Human ADAM Metallopeptidase With Thrombospondin Type 1 Motif 13 / vWFCP (ADAMTS13) Protein

Product specifications

Proteins and Peptides

ADAM Metallopeptidase With Thrombospondin Type 1 Motif 13 / vWFCP (ADAMTS13)

E. coli

Human

Unconjugated

Molecular Weight: Calculated MW: 22.3 kDa
Concentration: Prior to lyophilization: 200 µg/ml
Sequence Fragment: Pro682-Cys859
Tag: N-terminal His tag

Recombinant

> 97%

10 µg

50 µg

100 µg

200 µg

500 µg

Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.

WB, SDS-PAGE

Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.

Shipped within 5-7 working days.

Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.

No

Q76LX8

VWF-CP,VWFCP,Von Willebrand Factor-Cleaving Protease,ADAM-TS13,ADAMTS-13,A Disintegrin And Metalloproteinase With Thrombospondin Motifs 13

Protein ADAMTS13

RUO

This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

ADAMTS13 (ADAM metallopeptidase with thrombospondin type 1 motif 13) is a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. ADAMTS13 contains multiple domains, including a signal peptide, a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and multiple thrombospondin type 1 (TSP1) motifs. ADAMTS13 is primarily known for its role in cleaving VWF. VWF normally forms long multimeric strands, which are essential for platelet adhesion and aggregation during clot formation. However, excessively large VWF multimers can lead to thrombotic disorders. ADAMTS13 cleaves these large VWF multimers into smaller, less active forms, thereby regulating platelet aggregation and preventing excessive clot formation. Deficiency or dysfunction of ADAMTS13 can result in a rare but severe condition called thrombotic thrombocytopenic purpura (TTP). In TTP, the lack of functional ADAMTS13 leads to the buildup of large VWF multimers, which can cause widespread microvascular thrombosis and thrombocytopenia. ADAMTS13 may also have other physiological functions that are not fully understood. Some studies suggest potential involvement in angiogenesis, inflammation, and tissue remodeling. Autoantibodies inhibit ADAMTS13 activity, while in hereditary TTP, genetic mutations affect the production or function of ADAMTS13. Both conditions lead to the accumulation of large VWF multimers, resulting in microvascular thrombosis and associated complications. ADAMTS13 activity has also been implicated in other thrombotic disorders, such as arterial thrombosis and stroke.

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