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Mouse Anti-ADAM8 Recombinant Antibody (V2-179799) (CBMAB-A1162-YC)

Provided herein is a Mouse monoclonal antibody against Human ADAM Metallopeptidase Domain 8. The antibody can be used for immunoassay techniques, such as ELISA, IP, WB.
See all ADAM8 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-179799
Antibody Isotype
IgG2b
Application
ELISA, IP, WB

Basic Information

Immunogen
NS0-derived, recombinant human A Disintegrin and Metalloprotease-like Domain 8 ectodomain aa158-653
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
ELISA1 μg/ml
WB1-2 μg/ml
IP25 μg/ml

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

Format
Lyophilized
Buffer
PBS, pH 7.4, 5% trehalose
Preservative
None
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 8
Introduction
ADAM8 is a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involvin
Entrez Gene ID
101
UniProt ID
P78325
Alternative Names
ADAM Metallopeptidase Domain 8; A Disintegrin And Metalloproteinase Domain 8; Cell Surface Antigen MS2; MS2; Disintegrin And Metalloproteinase Domain-Containing Protein 8; Human Leukocyte Differentiation Antigen; CD156a Antigen;
Function
Possible involvement in extravasation of leukocytes.
Biological Process
Angiogenesis
Cell-cell adhesion
Cell morphogenesis
Cellular response to hypoxia
Extracellular matrix disassembly
Inflammatory response
Leukocyte migration involved in inflammatory response
Lymphocyte chemotaxis
Negative regulation of neuron apoptotic process
Neutrophil degranulation
Positive regulation of acute inflammatory response
Positive regulation of bone resorption
Positive regulation of cell adhesion
Positive regulation of cellular extravasation
Positive regulation of eosinophil migration
Positive regulation of fibronectin-dependent thymocyte migration
Positive regulation of innate immune response
Positive regulation of MAP kinase activity
Positive regulation of membrane protein ectodomain proteolysis
Positive regulation of neutrophil extravasation
Positive regulation of NF-kappaB transcription factor activity
Positive regulation of protein kinase B signaling
Positive regulation of protein processing
Positive regulation of protein secretion
Positive regulation of T cell differentiation in thymus
Positive regulation of thymocyte apoptotic process
Positive regulation of tumor necrosis factor (ligand) superfamily member 11 production
Regulation of cell-cell adhesion
Cellular Location
Membrane
Topology
Extracellular: 17-655 aa
Helical: 656-676 aa
Cytoplasmic: 677-824 aa

Park, G. B., Choi, S., Yoon, Y. S., & Kim, D. (2021). TrkB/C-induced HOXC6 activation enhances the ADAM8-mediated metastasis of chemoresistant colon cancer cells. Molecular Medicine Reports, 23(6), 1-10.

Awan, T., Babendreyer, A., Wozniak, J., Alvi, A. M., Sterzer, V., Cook, L., ... & Ludwig, A. (2021). Expression of the Metalloproteinase ADAM8 Is Upregulated in Liver Inflammation Models and Enhances Cytokine Release In Vitro. Mediators of inflammation, 2021.

Awan, T., Babendreyer, A., Mahmood Alvi, A., Düsterhöft, S., Lambertz, D., Bartsch, J. W., ... & Ludwig, A. (2021). Expression levels of the metalloproteinase ADAM8 critically regulate proliferation, migration and malignant signalling events in hepatoma cells. Journal of cellular and molecular medicine, 25(4), 1982-1999.

van der Vorst, E. P., & Donners, M. M. (2019). ADAM8 in the cardiovascular system: An innocent bystander with clinical use?. Atherosclerosis, 286, 147-149.

Gao, Y., Yu, X., Zhang, F., & Dai, J. (2019). Propofol inhibits pancreatic cancer progress under hypoxia via ADAM 8. Journal of Hepato‐Biliary‐Pancreatic Sciences, 26(6), 219-226.

Chung, H. W., Kim, J. J., Choi, J. I., Lee, H. R., & Lim, J. B. (2019). A disintegrin and metalloproteinase 8 as a potential blood biomarker for early diagnosis of gastric cancer. Yonsei medical journal, 60(8), 713-719.

Conrad, C., Benzel, J., Dorzweiler, K., Cook, L., Schlomann, U., Zarbock, A., ... & Bartsch, J. W. (2019). ADAM8 in invasive cancers: links to tumor progression, metastasis, and chemoresistance. Clinical Science, 133(1), 83-99.

Polverino, F., Rojas-Quintero, J., Wang, X., Petersen, H., Zhang, L., Gai, X., ... & Owen, C. A. (2018). A disintegrin and metalloproteinase domain-8: a novel protective proteinase in chronic obstructive pulmonary disease. American journal of respiratory and critical care medicine, 198(10), 1254-1267.

Johansson, M. W., Khanna, M., Bortnov, V., Annis, D. S., Nguyen, C. L., & Mosher, D. F. (2017). IL‐5‐stimulated eosinophils adherent to periostin undergo stereotypic morphological changes and ADAM 8‐dependent migration. Clinical & Experimental Allergy, 47(10), 1263-1274.

Aung, W. P. P., Chotjumlong, P., Pata, S., Montreekachon, P., Supanchart, C., Khongkhunthian, S., ... & Krisanaprakornkit, S. (2017). Inducible expression of A Disintegrin and Metalloproteinase 8 in chronic periodontitis and gingival epithelial cells. Journal of periodontal research, 52(3), 582-593.

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

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