Analytical Data
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Gene name
lytA
- Application
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Alternative Names
lytA；Autolysin
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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
P24556
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Expression Region
1-481aa
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AA Sequence
MQAKLTKNEFIERLKTSEGKQFNVDLWYGFQCFDYANAGWKVLFGLLLKGLGAKDIPFANNFDGLATVYQNTPDFLAQPGDMVVFGSNYGAGYGHVAWVIEATLDYIIVYEQNWLGGGWTDGIEQPAGVGKKLQDDNMLMISLCGLSVRILKVRQRHDQFNLLHKHPKKETAKPQPKAVELKIIKDVVKGYDLPKRGSNPKGIVIHNDAGSKGATAEAYRNGLVNAPLSRLEAGIAHSYVSGNTVWQALDESQVGWHTANQIGNKYYYGIEVCQSMGADNATFLKNEQATFQECARLLKKWGLPANRNTIRLHNEFTSTSCPHRSSVLHTGFDPVTRGLLPEDKRLQLKDYFIKQIRAYMDGKIPVATVSNESSASSNTVKPVASAWKRNKYGTYYMEESARFTNGNQPITVRKVGPFLSCPVGYQFQPGGYCDYTEVMLQDGHVWVGYTWEGQRYYLPIRTWNGSAPPNQILGDLWGEIS
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Molecular Weight
57.8 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
LytA, a crucial pneumococcal autolysin, plays a significant role in bacterial cell wall metabolism, particularly in the lysis and growth processes of Streptococcus pneumoniae. Its enzymatic activity is primarily associated with peptidoglycan hydrolysis, which is vital for maintaining cell shape and promoting cellular division. This protein has garnered attention due to its potential implications in pneumococcal pathogenesis and resistance to antibiotic treatment. Research surrounding the recombinant production of LytA has focused on elucidating its structure-function relationship, which can provide insights into novel therapeutic strategies against pneumococcal infections. By generating and characterizing LytA recombinant proteins, scientists aim to understand its catalytic mechanisms and interactions with other bacterial components. Additionally, these studies are pivotal in exploring the potential of LytA as a vaccine candidate or as a target for developing new antibiotics, especially in light of increasing antibiotic resistance among S. pneumoniae strains. The insights gained from LytA research not only contribute to our fundamental understanding of bacterial physiology but also offer promising avenues for combating pneumococcal diseases, which remain a substantial global health threat.
