Analytical Data
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Gene name
Adamts13
- Application
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Alternative Names
Adamts13；C9orf8；A disintegrin and metalloProteinase with thrombospondin motifs 13
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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
Q76LX8
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Expression Region
1328-1427aa
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AA Sequence
FINVAPHARIAIHALATNMGAGTEGANASYILIRDTHSLRTTAFHGQQVL YWESESSQAEMEFSEGFLKAQASLRGQYWTLQSWVPEMQDPQSWKGKEGT
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Molecular Weight
37 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
ADAMTS13 is a metalloproteinase that plays a crucial role in the regulation of von Willebrand factor (VWF) in the bloodstream. It is primarily responsible for cleaving large VWF multimers into smaller, functionally active forms, thereby preventing excessive platelet aggregation and the formation of thrombi. Deficiencies or dysfunctions in ADAMTS13 are linked to disordered blood coagulation states, particularly thrombotic thrombocytopenic purpura (TTP), a life-threatening condition characterized by microangiopathic hemolytic anemia and thrombocytopenia. Research into recombinant ADAMTS13 has emerged as a potential therapeutic strategy for TTP and similar coagulation disorders. Recombinant forms of ADAMTS13 aim to restore its function in patients with congenital or acquired deficiencies. Additionally, understanding the structure-function relationship and the molecular mechanisms of ADAMTS13 can provide insights into its role in hemostasis and thrombosis. Studies have focused on optimizing the production and stability of recombinant ADAMTS13 to enhance its clinical efficacy. The therapeutic potential of this protein underscores the importance of ongoing research to develop effective treatments for conditions associated with VWF dysregulation, ultimately improving patient outcomes in coagulation disorders.
