Analytical Data
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Gene name
LW-1
- Application
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Alternative Names
HSFX1; LW-1;; HSFX2Heat shock transcription factor; X-linked
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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
Q9UBD0
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Expression Region
1-423aa
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AA Sequence
MEDKRSLSMARCEERNSRGQDHGLERVPFPPQLQSETYLHPADPSPAWDDPGSTGSPNLRLLTEEIAFQPLAEEASFRRPHPDGDVPPQGEDNLLSLPFPQKLWRLVSSNQFSSIWWDDSGACRVINQKLFEKEILKRDVAHKVFATTSIKSFFRQLNLYGFRKRRQCTFRTFTRIFSAKRLVSILNKLEFYCHPYFQRDSPHLLVRMKRRVGVKSAPRHQEEDKPEAAGSCLAPADTEQQDHTSPNENDQVTPQHREPAGPNTQIRSGSAPPATPVMVPDSAVASDNSPVTQPAGEWSEGSQAHVTPVAAVPGPAALPFLYVPGSPTQMNSYGPVVALPTASRSTLAMDTTGLPAPGMLPFCHLWVPVTLVAAGAAQPAASMVMFPHLPALHHHCPHSHRTSQYMPASDGPQAYPDYADQST
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Molecular Weight
72.27 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 LW-1 recombinant protein has garnered significant attention in the field of molecular biology and biotechnology due to its potential applications in therapeutic development and disease diagnosis. Originally derived from the LW-1 gene, which encodes a protein with intriguing properties, researchers have focused on its role in cellular processes and its implications in various pathologies. The LW-1 protein is believed to play a crucial role in immune response modulation, making it a candidate for vaccine development and autoimmune disease treatments. Moreover, studies have indicated that recombinant forms of LW-1 can enhance the efficacy of existing therapies or serve as biomarkers for certain diseases, thereby facilitating early diagnosis and personalized medicine approaches. The production of LW-1 as a recombinant protein allows for higher yields and better purity compared to traditional extraction methods, paving the way for further exploration of its biochemical properties and therapeutic potential. Ongoing research is aimed at elucidating the protein's structure-function relationships and understanding the underlying mechanisms of its bioactivity, which could lead to novel therapeutic interventions and advancements in biomedical research. As a result, the LW-1 recombinant protein stands at the forefront of innovative strategies in protein engineering and molecular therapeutics, reflecting the growing intersection between basic research and clinical application.
