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Sigma-Aldrich

Thrombin CleanCleave™ Kit

Sinónimos:

Thrombin Cleavage Kit

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About This Item

Código UNSPSC:
12352200
NACRES:
NA.56

Formulario

suspension

Nivel de calidad

200

mol peso

37 kDa

técnicas

protein purification: suitable

Condiciones de envío

wet ice

temp. de almacenamiento

2-8°C

Descripción general

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

Aplicación

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.

Características y beneficios

  • 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.

Cantidad

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

Información legal

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

Solo componentes del kit

Referencia del producto
Descripción
  • Thrombin Cleavage Buffer, 10× 10 mL

Producto relacionado

Referencia del producto
Descripción
Precios

08168

Timestrip Plus™ 8 °C

Código de clase de almacenamiento

10 - Combustible liquids

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

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Certificados de análisis (COA)

Lot/Batch Number
0000395426
0000395426
0000331150
0000327823
0000327828

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Claudia H Huichalaf et al.
Human molecular genetics, 28(12), 2014-2029 (2019-02-13)
An early hallmark of Alzheimer's disease is the accumulation of amyloid-β (Aβ), inspiring numerous therapeutic strategies targeting this peptide. An alternative approach is to destabilize the amyloid beta precursor protein (APP) from which Aβ is derived. We interrogated innate pathways
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
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
Bhavna Chawla et al.
PloS one, 7(3), e33138-e33138 (2012-03-23)
Deoxyhypusine hydroxylase (DOHH) catalyzes the final step in the post-translational synthesis of an unusual amino acid hypusine (N(€)-(4-amino-2-hydroxybutyl) lysine), which is present on only one cellular protein, eukaryotic initiation factor 5A (eIF5A). We present here the molecular and structural basis
Jolanta Krucinska et al.
Biochemistry, 58(9), 1188-1197 (2019-02-05)
Enolase is a glycolytic metalloenzyme involved in carbon metabolism. The advantage of targeting enolase lies in its essentiality in many biological processes such as cell wall formation and RNA turnover and as a plasminogen receptor. We initially used a DARTS
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