EZSolution™ Protein Stabilizer

A ready-to-use protein formulation to increase the stability of inactive proenzymes and active enzymes under chemical or thermal stress.
Catalog #: 7928 | abID:

Product Details

Highlights FORM: Liquid
FORMULATION: Provided as a 1 mg/ml solution in phosphate buffer, pH 7.5.
MOL. WEIGHT: Oligomeric mixture of ~50 kDa proprietary protein.
APPLICATIONS: BioVision’s EZSolution™ Protein Stabilizer can be used for multiple purposes, including:
• To increase the stability of inactive proenzymes and active enzymes under chemical or thermal stress.
• As an inert protein stabilizer for increasing shelf-life of purified recombinant proteins.
• Protective additive in cell culture.
• Can also be used to stabilize antibodies/antigens in immunoassays (optimization required).
ADVANTAGES OF EZSolution™ Protein Stabilizer:
• Non-toxic and non-antigenic.
• Does not destabilize biomolecules in downstream assays
• Filterable through a 0.2 µm membrane and easily pipettable.
• Free from nucleic acids, polysaccharides and lipids.
• Stabilizes protein classes including proteases, kinases, phosphatases, and cytokines.
Storage Conditions 4°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not For Use in Humans.

Details

BioVision’s EZSolution™ Protein Stabilizer is a very effective BSA alternative. It consists of a proprietary protein expressed in E. coli. The proprietary formulation helps protect proteins and enzymes against heat or chemically-induced environmental stresses that can otherwise lead to enzyme inactivation or hyper-activation, aggregation and freeze-thaw damage. The EZSolution™ Protein Stabilizer is provided as a ready-to-use liquid formulation that can be directly added to protein/enzyme of interest. Such samples can be further refrigerated or frozen for storage with enhanced stability. The degree of stabilization is protein-specific; the EZSolution™ Protein Stabilizer has been tested to significantly increase the stability of a variety of proteins under thermal and chemical stress (see supplemental data).


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