Analytical Data
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Gene name
SPINT2
- Application
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Alternative Names
SPINT2;HAI2;KOP;Kunitz-type protease inhibitor 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
O43291
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Expression Region
28-197aa
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AA Sequence
ADRERSIHDFCLVSKVVGRCRASMPRWWYNVTDGSCQLFVYGGCDGNSNN YLTKEECLKKCATVTENATGDLATSRNAADSSVPSAPRRQDSEDHSSDMF NYEEYCTANAVTGPCRASFPRWYFDVERNSCNNFIYGGCRGNKNSYRSEE ACMLRCFRQQENPPLPLGSKVDHHHHHH
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Molecular Weight
20 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
SPINT2, or Serine Proteinase Inhibitor, is a member of the serpin family and plays a crucial role in regulating serine proteases, which are enzymes that participate in various physiological processes, including inflammation, tissue remodeling, and cell signaling. Research has indicated that SPINT2 is involved in the modulation of proteolytic activity and may have implications in pathological conditions, such as cancer, cardiovascular diseases, and neurodegenerative disorders. Its expression levels and functional mechanisms have garnered attention, particularly in understanding how SPINT2 can influence disease progression through its inhibitory effects on proteases. The recombinant production of SPINT2 allows for detailed studies of its structure-function relationships and facilitates the development of potential therapeutic interventions. By generating high-purity SPINT2 proteins, researchers can explore its role in cellular pathways, assess its binding affinities to specific target proteases, and evaluate its efficacy in preclinical models. This research not only enhances our understanding of SPINT2’s biological significance but also contributes to the broader field of protease regulation, opening avenues for novel drug development aimed at conditions where serine protease activity is dysregulated. Thus, SPINT2 emerges as a pivotal molecule in both basic and translational research, offering valuable insights into therapeutic strategies for a variety of diseases linked to protease activity.
