Analytical Data
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Gene name
SUMF2
- Application
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Alternative Names
SUMF2; PSEC0171; UNQ1968/PRO4500; Inactive C-alpha-formylglycine-generating enzyme 2; Paralog of formylglycine-generating enzyme; pFGE; Sulfatase-modifying factor 2
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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
Q8NBJ7
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Expression Region
26-301 aa
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AA Sequence
QATSM VQLQGGRFLM GTNSPDSRDG DGPVREATVK PFAIDIFPVT NKDFRDFVRE KKYRTEAEMF GWSFVFEDFV SDELRNKATQ PMKSVLWWLP VEKAFWRQPA GPGSGIRERL EHPVLHVSWN DARAYCAWRG KRLPTEEEWE FAARGGLKGQ VYPWGNWFQP NRTNLWQGKF PKGDKAEDGF HGVSPVNAFP AQNNYGLYDL LGNVWEWTAS PYQAAEQDMR VLRGASWIDT ADGSANHRAR VTTRMGNTPD SASDNLGFRC AADAGRPPGE L
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Molecular Weight
33.8 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
SUMF2, or Sulfatase-Modifying Factor 2, is a crucial protein that plays a significant role in the post-translational modification of sulfatases, which are enzymes that catalyze the hydrolysis of sulfate esters. Deficiencies in sulfatases are associated with various genetic disorders, such as Multiple Sulfatase Deficiency (MSD), which results from the lack of proper enzymatic activity leading to the accumulation of sulfated metabolites. SUMF2, along with its counterpart SUMF1, is essential for the activation of these sulfatases by facilitating the conversion of inactive forms to their active states. The research into SUMF2 is vital for understanding its molecular mechanisms, interactions, and influence on sulfatase activity, particularly regarding its potential therapeutic applications in treating MSD and related conditions. Recent studies have focused on elucidating the structure-function relationship of SUMF2, its role in cellular processes, and its potential implications in enzyme replacement therapies. Advances in structural biology techniques, such as X-ray crystallography and cryo-electron microscopy, have provided insights into SUMF2's functional domains and how mutations can affect its activity, thereby shaping future research directions aimed at developing targeted therapies for sulfatase-related disorders. Understanding SUMF2's biological significance offers a promising avenue for improving diagnostic and treatment strategies that may alleviate the burden of diseases associated with sulfatase deficiencies.
