Analytical Data
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Gene name
I340M
- Application
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Alternative Names
I340M
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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
P15151
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Expression Region
21-343aa
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AA Sequence
WPPPGTGDVVVQAPTQVPGFLGDSVTLPCYLQVPNMEVTHVSQLTWARHGESGSMAVFHQTQGPSYSESKRLEFVAARLGAELRNASLRMFGLRVEDEGNYTCLFVTFPQGSRSVDIWLRVLAKPQNTAEVQKVQLTGEPVPMARCVSTGGRPPAQITWHSDLGGMPNTSQVPGFLSGTVTVTSLWILVPSSQVDGKNVTCKVEHESFEKPQLLTVNLTVYYPPEVSISGYDNNWYLGQNEATLTCDARSNPEPTGYNWSTTMGPLPPFAVAQGAQLLIRPVDKPINTTLICNVTNALGARQAELTVQVKEGPPSEHSGMSRN
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Molecular Weight
64.0 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
I340M is a recombinant protein variant that has gained attention in recent years due to its potential applications in biomedicine and biotechnology. The I340M mutation is part of the ongoing research focused on understanding the structure-function relationships of proteins and how specific amino acid substitutions can influence protein stability, activity, and interactions. This area of study is particularly relevant in the context of therapeutic protein development, where modifications can enhance efficacy and reduce immunogenicity. Research involving I340M includes investigations into its biochemical properties, folding mechanisms, and bioactivity, which may provide insights into developing more effective drugs or biocatalysts. Additionally, understanding such variants can aid in the design of protein engineering strategies for industrial applications. The significance of studying I340M lies not only in its specific characteristics but also in its contribution to the broader understanding of protein dynamics and function in a cellular context. As the scientific community continues to explore the implications of protein modifications, the study of I340M serves as a critical case in the quest to unlock the full potential of recombinant proteins in various fields.
