Analytical Data
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Gene name
BAM1
- Application
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Alternative Names
BAM1；BMY7；TRBAMY；Beta-amylase 1. chloroplastic
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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
Q9LIR6
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Expression Region
42-354aa
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AA Sequence
AMNRNYKAHGTDPSPPMSPILGATRADLSVACKAFAVENGIGTIEEQRTYREGGIGGKKEGGGGVPVFVMMPLDSVTMGNTVNRRKAMKASLQALKSAGVEGIMIDVWWGLVEKESPGTYNWGGYNELLELAKKLGLKVQAVMSFHQCGGNVGDSVTIPLPQWVVEEVDKDPDLAYTDQWGRRNHEYISLGADTLPVLKGRTPVQCYADFMRAFRDNFKHLLGETIVEIQVGMGPAGELRYPSYPEQEGTWKFPGIGAFQCYDKYSLSSLKAAAETYGKPEWGSTGPTDAGHYNNWPEDTQFFKKEGGGWNSE
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Molecular Weight
36.3 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
BAM1, or the Beta-barrel assembly machinery protein 1, is a vital component in the biogenesis of membrane proteins in bacteria, particularly in the assembly of outer membrane proteins (OMPs) in Gram-negative bacteria. The proper functioning of BAM1 is crucial as it facilitates the insertion and folding of OMPs into the bacterial outer membrane, which is essential for maintaining membrane integrity and function. Mutations or malfunctions in the BAM complex can lead to severe defects in bacterial growth and virulence, making it a significant target for antibiotic development. Recent studies have focused on elucidating the structural and functional mechanisms of BAM1, revealing its interactions with various substrate proteins and its role in recognizing and incorporating OMPs into the membrane. Understanding these processes at a molecular level is critical for advancing our knowledge of bacterial physiology and could provide novel strategies for combating antibiotic resistance. Research on BAM1 also offers insights into the evolutionary adaptations of bacteria to their environments, highlighting its potential as a target for novel antimicrobial therapies. As the world grapples with rising antibiotic resistance, the exploration of BAM1 and related components presents an exciting frontier in microbiology and drug discovery.
