Analytical Data
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Gene name
LRRC40
- Application
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Alternative Names
dJ677H15.1; Leucine rich repeat containing protein 40; Leucine-rich repeat-containing protein 40; LRC40_HUMAN; LRRC40; testicular tissue protein Li 109
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H9A6
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Expression Region
1-602aa
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Molecular Weight
72.2 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
LRRC40 (Leucine-Rich Repeat Containing Protein 40) is a relatively novel protein that has garnered attention in the field of molecular biology and cancer research. It is characterized by a unique composition of leucine-rich repeat motifs, which are known to be involved in protein-protein interactions, a critical aspect of various cellular processes. Recent studies have indicated that LRRC40 may play a significant role in cellular signaling pathways, particularly those related to cell proliferation and survival. Interestingly, its expression levels have been linked to several types of cancers, suggesting a potential role in tumorigenesis. The exploration of LRRC40 as a recombinant protein has become an area of great interest, as understanding its structure and function could provide insights into its biological roles and mechanisms. Researchers are particularly focused on elucidating its interactions within key cellular pathways and its potential as a therapeutic target. Given the increasing incidence of cancer and the need for innovative treatment strategies, studying LRRC40 not only advances the understanding of fundamental biological mechanisms but also opens avenues for developing novel cancer therapies. The production of LRRC40 as a recombinant protein allows for detailed structural studies and functional analyses, paving the way for future research aimed at harnessing this protein's properties in clinical applications. Overall, the investigation of LRRC40 presents promising opportunities to enhance our understanding of its biological significance and therapeutic potential in cancer treatment.
