Analytical Data
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Gene name
SPRL2A
- Application
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Alternative Names
SPRL2A；LEP2；SPRL2A；Late cornified envelope Protein 1B
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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
Q5T7P3
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Expression Region
1-118aa
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AA Sequence
MSCQQNQQQC QPPPKCIPKC PPKCLTPRCP PKCPPKCPPV SSCCSVSSGG CCGSSSGGSC GSSSGGCCSS GGGGCCLSHH RRRRSHCHRP QSSGCCSQPS GGSSCCGGGS GQHSGGCC
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Molecular Weight
11.6 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
SPRL2A, a member of the SPRL (Small Protein with RING-type Ligase) family, has garnered attention in recent scientific research due to its potential roles in cellular processes and disease mechanisms. This protein is characterized by the presence of a RING finger domain, which is known to be associated with E3 ubiquitin ligases, a crucial component of the ubiquitin-proteasome system that regulates protein degradation. The regulation of protein stability and turnover is critical for maintaining cellular homeostasis and has implications in various biological processes, including cell cycle progression, signal transduction, and apoptosis. Dysregulation of these processes can lead to various diseases, including cancer. Recent studies have suggested that SPRL2A may be involved in the modulation of these pathways, although its specific functions and interacting partners are still being elucidated. Understanding the biochemical properties and molecular interactions of SPRL2A could provide insights into its role as a potential therapeutic target, as well as its contribution to the pathogenesis of diseases associated with aberrant protein regulation. Additionally, the generation of SPRL2A recombinant protein provides a valuable tool for researchers to further investigate its functional characteristics and involvement in complex biological networks, paving the way for future studies that aim to unveil its clinical relevance and therapeutic potential.
