Analytical Data
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Gene name
GAGA
- Application
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Alternative Names
GAGA;Myc-associated zinc finger Protein
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Species
Drosophila melanogaster
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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
Q08605
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Expression Region
1-130aa
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AA Sequence
MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLL DLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQ TVTKDDYTTH
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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
GAGA protein, a member of the transcription factor family, plays a crucial role in gene regulation and chromatin structure. Initially identified in Drosophila, GAGA is characterized by its ability to bind to specific DNA sequences known as GAGA motifs, which are often found in the promoters of various genes. Research on GAGA protein has expanded significantly due to its involvement in critical biological processes such as development, cell differentiation, and stress responses. Its unique structure, featuring a zinc finger domain and a glutamine-rich region, enables it to interact with other proteins and DNA effectively. The recombinant production of GAGA protein has garnered interest for its potential applications in studying gene expression mechanisms and developing gene therapies. By creating recombinant GAGA, researchers aim to elucidate its functional roles in various cellular contexts, potentially unlocking novel insights into transcriptional regulation and chromatin remodeling. Furthermore, the study of GAGA protein may lead to advancements in understanding genetic disorders associated with aberrant transcription factor activity. Overall, the research on GAGA protein serves as a pivotal area in molecular biology, offering the potential for significant contributions to genetics and therapeutic strategies.
