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EMS0006

Trypsin Protease

Hydrolyzes peptide bonds at the carboxyl side of arginine and lysine residues, suitable for mass spectrometry, recombinant, expressed in Pichia pastoris

Sinónimos:

Mass Spectrometry Trypsin, Proteomics grade Trypsin, rTrypsin

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Talla/SKUDisponibilidadPrecio
100 μg
Comprobar disponibilidad del carrito
$94.800
4 x 100 μg
Comprobar disponibilidad del carrito
$351.000

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UNSPSC Code:
12352204
NACRES:
NA.26
Specific activity:
≥10,000 units/mg protein
Recombinant:
expressed in Pichia pastoris

$94.800


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Nombre del producto

Recombinant Trypsin, Proteomics Grade, lyophilized powder, recombinant, expressed in Pichia pastoris

recombinant

expressed in Pichia pastoris

Quality Segment

grade

Proteomics Grade

form

lyophilized powder

specific activity

≥10,000 units/mg protein

technique(s)

protein mass spectrometry: suitable

suitability

suitable for , suitable for mass spectrometry

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

General description

Trypsin is a major proteolytic enzyme, synthesized as a preproenzyme by pancreas and is stored as proenzyme trypsinogen in secretory granules. Trypsin belongs to the family of serine proteases that are characterized by the catalytic triad His57, Asp102 and Ser195. Trypsin is routinely used in proteomics research for peptide mapping and protein sequence work due to its highly specific cleavage resulting in a limited number of tryptic peptides. Trypsin is a pancreatic serine endoprotease which hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues. The rate of hydrolysis is slower if an acidic residue is on either side of the cleavage site and cleavage may not occur if a proline residue is on the carboxyl side. The enzyme also exhibits esterase and amidase activities. Trypsin has an average molecular mass of 23.29 kDa and a pH optimum near 8.0. This product is prepared from recombinant trypsin, porcine sequence. It is naturally devoid of chymotryptic activity. This high-quality trypsin is suitable for proteomics use.

Biochem/physiol Actions

Trypsin plays an important role in the digestion of consumed protein and contributes to the activation of other proteolytic enzymes like chemotrypsin and elastase.

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Este artículo
EMS0007EMS0004EMS0005
description

Proteomics Grade, lyophilized powder, recombinant, expressed in Pichia pastoris

description

Proteomics Grade, lyophilized powder, recombinant, expressed in Pichia pastoris

description

recombinant, expressed in Pichia pastoris, Proteomics Grade, liquid

description

Dimethlyated, Proteomics Grade, recombinant, expressed in Pichia pastoris, ready-to-use solution

specific activity

≥10,000 units/mg protein

specific activity

≥10,000 units/mg protein

specific activity

-

specific activity

≥10,000 units/mg protein (Enzymatic activity)

grade

Proteomics Grade

grade

Proteomics Grade

grade

Proteomics Grade

grade

Proteomics Grade

suitability

suitable for mass spectrometry

suitability

suitable for mass spectrometry

suitability

suitable for mass spectrometry

suitability

suitable for mass spectrometry

recombinant

expressed in Pichia pastoris

recombinant

expressed in Pichia pastoris

recombinant

expressed in Pichia pastoris

recombinant

expressed in Pichia pastoris

form

lyophilized powder

form

lyophilized powder

form

ready-to-use solution

form

ready-to-use solution

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C


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Palabra de advertencia

Danger

Hazard Classifications

Aquatic Chronic 2 - Eye Dam. 1 - Met. Corr. 1 - Resp. Sens. 1 - Skin Corr. 1A - Skin Sens. 1 - STOT SE 3

Órganos diana

Respiratory system

supp_hazards

Clase de almacenamiento

8A - Combustible corrosive hazardous materials

¿Qué está pasando?

WGK 3

Punto de inflamación (°F)

Not applicable

Punto de inflamación (°C)

Not applicable



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