Analytical Data
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Gene name
SULF1
- Application
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Alternative Names
HSULF-1; Extracellular sulfatase Sulf-1
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Species
Human
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Source
E. coli
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Tag
Two N- s, His- & SUMO-
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IWU6
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Expression Region
Pro609~Gly871
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Molecular Weight
45&35kDa
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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
SULF1, a member of the sulfatase family, is an important enzyme that plays a critical role in the regulation of heparan sulfate (HS) proteoglycans, which are pivotal in various biological processes, including cell signaling, development, and tumorigenesis. Research into SULF1 has gained attention due to its potential implications in cancer biology, particularly in modulating the activity of growth factors and their receptors. Elevated levels of SULF1 have been associated with various cancer types, where it may contribute to tumor progression by altering the HS landscape and impacting signaling pathways such as Wnt and FGF. Additionally, SULF1 has been implicated in the regulation of stem cell behavior and the tumor microenvironment, making it a promising target for therapeutic interventions. Recent studies have focused on the structural and functional characterization of the recombinant SULF1 protein, aiming to elucidate its enzymatic mechanisms and interactions with HS substrates. Understanding SULF1's role at the molecular level could inform novel strategies for cancer treatment and regenerative medicine. Overall, the study of SULF1 and its recombinant protein holds significant promise for enhancing our understanding of cell biology and developing targeted therapies for malignancies where heparan sulfate dysregulation plays a key role.
