Analytical Data
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Gene name
LELP1
- Application
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Alternative Names
Novel small proline-rich protein
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5T871
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Expression Region
1-98aa
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Molecular Weight
37.7 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
LELP1 (Leucine-rich repeat and immunoglobulin-like domain-containing protein 1) is a protein involved in various cellular processes, including cell signaling and immune responses. Recent studies have highlighted its potential roles in development, differentiation, and tumor biology, making it a significant target for research in both basic and applied sciences. Understanding LELP1's structure and function is crucial for elucidating its mechanisms in health and disease, particularly its involvement in cancer progression and immune system modulation. The recombinant expression of LELP1 allows for detailed biochemical studies, facilitating the investigation of its interactions with other proteins and cellular pathways. Furthermore, by producing LELP1 in a controlled laboratory environment, researchers can explore its functional properties, characterize its domain architecture, and assess its biological activities in vitro and in vivo. This approach aims to provide insights into how LELP1 may serve as a biomarker or therapeutic target, thereby contributing to the development of novel treatments for diseases associated with its dysregulation. As research progresses, LELP1 holds promise for uncovering new therapeutic strategies and enhancing our overall understanding of cellular dynamics in health and disease.
