Cow A Disintegrin And Metalloproteinase With Thrombospondin 2 (ADAMTS2) Protein

Product specifications

Proteins and Peptides

A Disintegrin And Metalloproteinase With Thrombospondin 2 (ADAMTS2)

E. coli

Cow

Unconjugated

Molecular Weight: Calculated MW: 16.6 kDa
Concentration: Prior to lyophilization: 200 µg/ml
Sequence Fragment: Gln474-Pro610
Tag: N-terminal His tag

> 95%

50 µg

100 µg

200 µg

500 µg

1 mg

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 5-12 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

P79331

PCINP,NPI,ADAM-TS2,Procollagen N-Endopeptidase,ADAMTS-2

Protein ADAMTS2

RUO

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

Descripción

ADAMTS2, also known as A Disintegrin And Metalloproteinase with Thrombospondin Motifs 2, is another member of the ADAMTS protein family ADAMTS2, like other members of the ADAMTS family, contains multiple domains including a metalloproteinase domain responsible for its enzymatic activity, as well as thrombospondin type-1 (TSP-1) motifs. ADAMTS2 is primarily known for its role in collagen processing and extracellular matrix remodeling. It specifically cleaves procollagen molecules, which are precursors to collagen, at specific sites to produce mature collagen molecules. This process is crucial for the proper assembly and organization of collagen fibers in various tissues, including skin, bone, and cartilage. Mutations in the ADAMTS2 gene have been linked to a rare genetic disorder called Ehlers-Danlos syndrome type VIIC (EDS VIIC), also known as dermatosparaxis type EDS. EDS VIIC is characterized by severe skin fragility, joint laxity, and easy bruising due to abnormal collagen processing and structure. These mutations disrupt the enzymatic activity of ADAMTS2, leading to impaired collagen processing and the characteristic symptoms of the disorder.Studies on ADAMTS2 and its role in collagen processing have implications for understanding the pathogenesis of connective tissue disorders like Ehlers-Danlos syndrome and for developing potential therapeutic approaches. Research efforts are focused on elucidating the molecular mechanisms underlying ADAMTS2 function and its regulation in collagen metabolism.

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