Human ADAMTS5 ELISA Kit (V2LY-0626-LY4305)

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Tested Data
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Basic Information

Sensitivity
4.69 ng/mL
Detection Range
10-2000 ng/mL
Sample Type
Serum, Plasma, cell culture supernates
Specificity
Human
Assay Type
Sandwich
Reactivity
Human
Assay Time
1.5 h
Molecule Mass
101.7 kDa
Components
  • Pre-coated ELISA Plate: 12 wells * 8 detachable strips
  • Standard solution: 0.5ml x1
  • Standard diluent: 3ml x1
  • Streptavidin-HRP: 6ml x1
  • Stop solution: 6ml x1
  • Substrate solution A: 6ml x1
  • Substrate solution B: 6ml x1
  • Wash buffer concentrate (25x): 20ml x1
  • Biotinylated antibody: 1ml x1

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 2-8°C
More Infomation

Target

Full Name
ADAM Metallopeptidase With Thrombospondin Type 1 Motif 5
Function
Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its VCAN remodeling properties. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration (By similarity). Participates in development of brown adipose tissue and browning of white adipose tissue (By similarity). Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection.
Biological Process
Defense response to bacterium
Extracellular matrix disassembly
Extracellular matrix organization
Myoblast fusion
Negative regulation of cold-induced thermogenesis
Proteolysis
Tooth eruption
Cellular Location
Extracellular matrix
PTM
The precursor is cleaved by furin and PCSK7 outside of the cell.
Glycosylated. Can be 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. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).

Wang, W., Zhang, H., Hou, C., Liu, Q., Yang, S., Zhang, Z., ... & Yang, X. (2021). Internal modulation of proteolysis in vascular extracellular matrix remodeling: role of ADAM metallopeptidase with thrombospondin type 1 motif 5 in the development of intracranial aneurysm rupture. Aging (Albany NY), 13(9), 12800.

Weng, K., Luo, M., & Dong, D. (2020). Elucidation of the Mechanism by Which a ADAMTS5 Gene MicroRNA-Binding Site Single Nucleotide Polymorphism Affects the Risk of Osteoarthritis. Genetic Testing and Molecular Biomarkers, 24(8), 467-477.

Zeng, T., Gan, J., Liu, Y., Shi, L., Lu, Z., Xue, Y., ... & Yuan, J. (2020). ADAMTS-5 decreases in aortas and plasma from aortic dissection patients and alleviates angiotensin II-induced smooth muscle-cell apoptosis. Frontiers in Cardiovascular Medicine, 7.

Ozler, S., Oztas, E., Gumus Guler, B., Erel, O., Turhan Caglar, A., Ergin, M., ... & Danisman, N. (2020). Are serum levels of ADAMTS5, TAS and TOS at 24–28 gestational weeks associated with adverse perinatal outcomes in gestational diabetic women?. Journal of Obstetrics and Gynaecology, 40(5), 619-625.

Wang, Z., Ye, D., Ye, J., Wang, M., Liu, J., Jiang, H., ... & Wan, J. (2019). ADAMTS-5 decreases in coronary arteries and plasma from patients with coronary artery disease. Disease markers, 2019.

Fava, M., Barallobre-Barreiro, J., Mayr, U., Lu, R., Didangelos, A., Baig, F., ... & Mayr, M. (2018). Role of ADAMTS-5 in aortic dilatation and extracellular matrix remodeling. Arteriosclerosis, thrombosis, and vascular biology, 38(7), 1537-1548.

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For research use only. Not intended for any clinical use.

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