Analytical Data
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Gene name
Hyaluronidase 2/HYAL2
- Application
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Alternative Names
Hyaluronidase-2; Hyaluronoglucosaminidase-2; Hyal2; Hyal-2
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Species
Mouse
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Source
HEK293
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Tag
C-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O35632
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Expression Region
L23-D448
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Protein Length
Full Length of Mature Protein
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Molecular Weight
52-68 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
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Protein Description
Hyaluronidase 2 (HYAL2) is a crucial enzyme involved in the degradation of hyaluronic acid, a glycosaminoglycan that plays a vital role in various physiological processes, including tissue hydration, cell proliferation, and wound healing. Unlike its counterparts, HYAL2 is distinct in its preference for hyaluronic acid with a lower molecular weight, making it essential for modulating the extracellular matrix and facilitating cell migration. The recombinant production of HYAL2 has gained attention in biomedical research due to its potential therapeutic applications in treating conditions related to hyaluronic acid accumulation, such as certain cancer types, inflammatory diseases, and skin disorders. Furthermore, the understanding of HYAL2’s structure and function could lead to the development of targeted delivery systems for drugs and biologics, enhancing their efficacy. Recent studies have focused on optimizing the expression and purification processes of recombinant HYAL2, alongside exploring its enzymatic mechanisms and interaction with hyaluronic acid. This research not only contributes to our fundamental knowledge of glycosaminoglycan metabolism but also opens avenues for innovative therapeutic strategies leveraging HYAL2’s enzymatic properties. As such, the exploration of recombinant HYAL2 stands at the intersection of biochemistry, molecular biology, and clinical research, highlighting its importance in advancing both scientific knowledge and potential medical applications.
