Analytical Data
-
基因名
SUMF2
- Application
-
别名
SUMF2; PSEC0171; UNQ1968/PRO4500; Inactive C-alpha-formylglycine-generating enzyme 2; Paralog of formylglycine-generating enzyme; pFGE; Sulfatase-modifying factor 2
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q8NBJ7
-
表达区间
26-301 aa
-
氨基酸序列
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
-
分子量
33.8 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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.
