Analytical Data
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Gene name
FUZ
- Application
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Alternative Names
FLJ22688; fuz; FUZZY_HUMAN; Fy; Protein fuzzy homolog
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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
Q9BT04
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Expression Region
1-418aa
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AA Sequence
MGEEGTGGTVHLLCLAASSGVPLFCRSSRGGAPARQQLPFSVIGSLNGVHMFGQNLEVQLSSARTENTTVVWKSFHDSITLIVLSSEVGISELRLERLLQMVFGAMVLLVGLEELTNIRNVERLKKDLRASYCLIDSFLGDSELIGDLTQCVDCVIPPEGSLLQEALSGFAEAAGTTFVSLVVSGRVVAATEGWWRLGTPEAVLLPWLVGSLPPQTARDYPVYLPHGSPTVPHRLLTLTLLPSLELCLLCGPSPPLSQLYPQLLERWWQPLLDPLRACLPLGPRALPSGFPLHTDILGLLLLHLELKRCLFTVEPLGDKEPSPEQRRRLLRNFYTLVTSTHFPPEPGPPEKTEDEVYQAQLPRACYLVLGTEEPGTGVRLVALQLGLRRLLLLLSPQSPTHGLRSLATHTLHALTPLL
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Molecular Weight
72.1 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
FUZ (forgotten zinc-finger) is a protein that plays a critical role in various cellular processes, including development, cell signaling, and gene regulation. Research into FUZ has gained momentum due to its potential implications in developmental disorders and cancers. Initially identified as a component of the Wnt signaling pathway, FUZ has been found to interact with several key signaling molecules, influencing their activity and localization. Studies have shown that FUZ is crucial for proper embryonic development, particularly in the formation of structures such as the vertebrate body axis and organogenesis. Abnormal FUZ expression or function has been linked to malformations and tumorigenesis, indicating its importance in maintaining cellular homeostasis. Furthermore, the unique zinc-finger domain of FUZ suggests potential regulatory functions in chromatin remodeling and transcriptional regulation. As researchers explore the mechanisms underlying FUZ's role in these biological processes, understanding its detailed signaling pathways and molecular interactions becomes imperative. This knowledge could lead to novel therapeutic strategies for diseases associated with FUZ dysregulation. Consequently, FUZ remains a significant focus of molecular biology and medical research, highlighting its relevance in both fundamental biology and clinical applications.
