Analytical Data
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Gene name
Sharpin
- Application
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Alternative Names
Sharpin；SIPL1；Sharpin
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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
Q9H0F6
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Expression Region
1-387aa
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AA Sequence
MAPPAGGAAAAASDLGSAAVLLAVHAAVRPLGAGPDAEAQLRRLQLSADPERPGRFRLELLGAGPGAVNLEWPLESVSYTIRGPTQHELQPPPGGPGTLSLHFLNPQEAQRWAVLVRGATVEGQNGSKSNSPPALGPEACPVSLPSPPEASTLKGPPPEADLPRSPGNLTEREELAGSLARAIAGGDEKGAAQVAAVLAQHRVALSVQLQEACFPPGPIRLQVTLEDAASAASAASSAHVALQVHPHCTVAALQEQVFSELGFPPAVQRWVIGRCLCVPERSLASYGVRQDGDPAFLYLLSAPREAPATGPSPQHPQKMDGELGRLFPPSLGLPPGPQPAASSLPSPLQPSWSCPSCTFINAPDRPGCEMCSTQRPCTWDPLAAAST
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Molecular Weight
47.4 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
The study of Sharpin recombinant proteins stems from the increasing interest in their role within the immune system and their implications in various diseases. Sharpin, or SHANK-associated protein, is a cytoplasmic protein that has been identified as a critical regulator of immune responses, particularly in the formation of immune structures such as the lymph nodes and the maintenance of neutrophil homeostasis. Abnormalities in Sharpin expression or function have been linked to immunodeficiencies and inflammatory conditions, including the severe autoimmune disease known as "Sharpin deficiency." This condition highlights the necessity of Sharpin in the development and function of the immune system. Recent advances in recombinant DNA technology have enabled researchers to produce Sharpin proteins in vitro, allowing for a detailed analysis of their structure and function. Through the study of these recombinant proteins, scientists aim to elucidate the molecular mechanisms by which Sharpin contributes to immune regulation and to explore its potential as a therapeutic target. Furthermore, understanding Sharpin's interactions with other proteins involved in signaling pathways can provide insights into disease mechanisms and guide the development of novel treatments for immune-related disorders. Overall, the investigation of Sharpin recombinant proteins is essential for advancing our knowledge of immune system biology and for developing innovative strategies to combat immune diseases.
