Analytical Data
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Gene name
LPAL2
- Application
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Alternative Names
LPAL2; APOARGC; Putative apolipoprotein(a)-like protein 2; Apo(a)-like protein 2; Lp(a)-liker protein 2; Apolipoprotein a-related gene C protein; Apo(a)rg-C
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q16609
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Expression Region
1-132aa
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AA Sequence
MEHKEVVLLLLLFLKSAPTETGPSVQECYHSNGQSYRGTYFTTVTGRTCQAWSSMTPHQHSRTPEKYPNDGLISNYCRNPDCSAGPWCYTTDPNVRWEYCNLTRCSDDEGTVFVPLTVIPVPSLEDSFIQVA
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Molecular Weight
14.6 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
LPAL2 is a recombinant protein that has garnered attention in the fields of biotechnology and molecular biology due to its potential applications in therapeutic and diagnostic development. Originally identified from various sources, including plants and microorganisms, LPAL2 exhibits unique biochemical properties that suggest its involvement in critical biological processes. Research into LPAL2 highlights its capacity for specific interactions with cellular components, making it a candidate for further exploration in drug delivery systems and protein engineering. Additionally, studies have indicated that LPAL2 may play a role in modulating immune responses, which opens avenues for its use in vaccine development and immunotherapy. The recombinant production of LPAL2 enables large-scale synthesis and purification, thus facilitating in-depth studies into its structure-function relationships. Investigating the functionality of LPAL2 not only enhances our understanding of its biological mechanisms but also contributes to the broader landscape of protein science, offering insights into how engineered proteins can be harnessed for disease treatment and prevention. As ongoing research unfolds, the promise of LPAL2 as a valuable tool in medical and industrial applications continues to grow, positioning it as a significant focus for future studies in the field.
