Analytical Data
-
Gene name
SUMF1
- Application
-
Alternative Names
SUMF1；Formylglycine-generating enzyme
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8NBK3
-
Expression Region
34-374aa
-
AA Sequence
SQEAGTGAGAGSLAGSCGCGTPQRPGAHGSSAAAHRYSREANAPGPVPGE RQLAHSKMVPIPAGVFTMGTDDPQIKQDGEAPARRVTIDAFYMDAYEVSN TEFEKFVNSTGYLTEAEKFGDSFVFEGMLSEQVKTNIQQAVAAAPWWLPV KGANWRHPEGPDSTILHRPDHPVLHVSWNDAVAYCTWAGKRLPTEAEWEY SCRGGLHNRLFPWGNKLQPKGQHYANIWQGEFPVTNTGEDGFQGTAPVDA FPPNGYGLYNIVGNAWEWTSDWWTVHHSVEETLNPKGPPSGKDRVKKGGS YMCHRSYCYRYRCAARSQNTPDSSASNLGFRCAADRLPTMDVHHHHHH
-
Molecular Weight
38 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
SUMF1, or Sulfatase Modifying Factor 1, is a crucial post-translational modification enzyme that plays a significant role in the activation of sulfatases by catalyzing the conversion of a specific amino acid, cysteine, to formylglycine. This modification is essential for the proper function of sulfatases, which are a family of enzymes involved in the hydrolysis of sulfate esters from biomolecules. Dysfunctions or deficiencies in sulfatases are linked to several genetic disorders, including multiple sulfatase deficiency (MSD), which can lead to severe developmental issues and metabolic dysfunctions. Understanding SUMF1 and its mechanisms is vital for unraveling the complexities of sulfatase-related diseases and their potential therapeutic interventions. Research into SUMF1 has gained momentum due to its implications in enzyme regulation, cellular signaling, and its potential role in drug development, wherein enhancing or inhibiting SUMF1 activity could provide novel treatment avenues for disorders associated with sulfatase dysfunction. This burgeoning field of study highlights the significance of SUMF1 in both basic biological processes and clinical implications, as it provides insights into the intricate network of post-translational modifications and enzymatic functions necessary for maintaining cellular homeostasis. Furthermore, advances in biotechnological techniques have enabled researchers to explore recombinant SUMF1 proteins, facilitating a deeper understanding of its structure-function relationship and offering possibilities for therapeutic applications. The continued investigation of SUMF1 will not only contribute to our fundamental understanding of enzymatic functions but also pave the way for innovative strategies in treating sulfatase-related diseases.
