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Sigma-Aldrich

Thrombin CleanCleave Kit

Synonym(s):

Thrombin Cleavage Kit

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.56

form

suspension

mol wt

37 kDa

technique(s)

protein purification: suitable

shipped in

wet ice

storage temp.

2-8°C

General description

The Thrombin CleanCleave Kit contains a 50% suspension fo thrombin-agarose produced by immobilizing bovine thrombin and is designed for cleavage of recombinant fusion proteins

Application

For cleaving a tag from a recombinant fusion protein which contains the thrombin recognition sequence. Thrombin-agarose is compatible with recombinant proteins expressed in various types of expression systems.

Features and Benefits

  • Fast, efficient cleavage in as little as 2 hours
  • Thrombin is covalently bound to agarose for easy removal.
  • The robust cleavage reaction is effective at temperatures from 4 °C to 37 °C and over a wide range of pH and ionic strengths.
  • Cleave tags even in the presence of 0.1% Triton, 1 M urea or 5 mM EDTA
  • Thrombin-agarose is reusable.

Quantity

200 μl of a 50% slurry of thrombin-agarose cleaves >85% of 1 mg of fusion protein.

Legal Information

CleanCleave is a trademark of Sigma-Aldrich Co. LLC
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow

Kit Components Only

Product No.
Description

  • Thrombin Cleavage Buffer, 10× 10 mL

related product

Product No.
Description
Pricing

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Linda J Urbanski et al.
Journal of enzyme inhibition and medicinal chemistry, 35(1), 1834-1839 (2020-09-26)
This paper presents the production and kinetic and inhibitory characterisation of β-carbonic anhydrase from the opportunistic bacterium Staphylococcus aureus (SauBCA). From the eight different carbonic anhydrase (CA) families known to date, humans have only the α-form, whereas many clinically relevant
Linda J Urbański et al.
Applied microbiology and biotechnology, 106(11), 4065-4074 (2022-05-26)
We report the production and biochemical characterization of an α-carbonic anhydrase (LrhCA) from gram-positive probiotic bacteria Lactobacillus rhamnosus GG. CAs form a family of metalloenzymes that catalyze hydration of CO2/interconversion between CO2 and water to bicarbonate ions and protons. They
Robin Levy et al.
Biomolecules, 9(3) (2019-03-06)
The disordered p53 transactivation domain (p53TAD) contains specific levels of transient helical secondary structure that are necessary for its binding to the negative regulators, mouse double minute 2 (Mdm2) and MdmX. The interactions of p53 with Mdm2 and MdmX are
Andrea Angeli et al.
Journal of enzyme inhibition and medicinal chemistry, 36(1), 758-763 (2021-03-16)
We report the first activation study of the β-class carbonic anhydrase (CA, EC 4.2.1.1) encoded in the genome of the protozoan pathogen Trichomonas vaginalis, TvaCA1. Among 24 amino acid and amine activators investigated, derivatives incorporating a second carboxylic moiety, such
Carlos Alvarado et al.
Molecules (Basel, Switzerland), 24(18) (2019-09-22)
The Focal Adhesion Targeting (FAT) domain of Focal Adhesion Kinase (FAK) is a promising drug target since FAK is overexpressed in many malignancies and promotes cancer cell metastasis. The FAT domain serves as a scaffolding protein, and its interaction with

Articles

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Protocols

This page how to remove GST tags by enzymatic cleavage using Cytiva products.

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