Analytical Data
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Gene name
ldcA
- Application
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Alternative Names
ldcA；Lysine decarboxylase LdcA
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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
P76008
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Expression Region
1-304aa
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AA Sequence
MSLFHLIAPSGYCIKQHAALRGIQRLTDAGHQVNNVEVIARRCERFAGTETERLEDLNSLARLTTPNTIVLAVRGGYGASRLLADIDWQALVARQQHDPLLICGHSDFTAIQCGLLAHGNVITFSGPMLVANFGADELNAFTEHHFWLALRNETFTIEWQGEGPTCRAEGTLWGGNLAMLISLIGTPWMPKIENGILVLEDINEHPFRVERMLLQLYHAGILPRQKAIILGSFSGSTPNDYDAGYNLESVYAFLRSRLSIPLITGLDFGHEQRTVTLPLGAHAILNNTREGTQLTISGHPVLKM
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Molecular Weight
37.6 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
LdcA, a lysine decarboxylase, is a key enzyme involved in the metabolism of lysine in various microorganisms, contributing to the production of biogenic amines and influencing pH regulation within cells. The study of LdcA recombinant proteins has gained significance due to their potential applications in biotechnology and medicine, particularly in developing novel probiotics and understanding the mechanisms of pathogenicity in certain bacteria. Research has shown that LdcA plays a pivotal role in stress responses, aiding microorganisms in adapting to acidic environments. Additionally, insights into the structure and function of LdcA can facilitate the design of inhibitors that may serve as therapeutic targets against infections caused by pathogenic strains that utilize lysine for growth and survival. Investigating the expression, purification, and biochemical properties of LdcA recombinant proteins not only helps in elucidating the enzyme's function but also paves the way for innovative applications, such as enhancing fermentation processes and improving food preservation techniques. As such, the exploration of LdcA presents promising avenues for both scientific discovery and practical applications in various fields, including microbiology, food science, and pharmaceuticals.
