Analytical Data
-
Gene name
LPHN1
- Application
-
Alternative Names
CIRL1; CL1; LEC2; Calcium-independent alpha-latrotoxin receptor 1; Lectomedin-2
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O94910
-
Expression Region
Val248~Val390
-
Molecular Weight
17kDa
-
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
LPHN1, or LPHN1 (latrophilin 1), is a member of the adhesion GPCR (G protein-coupled receptor) family and has gained significant attention in recent years due to its crucial role in various physiological processes, including neuronal development, synaptic plasticity, and cell adhesion. Research has shown that LPHN1 is associated with neurodevelopmental disorders and may influence signaling pathways involved in the formation of synapses in the central nervous system. The recombinant protein expression of LPHN1 allows for detailed studies of its structure and function, facilitating the exploration of its interactions with other proteins and potential ligands. This research has implications for understanding the molecular mechanisms underlying neuropsychiatric conditions and could lead to novel therapeutic strategies. Recent advances in biochemistry and molecular biology techniques have enabled the efficient production and purification of LPHN1 recombinant proteins, paving the way for functional assays and structural biology studies. As a result, LPHN1 is an attractive target for further investigation, promising insights into its role in health and disease.
