Analytical Data
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Gene name
ispU
- Application
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Alternative Names
ispU；rth；uppS；yaeS；Ditrans.polycis-undecaprenyl-diphosphate synthase ((2E.6E)-farnesyl-diphosphate specific)
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Species
E.coli
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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
P60472
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Expression Region
1-253aa
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AA Sequence
MMLSATQPLSEKLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANNGIEALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDTSRFNSRLQERIRKSEALTAGNTGLTLNIAANYGGRWDIVQGVRQLAEKVQQGNLQPDQIDEEMLNQHVCMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALNAFANRERRFGGTEPGDETA
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Molecular Weight
32.4 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
The research on ISP (Inner Star Protein) recombinant proteins has gained significant attention in the field of biotechnology and molecular biology due to their potential applications in various scientific domains. ISP proteins, originally identified in specific bacterial species, play crucial roles in cellular processes such as signal transduction, stress response, and metabolic regulation. The ability to produce these proteins in recombinant form allows researchers to study their structure and function in detail, which is essential for understanding their biological roles. Moreover, ISP recombinant proteins have potential therapeutic applications, including the development of vaccines and enzyme-based treatments. Advances in recombinant DNA technology, including the use of expression systems such as yeast, bacteria, and mammalian cells, have facilitated the efficient production of these proteins, enabling researchers to explore their mechanisms of action and interactions with other biomolecules. As the demand for novel biopharmaceuticals grows, the study of ISP recombinant proteins represents a promising frontier in drug discovery and development, addressing the challenges of diseases that require innovative therapeutic strategies. Understanding the properties and functions of ISP proteins not only enhances our comprehension of fundamental biological processes but also paves the way for practical applications in medicine and industry. Overall, the investigation of ISP recombinant proteins is a dynamic and rapidly evolving field that holds great promise for future discoveries and advancements in health and technology.
