ADAMTS13 Recombinant Rabbit Monoclonal Antibody [JG39-21] (ET7108-86)

UNIPROT #

Q76LX8

PROTEIN NAME

ADAMTS13

SYNONYMS

A disintegrin and metalloproteinase with thrombospondin motifs 13 antibody;A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif 13 antibody;A disintegrin like and metalloprotease with thrombospondin type 1 motif 13 antibody;ADAM metallopeptidase with thrombospondin type 1 motif 13 antibody;ADAM TS antibody;ADAM-TS 13 antibody;ADAM-TS13 antibody;ADAMTS 13 antibody;ADAMTS-13 antibody;ADAMTS13 antibody;ADAMTS13 protein antibody;ATS13_HUMAN antibody;C9orf8 antibody;TTP antibody;Von Willebrand factor cleaving protease antibody;von Willebrand factor-cleaving protease antibody;vWF cleaving protease antibody;vWF CP antibody;vWF-cleaving protease antibody;vWF-CP antibody;vWFCP antibody

TISSUE SPECIFICITY

Plasma. Expressed primarily in liver.

POST-TRANSLATIONAL MODIFICATION

Glycosylated. O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS13. May also be C-glycosylated on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and also N-glycosylated. These other glycosylations can also facilitate secretion.; The precursor is processed by a furin endopeptidase which cleaves off the pro-domain.

SUBCELLULAR LOCATION

Secreted.

FUNCTION

ADAMTS13 (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13)—also known as von Willebrand factor-cleaving protease (VWFCP)—is a zinc-containing metalloprotease enzyme that cleaves von Willebrand factor (vWf), a large protein involved in blood clotting. It is secreted in blood and degrades large vWf multimers, decreasing their activity. Glycosylated. O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X2-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL.