Analytical Data
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Gene name
LRRIQ1
- Application
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Alternative Names
LRRIQ1; KIAA1801Leucine-rich repeat and IQ domain-containing protein 1
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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
Q96JM4
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Expression Region
1-240aa
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AA Sequence
MDDDDAKLKAEIEAELDKLSISSLEKEDIESDAKSETQSDDSDTDSVELPESVLHCINIIKNRSKAVEELILQDLEDILSCSYGAVSNNHMHLRTGLSTEYEESSEQLIKILSEIEKEEFMRSKTDCATPDFVPEPSPHDLPMDEHVLPDDADINFGYCEVEEKCRQSFEAWQEKQKELEDKEKQTLKAQRDREEKQFQEEEEKRHCWMKQFKVEKKKLENIQKVFCFCFSCIFKISSYL
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Molecular Weight
54.4 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
LRRIQ1 (Leucine-Rich Repeat IQ Motif-Containing Protein 1) has garnered attention in recent years due to its potential role in various cellular processes and its implications in disease mechanisms. This protein is characterized by the presence of leucine-rich repeats, which are known to facilitate protein-protein interactions, and an IQ motif, which is often involved in binding calmodulin and other calcium-binding proteins. Research indicates that LRRIQ1 is implicated in the regulation of neuronal signaling, synaptic function, and potentially in the development of neurodegenerative disorders. Studies have suggested that abnormal expression or mutations in LRRIQ1 may contribute to conditions such as Alzheimer's disease and autism spectrum disorders. Thus, understanding LRRIQ1's structure, function, and interaction partners is crucial for elucidating its biological roles. Researchers are actively investigating its recombinant protein for functional assays, structural studies, and potential therapeutic applications. The recombinant form of LRRIQ1 provides a valuable tool for further dissecting the molecular pathways in which it is involved while facilitating the exploration of its functional dynamics in vitro.
