Analytical Data
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Gene name
LCE2B
- Application
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Alternative Names
LCE2B; LEP10; SPRL1B; XP5Late cornified envelope protein 2B; Late envelope protein 10; Skin-specific protein Xp5; Small proline-rich-like epidermal differentiation complex protein 1B
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O14633
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Expression Region
1-110aa
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AA Sequence
MSCQQNQQQCQPPPKCPPKCTPKCPPKCPPKCLPQCPAPCSPAVSSCCGPISGGCCGPSSGGCCNSGAGGCCLSHHRPRLFHRRRHQSPDCCESEPSGGSGCCHSSGGCC
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Molecular Weight
38.5 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
The study of LCE2B recombinant protein is situated within the broader context of skin biology and immunology. LCE2B, part of the late cornified envelope (LCE) family, is implicated in the formation of the epidermal barrier and is crucial for maintaining skin homeostasis. Its expression is often upregulated in response to skin lesions and inflammatory conditions, making it a key player in the skin's defense mechanisms. Research has increasingly focused on the potential therapeutic applications of LCE2B in conditions such as psoriasis, eczema, and other skin disorders, where barrier dysfunction is evident. Recombinant technology allows for the production of LCE2B in controlled environments, facilitating the study of its structural and functional properties, as well as its interactions with other epidermal proteins. Understanding the precise role of LCE2B could yield insights into skin repair processes and open up avenues for innovative treatments aimed at enhancing skin barrier function or modulating inflammatory responses. As skin diseases significantly impact quality of life, the exploration of LCE2B offers hope for developing targeted therapies that effectively restore skin health and mitigate chronic dermatological conditions. Thus, research into LCE2B recombinant protein not only deepens our understanding of skin biology but also represents a critical step towards novel interventions in dermatological therapy.
