Analytical Data
-
Gene name
LELP1
- Application
-
Alternative Names
LELP1；Late cornified envelope-like proline-rich Protein 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q5T871
-
Expression Region
1-98aa
-
AA Sequence
MSSDDKSKSNDPKTEPKNCDPKCEQKCESKCQPSCLKKLLQRCFEKCPWEKCPAPPKCLPCPSQSPSSCPPQPCTKPCPPKCPSSCPHACPPPCPPPE
-
Molecular Weight
37.7 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
LELP1 (LIM and SH3 protein 1) is a member of the LIM domain-containing protein family, which has gained attention in recent years due to its potential role in various cellular processes, including cytoskeletal organization, signal transduction, and cellular differentiation. Research has indicated that LELP1 may be involved in important biological functions such as cell adhesion, migration, and the regulation of gene expression. The importance of LELP1 has prompted scientists to explore its structure and function through recombinant protein techniques, which allow for the production of purified LELP1 for further study. Recombinant LELP1 can be used to investigate its interactions with other proteins, elucidate its role in various signaling pathways, and assess its potential implications in diseases such as cancer and neurodegenerative disorders. Understanding the biochemical properties and mechanisms of action of LELP1 could provide insights into its physiological roles and its potential as a therapeutic target. As such, the generation of LELP1 recombinant protein is a crucial step in advancing our comprehension of this protein's function and its relevance in health and disease contexts. Continued research in this area is likely to unveil novel therapeutic strategies and enhance our understanding of cellular dynamics mediated by LELP1.
