Analytical Data
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Gene name
HYP2
- Application
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Alternative Names
HYP2；Hydrophobin-2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23301
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Expression Region
2-157aa
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AA Sequence
SDEEHTFETADAGSSATYPMQCSALRKNGFVVIKSRPCKIVDMSTSKTGKHGHAKVHLVAIDIFTGKKLEDLSPSTHNMEVPVVKRNEYQLLDIDDGFLSLMNMDGDTKDDVKAPEGELGDSLQTAFDEGKDLMVTIISAMGEEAAISFKEAARTD
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Molecular Weight
33.0 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
HYP2, a member of the hypoxia-inducible factor (HIF) family, plays a crucial role in cellular responses to low oxygen environments. Research into HYP2 has gained significance due to its implications in various physiological and pathological processes, including angiogenesis, metabolism, and cancer progression. Under hypoxic conditions, HYP2 regulates gene expression that promotes adaptation to low oxygen levels, supporting cell survival and function. Its role in tumor biology has attracted attention; tumor cells often exploit HYP2-mediated pathways to thrive in hypoxic tumor microenvironments, leading to enhanced growth and metastasis. Additionally, understanding HYP2's mechanism of action may provide insights into therapeutic strategies for targeting hypoxia-related diseases. Recent studies focus on the structural and functional characterization of HYP2, exploring its interactions with other cellular components and delineating its regulatory pathways. The reconstitution of HYP2 as a recombinant protein offers opportunities for in-depth analysis of its biological activities, facilitating advancements in drug development and the identification of potential biomarkers for disease prognosis. Overall, HYP2 represents a key protein for understanding the complexities of hypoxia-driven processes in health and disease.
