Analytical Data
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Gene name
SPRL4A
- Application
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Alternative Names
SPRL4A；LEP8；SPRL4A；Late cornified envelope Protein 4A
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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
Q5TA78
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Expression Region
1-99aa
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AA Sequence
MSCQQNQQQCQPPPKCPIPKYPPKCPSKCASSCPPPISSCCGSSSGGCGCCSSEGGGCCLSHHRHHRSHCHRPKSSNCYGSGSGQQSGGSGCCSGGGCC
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Molecular Weight
9.9 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
SPRL4A, a member of the serine protease receptor-like family, has garnered significant attention in recent years due to its potential roles in various biological processes and disease mechanisms. This protein is known to be involved in cellular signaling pathways and may play a critical role in modulating immune responses, cellular differentiation, and apoptosis. Research has indicated that abnormal expression or mutations in SPRL4A could be linked to several disorders, including certain cancers and autoimmune diseases. The recombinant version of this protein is particularly valuable for scientific studies, as it allows for the detailed examination of SPRL4A’s structure-function relationships, interaction with other biomolecules, and its role in physiological and pathological conditions. Producing SPRL4A as a recombinant protein enables researchers to investigate its enzymatic activity, receptor interactions, and potential as a therapeutic target. Additionally, such studies can contribute to the understanding of the underlying mechanisms involved in diseases associated with SPRL4A, paving the way for new diagnostic and therapeutic strategies. As a result, the ongoing research surrounding SPRL4A, especially in its recombinant form, is crucial for elucidating its biological significance and therapeutic potential.
