Analytical Data
-
Gene name
MAL
- Application
-
Alternative Names
MAL; Myelin and lymphocyte protein; T-lymphocyte maturation-associated protein
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P21145
-
Expression Region
1-153aa
-
AA Sequence
MAPAAATGGSTLPSGFSVFTTLPDLLFIFEFIFGGLVWILVASSLVPWPLVQGWVMFVSVFCFVATTTLIILYIIGAHGGETSWVTLDAAYHCTAALFYLSASVLEALATITMQDGFTYRHYHENIAAVVFSYIATLLYVVHAVFSLIRWKSS
-
Molecular Weight
16.7 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
MAL (Myelin and Lysosomal Protein) is a protein primarily associated with the membrane of myelin sheaths in the central nervous system and is crucial for maintaining myelin integrity and function. Research into MAL recombinant proteins has gained significant attention due to the protein's potential involvement in various neurodegenerative diseases and demyelinating conditions, such as multiple sclerosis and leukodystrophies. Understanding the structure-function relationships of MAL and its signaling pathways can provide insight into its role in myelination and neuronal health. Recent studies have focused on developing recombinant MAL for functional assays, facilitating investigations into its interactions with other myelin-associated proteins and lipids. Furthermore, the expression of MAL in non-neuronal cell types has opened avenues for exploring its broader biological implications. By engineering MAL to study its properties and therapeutic potential, researchers aim to unveil novel strategies for treating neurological disorders characterized by myelin sheath degradation. This line of research ultimately seeks to contribute to the understanding of central nervous system pathology and the development of regenerative therapies that can restore myelin and improve neuronal function. The advancement of MAL recombinant protein studies represents a promising frontier in neuroscience, offering hope for new interventions in demyelinating diseases.
