Analytical Data
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Gene name
Hyaluronidase-1/HYAL1
- Application
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Alternative Names
Hyaluronic Lase; Hyaluroniclase
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Species
Human
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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
Q12794
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Expression Region
Phe201~Trp435
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Molecular Weight
30kDa
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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-1 (HYAL1) is an enzyme that plays a crucial role in the degradation of hyaluronic acid, a vital component of the extracellular matrix in various tissues. The enzymatic activity of HYAL1 is significant in numerous physiological processes, including cell migration, tissue remodeling, and inflammatory responses. Due to its ability to break down hyaluronic acid, HYAL1 has garnered attention in medical research, particularly in the context of cancer biology, where aberrant hyaluronic acid metabolism can contribute to tumor progression and metastasis. Additionally, HYAL1 is being studied for its potential therapeutic applications in enhancing drug delivery, as it can facilitate the permeation of therapeutic agents through tissue barriers. The recombinant production of HYAL1 allows for a more detailed investigation of its functional properties, regulation, and potential biotechnological applications. Research focusing on the structural and functional characterization of recombinant HYAL1 proteins is essential for understanding its mechanisms of action and for developing innovative strategies to modulate its activity in various clinical settings. Ultimately, advancing our knowledge of HYAL1 could lead to novel interventions in conditions characterized by altered hyaluronic acid metabolism, including cancer, chronic inflammation, and other degenerative diseases.
