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| Talla/SKU | Disponibilidad | Precio |
|---|---|---|
50 units | Póngase en contacto con nuestro Servicio de Atención al Cliente para disponibilidad | 466,00 € |
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Número CAS:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-761-1
NACRES:
NA.56
MDL number:
Biological source:
bovine
Recombinant:
expressed in Pichia pastoris
466,00 €
Póngase en contacto con nuestro Servicio de Atención al Cliente para disponibilidad
Servicio técnico
¿Necesita ayuda? Nuestro equipo de científicos experimentados está aquí para ayudarle.
Permítanos ayudarleQuality Segment
biological source
bovine
recombinant
expressed in Pichia pastoris
form
powder
mol wt
42.3 kDa (+/- 6.4 kDa)
color
white
shipped in
dry ice
storage temp.
−20°C
General description
Enterokinase also referred to as enteropeptidase, is a transmembrane protein. The amino-terminal sequence of the bovine enteropeptidase is homologous to trypsin-like serine proteases. Enterokinase is a highly specific serine protease that is used for the removal of the FLAG peptide from N-terminal and Met-N-terminal fusion proteins. It does not remove the C-terminal FLAG.
Application
Enterokinase from bovine intestine has been used to remove S-Tag and N-terminal His-tag from recombinant glutathione peroxidase 1 (Gpx1). It has also been used to cleave interleukin-2 (IL-2) protein from the granules
Enterokinase is a member of the S1 peptidase family. In vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. Enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags.
Biochem/physiol Actions
Enterokinase catalyzes the proteolytic activation of pancreatic proteases. This action prevents the harmful tissue damage produced by the autoactivation of pancreatic proteases in the pancreas. Enterokinase recognizes Lys or Arg residues in the peptide. Lack of enterokinase can harm food digestion and absorption mechanism. Enterokinase is a highly specific serine protease that is used for the removal of the FLAG peptide from N-terminal and Met-N-terminal fusion proteins. It does not remove the C-terminal FLAG.
Packaging
Supplied with optimized enterokinase buffer
Other Notes
Do not used PVDF since free FLAG peptide will bind to the PVDF membrane.
One unit is that amount of enterokinase which results in >95% cleavage of 1 µg of purified FLAG-BAP fusion protein in 18 hours at 37 °C. One FLAG-BAP unit is equal to 10x the activity of a standard trypsinogen unit.
1 of 1
Este artículo | |||
|---|---|---|---|
| description powder | description lyophilized powder, ≥10 DEA units/mg solid | description lyophilized powder, 3-8 TIU/mg solid | description Type VIII, lyophilized powder, 300-1,000 U/mg |
| biological source bovine intestine | biological source bovine intestinal mucosa | biological source bovine lung | biological source bovine testis |
| form powder | form lyophilized powder | form lyophilized powder | form lyophilized powder |
| shipped in dry ice | shipped in wet ice | shipped in - | shipped in - |
| storage temp. −20°C | storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C |
| mol wt 150 kDa (consisting of 115kDa and 35kDa subunits.) | mol wt dimer ~160 kDa | mol wt ~6,500 | mol wt ~55 kDa (four subunits of 14 kDa each) |
| color white | color - | color - | color - |
wgk
WGK 3
Clase de almacenamiento
11 - Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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