Analytical Data
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Gene name
inlA
- Application
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Alternative Names
inlA；CDHE；UVO；；Cadherin-1
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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
P0DJM0
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Expression Region
32-414aa(S192N.Y369S)
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AA Sequence
NAQAATITQDTPINQIFTDTALAEKMKTVLGKTNVTDTVSQTDLDQVTTLQADRLGIKSIDGVEYLNNLTQINFSNNQLTDITPLKNLTKLVDILMNNNQIADITPLANLTNLTGLTLFNNQITDIDPLKNLTNLNRLELSSNTISDISALSGLTSLQQLNFGNQVTDLKPLANLTTLERLDISSNKVSDISVLAKLTNLESLIATNNQISDITPLGILTNLDELSLNGNQLKDIGTLASLTNLTDLDLANNQISNLAPLSGLTKLTELKLGANQISNISPLAGLTALTNLELNENQLEDISPISNLKNLTYLTLYFNNISDISPVSSLTKLQRLFFSNNKVSDVSSLANLTNINWLSAGHNQISDLTPLANLTRITQLGLND
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Molecular Weight
48.9 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
InlA, also known as internalin A, is a surface protein produced by the pathogenic bacterium Listeria monocytogenes, which is known for its ability to invade human cells and establish infections. This protein plays a crucial role in the bacterium’s pathogenesis by facilitating its entry into epithelial cells through interaction with the host’s E-cadherin, a key component of cell-cell adhesion. The study of InlA is of significant interest due to its implications for understanding infection mechanisms and developing therapeutic interventions. Research has shown that the binding affinity between InlA and E-cadherin is essential for Listeria's virulence, making it a potential target for vaccine development and antibody-based therapies. Furthermore, examining the structural and functional aspects of InlA can provide insights into the broader category of microbial pathogenesis, particularly in how pathogens exploit host cell machinery. Recent studies have employed techniques such as X-ray crystallography and mutagenesis to elucidate the molecular interactions involved, revealing potential sites for drug design. Given the increasing incidence of listeriosis, particularly in immunocompromised individuals and pregnant women, understanding the role of InlA is critical not only for microbiology but also for public health initiatives aimed at preventing foodborne diseases. Thus, ongoing research continues to focus on InlA, aiming to uncover its complete functional landscape and harness this knowledge for innovative therapeutic strategies against L. monocytogenes infections.
