Analytical Data
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Gene name
LRTM1
- Application
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Alternative Names
HT017; Leucine rich repeats and transmembrane domains 1; Leucine-rich repeat and transmembrane domain-containing protein 1; Lrtm1; LRTM1_HUMAN
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HBL6
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Expression Region
1-345aa
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AA Sequence
MKGELLLFSSVIVLLQVVCSCPDKCYCQSSTNFVDCSQQGLAEIPSHLPPQTRTLHLQDNQIHHLPAFAFRSVPWLMTLNLSNNSLSNLAPGAFHGLQHLQVLNLTQNSLLSLESRLFHSLPQLRELDLSSNNISHLPTSLGETWENLTILAVQQNQLQQLDRALLESMPSVRLLLLKDNLWKCNCHLLGLKLWLEKFVYKGGLTDGIICESPDTWKGKDLLRIPHELYQPCPLPAPDPVSSQAQWPGSAHGVVLRPPENHNAGERELLECELKPKPRPANLRHAIATVIITGVVCGIVCLMMLAAAIYGCTYAAITAQYHGGPLAQTNDPGKVEEKERFDSSPA
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Molecular Weight
64.6 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
Related Products
Protein Description
LRTM1, or leucine-rich repeat and transmembrane domain 1, is a protein that has garnered attention in the field of cellular and molecular biology due to its role in various physiological processes, including cell signaling and membrane trafficking. Research has indicated that LRTM1 is involved in the regulation of synaptic functions in neurons, making it a critical component in understanding neurodevelopmental disorders and cognitive functioning. The protein is characterized by a series of leucine-rich repeats that suggest a role in protein-protein interactions, potentially influencing cellular mechanisms such as endocytosis and receptor recycling. Additionally, studies have shown that LRTM1 may participate in the modulation of immune responses, linking it to inflammatory diseases. Given its diverse functions, the recombinant expression and study of LRTM1 are vital for elucidating its biological roles and mechanisms. Characterizing LRTM1 through recombinant protein techniques not only aids in deciphering its structure-function relationships but also lays the groundwork for therapeutic developments targeting conditions associated with its dysregulation. The exploration of LRTM1's interactions with other cellular components could provide insights into novel signaling pathways, making it an important focus for future research in both neuroscience and immunology.
