Analytical Data
-
Gene name
RELN
- Application
-
Alternative Names
RELN；Reelin
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P78509
-
Expression Region
26-254aa
-
AA Sequence
AAGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSVQASQSIGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLSFIWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQGAPTDVTVHPHLAEIHSDSIILRDDFDSYHQLQLNPNIWVECNNCETGEQCGAIMHGNAVTFCEPYGPRELITT
-
Molecular Weight
28.9kDa
-
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
Reelin (RELN) is a large extracellular glycoprotein that plays a crucial role in neuronal migration, positioning, and synaptic plasticity during brain development. Its discovery in the early 1990s marked a significant advancement in understanding the molecular mechanisms underlying neurodevelopmental processes. Reelin functions through its interaction with specific receptors on the surface of neurons, notably the apolipoprotein E receptor 2 (ApoER2) and very low-density lipoprotein receptor (VLDLR), which initiates intracellular signaling cascades essential for proper neuronal organization. Abnormalities in Reelin's signaling pathway have been implicated in various neurological disorders, including schizophrenia, autism, and Alzheimer's disease, highlighting its importance not only in normal brain function but also in the pathophysiology of these conditions. As a result, the recombinant production of RELN protein has garnered significant interest, facilitating detailed studies of its functional roles and potential therapeutic applications. Researchers are now utilizing recombinant RELN to explore its effects on neuronal cultures, providing insights into its physiological mechanisms and potential for regenerative medicine. This research holds promise for developing novel strategies to manipulate Reelin signaling, aiming to restore normal neuronal function in diseases characterized by disrupted brain architecture.
