Analytical Data
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Gene name
alaA
- Application
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Alternative Names
alaA；ACVRLK1；ALK1；Serine/threonine-Protein kinase receptor R3
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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
P0A959
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Expression Region
1-405aa
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AA Sequence
MSPIEKSSKLENVCYDIRGPVLKEAKRLEEEGNKVLKLNIGNPAPFGFDAPDEILVDVIRNLPTAQGYCDSKGLYSARKAIMQHYQARGMRDVTVEDIYIGNGVSELIVQAMQALLNSGDEMLVPAPDYPLWTAAVSLSSGKAVHYLCDESSDWFPDLDDIRAKITPRTRGIVIINPNNPTGAVYSKELLMEIVEIARQHNLIIFADEIYDKILYDDAEHHSIAPLAPDLLTITFNGLSKTYRVAGFRQGWMVLNGPKKHAKGYIEGLEMLASMRLCANVPAQHAIQTALGGYQSISEFITPGGRLYEQRNRAWELINDIPGVSCVKPRGALYMFPKIDAKRFNIHDDQKMVLDFLLQEKVLLVQGTAFNWPWPDHFRIVTLPRVDDIELSLSKFARFLSGYHQL
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Molecular Weight
61.5 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 alaA gene, which encodes the alanine racemase enzyme, plays a vital role in the biosynthesis of the amino acid L-alanine, a crucial component of proteins and metabolic pathways. This enzyme catalyzes the interconversion between L-alanine and D-alanine, the latter being essential for bacterial cell wall synthesis. Research on the alaA recombinant protein has gained significant interest due to its potential applications in understanding bacterial resistance mechanisms and developing novel antibiotics. As bacterial infections increasingly become resistant to existing treatments, targeting enzymes like alanine racemase presents a promising avenue for drug discovery. Moreover, studying the structural and functional properties of the alaA protein can provide insights into the enzymatic activity and the physiological roles of L-alanine in various organisms. Additionally, the overexpression of alaA in host systems, such as E. coli, facilitates the production of recombinant proteins, enabling further biochemical assays and structural analysis. This research not only contributes to our fundamental understanding of amino acid metabolism but also holds promise for the development of new therapeutic strategies against antibiotic-resistant bacteria, making it a critical area of investigation in the fields of microbiology and biochemistry.
