Analytical Data
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Gene name
SLURP2
- Application
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Alternative Names
SLURP2；Secreted Ly-6/uPAR domain-containing Protein 2
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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
P0DP57
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Expression Region
23-97aa
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AA Sequence
IWCHQCTGFGGCSHGSRCLRDSTHCVTTATRVLSNTEDLPLVTKMCHIGCPDIPSLGLGPYVSIACCQTSLCNHD
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Molecular Weight
10.0 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
SLURP2 (Secreted LY6/uPAR-related protein 2) is a member of the LY6/uPAR protein superfamily, which is known for its diverse roles in cell signaling and immune responses. Discovered due to its expression in human tissues, SLURP2 has garnered attention for its potential physiological and pathological significance. Research indicates that it may play a critical role in various biological processes, including neuromodulation and the regulation of inflammation. Importantly, SLURP2 has been associated with certain neuropathic and inflammatory conditions, hinting at its possible involvement in disease mechanisms. Recent studies have focused on the recombinant production of SLURP2 to facilitate investigations into its structure and function. The recombinant protein allows for advanced assays that can elucidate its interactions with other molecules and its effects on cellular pathways. Understanding SLURP2's mechanisms could provide insights into novel therapeutic strategies for conditions where its dysregulation is implicated. As research progresses, SLURP2 is emerging as a promising target for better understanding complex diseases and exploring new avenues for treatment, showcasing the importance of recombinant protein studies in elucidating the roles of specific proteins in health and disease.
