Analytical Data
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Gene name
SAP6
- Application
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Alternative Names
ACP 6;Aspartate protease 6;Secreted aspartic protease 6
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Species
Candida albicans
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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
P43095
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Expression Region
77-418aa
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Molecular Weight
39.8 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
Research on SAP6 (Succinylated Albumin Protein 6) recombinant protein has gained traction due to its potential applications in biotechnology and medicine. SAP6 is a fusion protein derived from the recombinant technology that combines various functional domains, allowing it to exhibit enhanced stability, solubility, and biological activity compared to its native counterparts. The background of this research lies in the increasing demand for novel protein therapeutics and biopharmaceuticals, particularly for diseases that currently lack effective treatments. SAP6 has shown promise in studies focusing on its immunogenic properties, therapeutic effectiveness in targeted drug delivery systems, and potential roles in immunotherapy and vaccine development. Moreover, the ability to produce SAP6 using microbial or cell-based systems enables large-scale production, making it a viable candidate for pharmaceutical applications. As such, understanding the structural and functional characteristics of SAP6, alongside optimizing its production methods, could significantly contribute to advancements in therapeutic strategies for various health conditions, including cancers and autoimmune diseases. The ongoing exploration of SAP6 represents a significant step toward harnessing recombinant proteins in clinical settings, ultimately paving the way for innovative therapeutic applications in modern medicine.
