E1250

Elastase from porcine pancreas

Type I, ≥4.0 units/mg protein

• Sinónimos: Elastase from hog pancreas, Pancreatopeptidase E
• Número de CAS: 39445-21-1
• Comisión internacional de enzimas: 3.4.21.36 (BRENDA, IUBMB)
• Número CE: 254-453-6
• Número MDL: MFCD00130998
• Código UNSPSC: 12352204
• NACRES: NA.54

Propiedades

• origen biológico: Porcine pancreas
• Nivel de calidad: 200
• tpo: Type I
• Formulario: suspension
• actividad específica: ≥4.0 units/mg protein
• mol peso: 25.9 kDa
• contiene: 0.1% thymol
• concentración: 0.5-15.0 mg/mL in water
• actividad extraña: trypsin ≤50 BAEE units/mg protein
• temp. de almacenamiento: 2-8°C

Descripción

Aplicación

Elastase from porcine pancreas has been used in a study to investigate the design, synthesis and evaluation of biomimetic affinity ligands for elastases. Elastase from porcine pancreas has also been used in a study to investigate the purification and partial characterization of the pancreatic proteolytic enzymes trypsin, chymotrypsin, and elastase.

Elastase from porcine pancreas has been used:

• to induce abdominal aortic aneurysm (AAA)
• to study the impact of indoleamine 2-3 dioxygenase 1 (IDO) in mice[1]
• to digest aortas for aortic smooth muscle cells (SMC) isolation[2]
• as a positive control of proteolytic digestion[3]

The enzyme from Sigma has been used in the development of elastase-perfused animal model . This study determined if tobacco exposure could lower the threshold of aortic injury necessary for AAA (abdominal aortic aneurysm) development.[4] It has also been used during the isolation of type II pneumocytes from human lungs.[5]

Acciones bioquímicas o fisiológicas

Elastase hydrolyses elastin, the specific protein of elastic fibers, and digests hemoglobin, casein and fibrin.

Elastase is a single polypeptide chain of 240 amino acid residues and contains four disulfide bridges. The molecular mass is approximately 25.9 kDa. The enzyme is synthesized as an inactive zymogen, proelastase, which is converted to the active form by limited proteolysis at the N-terminal by trypsin.[6] It is a serine protease with broad specificity. It cleaves protein at the carboxyl side of small hydrophobic amino acids such as Ile, Gly, Ala, Ser, Val, and Leu. The enzyme also hydrolyzes amides and esters such as N-Benzoyl-L-alanine methyl ester.[6][7] The pH optimum is found to be 8.0-8.5. It does not require any activator, but it is inhibited by diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride, α2-macroglobulin, α1-antitrypsin, sulfonyl fluorides and p-dinitrophenyl diethylphosphate and high salt concentrations. It is extensively used in tissue and cell dissociation procedures. Elastase is effective in the isolation of Type II lung cells.

Envase

Package size based on protein content

Definición de unidad

One unit will hydrolyze 1.0 μmole of N-succinyl-L-Ala-Ala-Ala-p-nitroanilide per min, pH 8.0 at 25 °C.

Nota de preparación

2× crystallized

Información de seguridad

• Pictogramas: GHS08,GHS07
• Palabra de señalización: Danger
• Frases de peligro: H315,H319,H334,H335
• Consejos de prudencia: P261 - P264 - P271 - P280 - P302 + P352 - P305 + P351 + P338
• Clasificaciones de peligro: Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
• Órganos de actuación: Respiratory system
• Código de clase de almacenamiento: 11 - Combustible Solids
• Clase de riesgo para el agua (WGK): WGK 3
• Punto de inflamabilidad (°F): Not applicable
• Punto de inflamabilidad (°C): Not applicable
• Equipo de protección personal: dust mask type N95 (US), Eyeshields, Faceshields, Gloves