Analytical Data
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Gene name
Hyaluronidase
- Application
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Alternative Names
Hyaluronoglucosaminidase (Vesp ma 2) (Hya)
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Species
Vespa magnifica
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P86875
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Expression Region
27-357aa
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Molecular Weight
45.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Hyaluronidase is an enzyme that plays a critical role in the degradation of hyaluronic acid, a key component of the extracellular matrix that influences tissue hydration, cell migration, and angiogenesis. The interest in recombinant hyaluronidase has surged due to its potential therapeutic applications in medicine and cosmetic treatments. Traditional sources of hyaluronidase, primarily derived from animal tissues, raise concerns about immune responses and batch-to-batch variability. Therefore, the development of a recombinant form offers a more consistent and potentially safer alternative. Researchers are focused on optimizing the production of recombinant hyaluronidase using various expression systems, such as bacterial and yeast platforms, to enhance yield and activity. Studies have demonstrated the enzyme’s utility in several clinical contexts, including enhancing drug delivery efficiency by increasing the permeability of tissues, facilitating the treatment of hematomas and local anesthetics, and improving the efficacy of cancer therapies. Additionally, in aesthetic medicine, recombinant hyaluronidase is employed to dissolve hyaluronic acid fillers, allowing for refined results in cosmetic procedures. The ongoing research aims to further understand its mechanisms of action, improve its therapeutic applications, and assess potential side effects, ultimately contributing to the advancement of medical and aesthetic practices. Overall, recombinant hyaluronidase presents a promising avenue for innovation in biopharmaceuticals, with significant implications for both therapeutic developments and aesthetic applications.
