Analytical Data
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Gene name
pat
- Application
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Alternative Names
pat；N-acetyltransferase Pat
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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
Q57146
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Expression Region
1-183aa
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AA Sequence
MSPERRPVEIRPATAADMAAVCDIVNHYIETSTVNFRTEPQTPQEWIDDLERLQDRYPWLVAEVEGVVAGIAYAGPWKARNAYDWTVESTVYVSHRHQRLGLGSTLYTHLLKSMEAQGFKSVVAVIGLPNDPSVRLHEALGYTARGTLRAAGYKHGGWHDVGFWQRDFELPAPPRPVRPVTQI
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Molecular Weight
36.6 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
PAT (proteins associated with translocation) recombinant proteins have garnered significant attention in biochemical and pharmaceutical research due to their crucial roles in various cellular processes. These proteins are involved in the modulation of protein translocation across membranes, which is vital for cellular homeostasis and signaling. The study of PAT recombinant proteins has expanded in recent years, driven by advances in genetic engineering and protein expression systems that allow for the production of large quantities of functional proteins. Understanding the structure and function of PAT proteins can provide insights into their mechanisms and interactions within the cell, which may lead to the development of novel therapeutic strategies for diseases associated with protein misfolding and translocation defects, such as neurodegenerative diseases and certain types of cancer. Moreover, these proteins serve as valuable tools in biotechnology and research, enabling the exploration of intracellular trafficking pathways and the design of targeted drug delivery systems. As a result, research on PAT recombinant proteins is pivotal for both basic science and applied medical research, highlighting the need for continued investigation into their properties and applications.
