucine
SCI_ED

Immobilized L-Leucine Resin Column is used for purification of amino acid binding proteins.