Recombinant Human ADAMTS8 Protein, MYC/DDK-tagged

• Cat.No.: ADAMTS8-29H
• Product Overview: Recombinant Human ADAMTS8 Protein was expressed in HEK293 cells with C-terminal MYC/DDK tag.

Specification

• Source: HEK293
• Species: Human
• Form: 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol.
• Molecular Mass: 96.3 kDa
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Concentration: >50 ug/mL as determined by microplate BCA method

Gene Information

• Gene Name: ADAMTS8 ADAM metallopeptidase with thrombospondin type 1 motif, 8 [ Homo sapiens ]
• Official Symbol: ADAMTS8
• Synonyms: ADAMTS8; ADAM metallopeptidase with thrombospondin type 1 motif, 8; a disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 8; A disintegrin and metalloproteinase with thrombospondin motifs 8; ADAM TS8; FLJ41712; METH2; METH-2; METH-8; ADAMTS-8; ADAM-TS 8; a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 8; ADAM-TS8
• Gene ID: 11095
• mRNA Refseq: NM_007037
• Protein Refseq: NP_008968
• MIM: 605175
• UniProt ID: Q9UP79

Reviews

06/02/2022

The technician modified my experimental protocol so that my experiment went smoothly.

06/15/2021

Very good after-sales service to get my experiments going!

01/05/2021

The protein composition was stable and concentrated, allowing me to obtain satisfactory experimental results.

Q&As

What is the biological function of ADAMTS8?

ADAMTS8 shows anti-angiogenesis and inhibition of endothelial cell production

What diseases is ADAMTS8 used to study?

ADAMTS8 is used in more studies of heart and cardiovascular diseases

What is ADAMTS8 also called?

ADAMTS8 used to be called METH-2.

Where is ADAMTS8 mainly expressed?

ADAMTS8 is predominantly expressed in the lungs and heart

What is the structure domain of ADAMTS8?

Pre-structural domains, metalloproteinase structural domains, disintegrin-like structural domains, central thrombospondin-like motifs, cysteine-rich structural domains, spacer region structural domains and C-terminal motifs