Analytical Data
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Gene name
SOST
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简介
SOST protein inhibits bone growth by suppressing Wnt signaling and interacting with LRP4 and LRP5. Its interactions with LRP4 and LRP5 play crucial roles in suppressing Wnt signaling. The involvement of SOST in interactions with LRP6 highlights its regulatory role in bone growth. SOST Protein, Rat (Myc, His) is the recombinant rat-derived SOST protein, expressed by E. coli , with N-His, C-Myc labeled tag.
- Application
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Alternative Names
Sost; Sclerostin
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Species
Rat
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Source
E. coli
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Tag
N-His;C-Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99P67
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Expression Region
F29-Y213
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AA Sequence
FKNDATEIIPGLREYPEPPQELENNQTMNRAENGGRPPHHPYDTKDVSEYSCRELHYTRFVTDGPCRSAKPVTELVCSGQCGPARLLPNAIGRVKWWRPNGPDFRCIPDRYRAQRVQLLCPGGAAPRSRKVRLVASCKCKRLTRFHNQSELKDFGPETARPQKGRKPRPRARGAKANQAELENAY
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Protein Length
Full Length of Mature Protein
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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
Collectrin, also known as TMEM27, is a transmembrane protein that plays a crucial role in various physiological processes, particularly in kidney function and glucose homeostasis. Initially discovered for its involvement in the secretion of insulin by pancreatic beta cells, Collectrin has garnered attention due to its implications in metabolic disorders such as obesity and diabetes. Research shows that Collectrin facilitates the proper positioning of glucose transporters and is implicated in the regulation of renal ion balance, making it vital for maintaining homeostasis. Recent studies have explored its potential role as a biomarker for kidney injury and as a therapeutic target for metabolic diseases. The recombinant form of Collectrin/TMEM27 allows for in-depth characterization of its structural and functional properties, enabling scientists to dissect its mechanisms of action and interactions with other proteins within cellular pathways. Thus, understanding the biology of Collectrin not only enhances our knowledge of metabolic regulation but also offers promising avenues for developing interventions for related disorders.
