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Mouse Anti-ADAMTS1 Recombinant Antibody (V2-179819) (CBMAB-A1182-YC)

Provided herein is a Mouse monoclonal antibody against Human ADAM Metallopeptidase With Thrombospondin Type 1 Motif 1. The antibody can be used for immunoassay techniques, such as WB.
See all ADAMTS1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-179819
Antibody Isotype
IgG1
Application
WB

Basic Information

Immunogen
Human recombinant protein fragment corresponding to amino acids 412-644 of human ADAMTS1 (NP_008919) produced in E.coli.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:2,000

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

Format
PBS, pH 7.3, 1% BSA, 50% glycerol, 0.02% sodium azide
Buffer
PBS, pH7.3, 1% BSA, 50% glycerol
Preservative
0.02% sodium azide
Concentration
1 mg/ml
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
aa 412-644

Target

Full Name
ADAM Metallopeptidase With Thrombospondin Type 1 Motif 1
Introduction
ADAMTS1 is a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) protein family. The expression of this gene may be associated with various inflammatory processes as well as development of cancer cachexia.
Entrez Gene ID
9510
UniProt ID
Q9UHI8
Alternative Names
ADAM Metallopeptidase With Thrombospondin Type 1 Motif 1; A Disintegrin-Like And Metalloprotease (Reprolysin Type) With Thrombospondin Type 1 Motif, 1; ADAM-TS 1; ADAM-TS1; ADAMTS-1; METH-1; METH1; A Disintegrin And Metalloproteinase With Thrombospondin M
Function
Cleaves aggrecan, a cartilage proteoglycan, at the '1938-Glu-|-Leu-1939' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover (By similarity). Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture.
Biological Process
Extracellular matrix organization
Heart trabecula formation
Integrin-mediated signaling pathway
Kidney development
Negative regulation of angiogenesis
Negative regulation of cell population proliferation
Ovulation from ovarian follicle
Positive regulation of G1/S transition of mitotic cell cycle
Positive regulation of vascular associated smooth muscle cell migration
Positive regulation of vascular associated smooth muscle cell proliferation
Cellular Location
Extracellular matrix
PTM
The precursor is cleaved by a furin endopeptidase.
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).

de Assis Lima, M., da Silva, S. V., Serrano-Garrido, O., Huelsemann, M., Santos-Neres, L., Rodríguez-Manzaneque, J. C., ... & Freitas, V. M. (2021). Metalloprotease ADAMTS-1 decreases cell migration and invasion modulating the spatiotemporal dynamics of Cdc42 activity. Cellular Signalling, 77, 109827.

Wang, Y., Xiao, Y., Zheng, Y., Yang, L., & Wang, D. (2021). An anti-ADAMTS1 treatment relieved muscle dysfunction and fibrosis in dystrophic mice. Life Sciences, 119756.

Hu, W., Tang, J., Zhang, Z., Tang, Q., Yan, Y., Wang, P., ... & Chu, M. (2020). Polymorphisms in the ASMT and ADAMTS1 gene may increase litter size in goats. Veterinary Medicine and Science, 6(4), 775-787.

Aydos, O. S., Yukselten, Y., Ozkavukcu, S., Sunguroglu, A., & Aydos, K. (2019). ADAMTS1 and ADAMTS5 metalloproteases produced by Sertoli cells: a potential diagnostic marker in azoospermia. Systems biology in reproductive medicine, 65(1), 29-38.

Tokmak, A., Ozaksit, G., Sarikaya, E., Kuru-Pekcan, M., & Kosem, A. (2019). Decreased ADAMTS-1,-9 and-20 levels in women with endometrial polyps: a possible link between extracellular matrix proteases and endometrial pathologies. Journal of Obstetrics and Gynaecology, 39(6), 845-850.

Rodríguez-Baena, F. J., Redondo-García, S., Peris-Torres, C., Martino-Echarri, E., Fernández-Rodríguez, R., del Carmen Plaza-Calonge, M., ... & Rodríguez-Manzaneque, J. C. (2018). ADAMTS1 protease is required for a balanced immune cell repertoire and tumour inflammatory response. Scientific reports, 8(1), 1-11.

Hirohata, S., Inagaki, J., & Ohtsuki, T. (2017). Diverse Functions of a Disintegrin and Metalloproteinase with Thrombospondin Motif-1. Yakugaku Zasshi: Journal of the Pharmaceutical Society of Japan, 137(7), 811-814.

Xue, W., Zhang, Z., Zeng, S., Xu, Y., Zhang, Q., Wang, W., ... & Hu, X. (2017). Expression and clinical significance of tissue inhibitor of metalloproteinases-1 (TIMP-1) and a disintegrin and metalloproteinase with thrombospondin type 1 motif 1 (ADAMTS1) in post-kidney-transplant bladder tumors. Annals of transplantation, 22, 622-630.

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

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