Analytical Data
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Gene name
SPRL3A
- Application
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Alternative Names
SPRL3A；LEP15；SPRL3A；Late cornified envelope Protein 3C
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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
Q5T5A8
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Expression Region
1-94aa
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AA Sequence
MSCQQNQQQCQPPPSCPSPKCPPKSPAQCLPPPSSDCALSSGGCGPSSESGCCLSHHRHFRSHQCRRQRSNSCDRGSGQQGGGSCRGHGSGGCC
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Molecular Weight
9.7 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
SPRL3A, a member of the SPRL family of proteins, has garnered attention in recent years due to its potential roles in various biological processes, including cellular signaling, immune response, and development. The study of SPRL3A recombinant proteins has been pivotal in understanding its structure-function relationship, as well as its interactions with other cellular components. Researchers aim to elucidate the molecular mechanisms by which SPRL3A influences cellular activities, particularly in the context of cancer and inflammatory diseases. Recombinant protein technology allows for the expression and purification of SPRL3A, facilitating detailed biochemical assays and structural analyses. Understanding the functional properties of SPRL3A could pave the way for developing targeted therapies and diagnostics, especially given its implications in critical pathways that regulate cell behavior. Moreover, SPRL3A’s potential as a biomarker for specific diseases is an area of active investigation, highlighting the necessity to deepen our knowledge of its biological significance. Overall, the exploration of SPRL3A recombinant proteins holds great promise for enhancing our understanding of complex biological systems and advancing medical science.
