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Native Porcine Pancreatic Elastase Suspension Proteins Molecular Depot
Native Porcine Pancreatic Elastase Suspension Proteins Molecular Depot
Native Porcine Pancreatic Elastase Suspension Proteins Molecular Depot
Native Porcine Pancreatic Elastase Suspension Proteins Molecular Depot

Native Porcine Pancreatic Elastase Suspension

$2,795.00

    Catalog Number: B2017268 (1000 mg)

    Native Porcine Pancreatic Elastase Suspension is derived from pig pancreas. Elastase breaks down elastin, a key extracellular matrix protein. It is used in research to study protein degradation and enzyme kinetics. The suspension is characterized by its purity and enzymatic activity. Proper storage (usually refrigeration) is necessary to maintain its activity. Follow safety and handling guidelines. This product has been used as a molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

    Products are for in vitro research use only (RUO).

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What's Included

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VR Headset

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2 Touch Controllers

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Charging Cable

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Native Porcine Pancreatic Elastase Suspension

Catalog number: B2017268
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 1000 mg
Molecular Weight or Concentration: 25.5 kDa
Supplied as: Suspension
Applications: a molecular tool for various biochemical applications
Storage: 2-8°C
Keywords: Chymotrypsin-like elastase family member 1, Elastase-1, ELA1
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

References

  • Terashima M, Murai Y, Kawamura M, Nakanishi S, Stoltz T, Chen L, Drohan W, Rodriguez RL, Katoh S. Production of functional human alpha 1-antitrypsin by plant cell culture Appl Microbiol Biotechnol. 1999 Oct;52(4):516-23.
  • Meyer E, Cole G, Radhakrishnan R, Epp O. Structure of native porcine pancreatic elastase at 1.65 A resolutions Acta Crystallogr B. 1988 Feb 1;44 ( Pt 1):26-38.
  • Würtele M, Hahn M, Hilpert K, Höhne W. Atomic resolution structure of native porcine pancreatic elastase at 1.1 A Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):520-3.
  • Geller M, Carlson-Golab G, Lesyng B, Swanson SM, Meyer EF Jr. Dynamic properties of the first enzymatic reaction steps of porcine pancreatic elastase. How rigid is the active site of the native enzyme? Molecular dynamics simulation Biopolymers. 1990;30(7-8):781-96.
  • Fu Z, Akula S, Thorpe M, Hellman L. Marked difference in efficiency of the digestive enzymes pepsin, trypsin, chymotrypsin, and pancreatic elastase to cleave tightly folded proteins Biol Chem. 2021 May 12;402(7):861-867.
  • Hogan JM, McLuckey SA. Charge state dependent collision-induced dissociation of native and reduced porcine elastase J Mass Spectrom. 2003 Mar;38(3):245-56.
  • Jaspard E. Role of protein-solvent interactions in refolding: effects of cosolvent additives on the renaturation of porcine pancreatic elastase at various pHs Arch Biochem Biophys. 2000 Mar 15;375(2):220-8.
  • Berglund GI, Willassen NP, Hordvik A, Smalås AO. Structure of native pancreatic elastase from North Atlantic salmon at 1.61 A resolution Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):925-37.
  • James HL, Cohen AB. Mechanism of inhibition of porcine elastase by human alpha-1-antitrypsin J Clin Invest. 1978 Dec;62(6):1344-53.

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Product Resources:

Copy of Technical Specifications

FeatureDetails
Viewing Head Siedentopf type trinocular head, inclined at 30°, Interpupillary adjustment 53mm to 75mm, graduated diopter on left eyetube (30mm I.D. eyetubes)
Eyepieces SWH10X Widefield high eyepoint eyepiece, Field No. 22, tube O.D. 30.0 mm
Nosepiece Quintuple
Quintuple LWD Planachromat Phase 10x, 20x
Condenser TC Condenser N.A. 0.30, W.D. 73.0mm
Stage180mm(X) x 245mm(Y) plain stage with replaceable glass insert with 45mm opening, Glass Stage plate insert
IlluminationKoehler without iris, with phase slider, 3W LED
WarrantyLIMITED LIFETIME WARRANTY

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