Analytical Data
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Gene name
LRP12
- Application
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Alternative Names
LRP12；ST7；Low-density lipoProtein receptor-related Protein 12
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y561
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Expression Region
28-488aa
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AA Sequence
EHSENVHISGVSTACGETPEQIRAPSGIITSPGWPSEYPAKINCSWFIRA NPGEIITISFQDFDIQGSRRCNLDWLTIETYKNIESYRACGSTIPPPYIS SQDHIWIRFHSDDNISRKGFRLAYFSGKSEEPNCACDQFRCGNGKCIPEA WKCNNMDECGDSSDEEICAKEANPPTAAAFQPCAYNQFQCLSRFTKVYTC LPESLKCDGNIDCLDLGDEIDCDVPTCGQWLKYFYGTFNSPNYPDFYPPG SNCTWLIDTGDHRKVILRFTDFKLDGTGYGDYVKIYDGLEENPHKLLRVL TAFDSHAPLTVVSSSGQIRVHFCADKVNAARGFNATYQVDGFCLPWEIPC GGNWGCYTEQ QRCDGYWHCPNGRDETNCTMCQKEEFPCSRNGVCYPRSDRCNYQNHCPNG SDEKNCFFCQ PGNFHCKNNRCVFESWVCDSQDDCGDGSDEENCPVIVDHHHHHH
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Molecular Weight
53 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
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Protein Description
LRP12 (LDL Receptor-Related Protein 12) is a member of the low-density lipoprotein receptor family, which plays critical roles in cellular processes, including endocytosis, intracellular signaling, and lipid metabolism. Due to its implications in various physiological and pathological conditions, such as cancer, neurodegenerative diseases, and metabolic disorders, understanding the function of LRP12 has garnered significant research interest. Recent studies suggest that LRP12 may be involved in modulating cellular responses to stress and regulating gene expression, making it a potential target for therapeutic interventions. The investigation of LRP12 recombinant proteins is essential for elucidating its biological functions, post-translational modifications, and interactions with other cellular components. By employing recombinant technology, researchers aim to produce purified LRP12 proteins, enabling detailed studies on their structural properties and functionality. These insights can deepen our understanding of LRP12's role in health and disease, potentially leading to novel strategies for disease management and drug development.
