Analytical Data
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Gene name
LRRC10
- Application
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Alternative Names
LRRC10; Leucine-rich repeat-containing protein 10
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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
Q5BKY1
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Expression Region
1-277aa
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AA Sequence
MGNTIRALVAFIPADRCQNYVVRDLREMPLDKMVDLSGSQLRRFPLHVCSFRELVKLYLSDNHLNSLPPELGQLQNLQILALDFNNFKALPQVVCTLKQLCILYLGNNKLCDLPSELSLLQNLRTLWIEANCLTQLPDVVCELSLLKTLHAGSNALRLLPGQLRRLQELRTIWLSGNRLTDFPTVLLHMPFLEVIDVDWNSIRYFPSLAHLSSLKLVIYDHNPCRNAPKVAKGVRRVGRWAEETPEPDPRKARRYALVREESQELQAPVPLLPPTNS
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Molecular Weight
58 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
LRRC10 (Leucine-Rich Repeat Containing 10) is a protein that has garnered interest in the field of molecular biology due to its potential roles in cellular signaling and development. Initially identified as a gene associated with various physiological processes, LRRC10 has been implicated in the regulation of cardiac and skeletal muscle development. Its leucine-rich repeat structure suggests a function in protein-protein interactions, which is critical for assembling signaling complexes that govern cellular responses. Abnormalities in LRRC10 expression have been linked to various diseases, including cardiac hypertrophy and other muscular disorders, highlighting its importance in maintaining normal physiological functions. Recent studies have focused on producing recombinant LRRC10 protein to elucidate its structure-function relationships and understand the molecular mechanisms underlying its role in muscle biology. This research aims to characterize LRRC10 interactions with other proteins and explore its potential as a therapeutic target. By using advanced techniques such as crystallography and biophysical methods, scientists hope to reveal the intricate workings of LRRC10 in health and disease, paving the way for novel interventions. Overall, the study of recombinant LRRC10 protein presents a promising avenue for understanding complex biological systems and developing strategies to combat muscle-related diseases.
