Analytical Data
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Gene name
LZIC
- Application
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Alternative Names
LZIC;Protein LZIC
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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
Q8WZA0
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Expression Region
1-190aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASRGKT ETSKLKQNLE EQLDRLMQQL QDLEECREEL DTDEYEETKK ETLEQLSEFN DSLKKIMSGN MTLVDELSGM QLAIQAAISQ AFKTPEVIRL FAKKQPGQLR TRLAEMDRDL MVGKLERDLY TQQKVEILTA LRKLGEKLTA DDEAFLSANA GAILSQFEKV STDLGSGDKI LALASFEVEK TKK
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Molecular Weight
24 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
LZIC, or LZIC homology domain-containing protein, is a fascinating subject of study in the field of molecular biology due to its potential roles in various biological processes, including cellular signaling and regulation. Recent research has highlighted the significance of LZIC in various diseases, particularly in cancer and metabolic disorders, where its expression levels are often altered. The protein is characterized by its Leucine Zipper (LZ) motif, which facilitates dimerization and interaction with other proteins, suggesting a crucial role in transcriptional regulation. Understanding LZIC's structure, function, and interaction partners is essential for elucidating its biological roles and therapeutic potential. Advances in recombinant protein technology have enabled the creation of LZIC fusion proteins for detailed study, including its biochemical properties, signaling pathways, and implications in pathophysiology. Researchers are employing various techniques, including mutagenesis, crystallography, and super-resolution microscopy, to uncover the functional mechanisms underlying LZIC activity in cells. As we delve deeper into LZIC research, it holds promise not only for unraveling fundamental biological questions but also for leading to potential therapeutic strategies targeting LZIC-related pathways in disease contexts. This exploration positions LZIC as a key player in the landscape of molecular research, making it a prominent target for future studies aimed at developing innovative treatments.
