ELISA/assay

Guinea Pig A Disintegrin like and Metalloproteinase with Thrombospondin type 1 motif 4 ELISA Kit

MBS720625

96 Strip Wells

675 USD

ELISA Kit

Guinea Pig A Disintegrin like and Metalloproteinase with Thrombospondin type 1 motif 4 ELISA Kit

A Disintegrin like and Metalloproteinase with Thrombospondin type 1 motif 4

A disintegrin and metalloproteinase with thrombospondin motifs 4 preproprotein; A disintegrin and metalloproteinase with thrombospondin motifs 4; A disintegrin and metalloproteinase with thrombospondin motifs 4; ADAM-TS4; ADAM-TS 4; aggrecanase-1; OTTHUMP00000032249; a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 4; ADAM metallopeptidase with thrombospondin type 1 motif, 4; ADMP-1; Aggrecanase-1

ADAMTS4

ADAMTS4; ADAMTS4; ADMP-1; ADAMTS-2; ADAMTS-4; KIAA0688; KIAA0688

ATS4_HUMAN

Guinea Pig

Store all reagents at 2-8 degree C

Signal Transduction

157427675

NP_005090.3

NM_005099.4

O75173

90,197 Da

Endochondral Ossification Pathway 198812

This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene lacks a C-terminal TS motif. It is responsible for the degradation of aggrecan, a major proteoglycan of cartilage, and brevican, a brain-specific extracellular matrix protein. The cleavage of aggrecan and brevican suggests key roles of this enzyme in arthritic disease and in the central nervous system, potentially, in the progression of glioma. [provided by RefSeq]

Function: Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the '392-Glu- -Ala-393' site. Catalytic activity: Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu- -Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan. Cofactor: Binds 1 zinc ion per subunit. Subunit structure: Interacts with SRPX2. Ref.8. Subcellular location: Secreted extracellular space extracellular matrix. Tissue specificity: Expressed in brain, lung and heart. Expressed at very low level in placenta and skeletal muscles. Induction: By IL1/interleukin-1. Domain: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. Post-translational modification: The precursor is cleaved by a furin endopeptidase. Sequence similarities: Contains 1 disintegrin domain.Contains 1 peptidase M12B domain.Contains 1 TSP type-1 domain. Caution: Has sometimes been referred to as ADAMTS2. Sequence caution: The sequence BAA31663.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

96 Strip Wells

675 USD