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Rat Anti-ADAM15 Recombinant Antibody (V2-179757) (CBMAB-A1119-YC)

Provided herein is a Rat monoclonal antibody against Mouse ADAM Metallopeptidase Domain 15. The antibody can be used for immunoassay techniques, such as WB.
See all ADAM15 antibodies

Summary

Host Animal
Rat
Specificity
Mouse
Clone
V2-179757
Antibody Isotype
IgG2
Application
WB

Basic Information

Immunogen
Mouse recombinant protein of ADAM15 ectodomain.
Host Species
Rat
Specificity
Mouse
Antibody Isotype
IgG2
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:1,000

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

Format
Lyophilized
Buffer
PBS
Preservative
None
Concentration
0.5 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.

Target

Full Name
ADAM Metallopeptidase Domain 15
Introduction
ADAM15 is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I transmembrane glycoproteins known to be involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules
Entrez Gene ID
11490
UniProt ID
O88839
Alternative Names
ADAM Metallopeptidase Domain 15; Metalloproteinase-Like, Disintegrin-Like, And Cysteine-Rich Protein 15; A Disintegrin And Metalloproteinase Domain 15 (Metargidin); Metalloprotease RGD Disintegrin Protein; Metargidin; MDC-15;
Function
Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.
Biological Process
Angiogenesis
Cardiac epithelial to mesenchymal transition
Cell-matrix adhesion
Cellular response to phorbol 13-acetate 12-myristate
Collagen catabolic process
Extracellular matrix disassembly
Extracellular matrix organization
Immune response to tumor cell
Innate immune response
Integrin-mediated signaling pathway
Male gonad development
Negative regulation of cell growth
Negative regulation of cell-matrix adhesion
Negative regulation of cell migration
Negative regulation of receptor binding
Response to hypobaric hypoxia
Tissue regeneration
Cellular Location
Endomembrane system; Adherens junction. The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity).
Topology
Extracellular: 207-696 aa
Helical: 697-717 aa
Cytoplasmic: 718-863 aa
PTM
The precursor is cleaved by a furin endopeptidase.
Phosphorylation increases association with PTKs.

Wang, X., Rojas-Quintero, J., Zhang, D., Nakajima, T., Walker, K. H., Peh, H. Y., ... & Owen, C. A. (2021). A disintegrin and metalloproteinase domain-15 deficiency leads to exaggerated cigarette smoke-induced chronic obstructive pulmonary disease (COPD)-like disease in mice. Mucosal Immunology, 14(2), 342-356.

Chute, M. (2021). The Role of Disintegrin and Metalloproteinase 15 (ADAM15) in Myocardial Infarction.

Yang, Q., Pei, R., Wang, Y., Zhou, Y., Yang, M., Chen, X., & Chen, J. (2021). ADAM15 participates in tick-borne encephalitis virus replication. Journal of Virology, 95(4), e01926-20.

Wang, X., Zhang, D., Higham, A., Wolosianka, S., Gai, X., Zhou, L., ... & Owen, C. A. (2020). ADAM15 expression is increased in lung CD8+ T cells, macrophages, and bronchial epithelial cells in patients with COPD and is inversely related to airflow obstruction. Respiratory research, 21(1), 1-17.

Jana, S., Chute, M., Hu, M., Winkelaar, G., Owen, C. A., Oudit, G. Y., & Kassiri, Z. (2020). ADAM (a disintegrin and metalloproteinase) 15 deficiency exacerbates Ang II (angiotensin II)–Induced aortic remodeling leading to abdominal aortic aneurysm. Arteriosclerosis, thrombosis, and vascular biology, 40(8), 1918-1934.

Aujla, P., Jana, S., Chute, M., & Kassiri, Z. (2020, July). Role of a Disintegrin and Metalloproteinase 15 in Cardiac Hypertrophy and Fibrosis Following Pressure Overload. In Circulation Research (Vol. 127, No. Suppl_1, pp. A282-A282). Hagerstown, MD: Lippincott Williams & Wilkins.

Mattern, J., Roghi, C. S., Hurtz, M., Knäuper, V., Edwards, D. R., & Poghosyan, Z. (2019). ADAM15 mediates upregulation of Claudin-1 expression in breast cancer cells. Scientific reports, 9(1), 1-14.

Horowitz, J. D., & Liu, S. (2018). ADAM-15 and glycocalyx shedding: a new perspective on sepsis-related vasomotor dysfunction.

Li, H., Guo, X., Li, Q., Ran, P., Xiang, X., Yuan, Y., ... & Zheng, S. (2018). Long non-coding RNA 1308 promotes cell invasion by regulating the miR-124/ADAM 15 axis in non-small-cell lung cancer cells. Cancer management and research, 10, 6599.

Yang, X., Meegan, J. E., Jannaway, M., Coleman, D. C., & Yuan, S. Y. (2018). A disintegrin and metalloproteinase 15-mediated glycocalyx shedding contributes to vascular leakage during inflammation. Cardiovascular research, 114(13), 1752-1763.

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

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