Analytical Data
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Gene name
SUFU
- Application
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Alternative Names
SUFU；Suppressor of fused homolog
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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
Q9UMX1
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Expression Region
1-484aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MAELRPSGAP GPTAPPAPGP TAPPAFASLF PPGLHAIYGE CRRLYPDQPN PLQVTAIVKY WLGGPDPLDY VSMYRNVGSP SANIPEHWHY ISFGLSDLYG DNRVHEFTGT DGPSGFGFEL TFRLKRETGE SAPPTWPAEL MQGLARYVFQ SENTFCSGDH VSWHSPLDNS ESRIQHMLLT EDPQMQPVQT PFGVVTFLQI VGVCTEELHS AQQWNGQGIL ELLRTVPIAG GPWLITDMRR GETIFEIDPH LQERVDKGIE TDGSNLSGVS AKCAWDDLSR PPEDDEDSRS ICIGTQPRRL SGKDTEQIRE TLRRGLEINS KPVLPPINPQ RQNGLAHDRA PSRKDSLESD SSTAIIPHEL IRTRQLESVH LKFNQESGAL IPLCLRGRLL HGRHFTYKSI TGDMAITFVS TGVEGAFATE EHPYAAHGPW LQILLTEEFV EKMLEDLEDL TSPEEFKLPK EYSWPEKKLK VSILPDVVFD SPLH
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Molecular Weight
56 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
Related Products
Protein Description
The study of SUFU (Suppressor of Fused) recombinant proteins has gained significant attention in recent years due to their critical role in the Hedgehog signaling pathway, which is essential for various developmental processes and tissue homeostasis. SUFU acts as a negative regulator of this pathway, preventing the activation of downstream target genes when Hedgehog ligands are absent. Dysregulation of SUFU and the Hedgehog pathway has been implicated in various diseases, including cancer, particularly medulloblastoma and basal cell carcinoma. Understanding the structure and function of SUFU recombinant proteins is vital for elucidating their mechanism of action and potential therapeutic implications. Researchers have been focusing on the production of SUFU recombinant proteins to investigate their biophysical properties, binding interactions with other pathway components, and their impact on Hedgehog signaling. By employing techniques such as X-ray crystallography, NMR spectroscopy, and biochemical assays, scientists aim to gain insights into SUFU's role in tumorigenesis and its potential as a target for novel cancer therapies. Overall, the exploration of SUFU recombinant proteins represents a promising frontier in understanding the complexities of cell signaling and developing strategies to combat Hedgehog-related malignancies.
