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Human Anti-ADAM17 Recombinant Antibody (V2-179767) (CBMAB-A1129-YC)

Provided herein is a Human monoclonal antibody against Human ADAM Metallopeptidase Domain 17. The antibody can be used for immunoassay techniques, such as FuncS.
See all ADAM17 antibodies

Summary

Host Animal
Human
Specificity
Human
Clone
V2-179767
Antibody Isotype
IgG1
Application
INeutralizationhibitioNeutralization

Basic Information

Immunogen
Recombinant human ADAM17 (TACE) ectodomain tagged to biotin
Host Species
Human
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
Inhibition30 μg/ml

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

Buffer
PBS
Preservative
None
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.

Target

Full Name
ADAM Metallopeptidase Domain 17
Introduction
ADAM17 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 biologic processes involving
Entrez Gene ID
6868
UniProt ID
P78536
Alternative Names
ADAM Metallopeptidase Domain 17; Tumor Necrosis Factor, Alpha, Converting Enzyme; Snake Venom-Like Protease; TNF-Alpha Convertase; EC 3.4.24.86; TACE; CSVP; Disintegrin And Metalloproteinase Domain-Containing Protein 17; ADAM Metallopeptidase Domain 18;
Function
Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2. Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R.
Biological Process
Amyloid precursor protein catabolic process
B cell differentiation
Cell adhesion
Cell adhesion mediated by integrin
Cell motility
Cellular response to high density lipoprotein particle stimulus
Defense response to Gram-positive bacterium
Epidermal growth factor receptor signaling pathway
Germinal center formation
Membrane protein ectodomain proteolysis
Membrane protein intracellular domain proteolysis
Negative regulation of cold-induced thermogenesis
Negative regulation of inflammatory response to antigenic stimulus
Negative regulation of transforming growth factor beta receptor signaling pathway
Neutrophil mediated immunity
Notch receptor processing
Notch signaling pathway
Positive regulation of blood vessel endothelial cell migration
Positive regulation of cell growth
Positive regulation of cell migration
Positive regulation of cell population proliferation
Positive regulation of cellular component movement
Positive regulation of chemokine production
Positive regulation of cyclin-dependent protein serine/threonine kinase activity
Positive regulation of epidermal growth factor-activated receptor activity
Positive regulation of G1/S transition of mitotic cell cycle
Positive regulation of leukocyte chemotaxis
Positive regulation of protein phosphorylation
Positive regulation of T cell chemotaxis
Positive regulation of transforming growth factor beta receptor signaling pathway
Positive regulation of tumor necrosis factor-mediated signaling pathway
Positive regulation of vascular endothelial cell proliferation
Protein processing
Proteolysis
Receptor transactivation
Regulation of mast cell apoptotic process
Response to drug
Response to hypoxia
Response to lipopolysaccharide
Spleen development
T cell differentiation in thymus
Tumor necrosis factor-mediated signaling pathway
Wound healing, spreading of epidermal cells
Cellular Location
Membrane
Involvement in disease
Inflammatory skin and bowel disease, neonatal, 1 (NISBD1): A disorder characterized by inflammatory features with neonatal onset, involving the skin, hair, and gut. The skin lesions involve perioral and perianal erythema, psoriasiform erythroderma, with flares of erythema, scaling, and widespread pustules. Gastrointestinal symptoms include malabsorptive diarrhea that is exacerbated by intercurrent gastrointestinal infections. The hair is short or broken, and the eyelashes and eyebrows are wiry and disorganized.
Topology
Extracellular: 215-671 aa
Helical: 672-692 aa
Cytoplasmic: 693-824 aa
PTM
The precursor is cleaved by a furin endopeptidase.
Phosphorylated. Stimulation by growth factor or phorbol 12-myristate 13-acetate induces phosphorylation of Ser-819 but decreases phosphorylation of Ser-791. Phosphorylation at THR-735 by MAPK14 is required for ADAM17-mediated ectodomain shedding.

Wang, H., Sun, X., VonCannon, J. L., Kon, N. D., Ferrario, C. M., & Groban, L. (2021). Estrogen receptors are linked to angiotensin-converting enzyme 2 (ACE2), ADAM metallopeptidase domain 17 (ADAM-17), and transmembrane protease serine 2 (TMPRSS2) expression in the human atrium: insights into COVID-19. Hypertension Research, 44(7), 882-884.

Kothari, V., Tang, J., He, Y., Kramer, F., Kanter, J. E., & Bornfeldt, K. E. (2021). ADAM17 Boosts Cholesterol Efflux and Downstream Effects of High-Density Lipoprotein on Inflammatory Pathways in Macrophages. Arteriosclerosis, Thrombosis, and Vascular Biology, 41(6), 1854-1873.

Radziejewska, I., Borzym‑Κluczyk, M., & Leszczyńska, K. (2021). Luteolin alters MUC1 extracellular domain, sT antigen, ADAM‑17, IL‑8, IL‑10 and NF‑κB expression in Helicobacter pylori‑infected gastric cancer CRL‑1739 cells: A preliminary study. Biomedical Reports, 14(2), 1-1.

Saha, S. K., Choi, H. Y., Yang, G. M., Biswas, P. K., Kim, K., Kang, G. H., ... & Cho, S. G. (2020). GPR50 promotes hepatocellular carcinoma progression via the Notch signaling pathway through direct interaction with ADAM17. Molecular Therapy-Oncolytics, 17, 332-349.

Chen, K., Shirley, W., & Sun, Z. (2019). Conditional Kidney-Specific Knockout of ADAM17 Causes Arterial Stiffness and Hypertension. Circulation, 140(Suppl_1), A16334-A16334.

Nayak, A., Das, S., Nayak, D., Sethy, C., Narayan, S., & Kundu, C. N. (2019). Nanoquinacrine sensitizes 5-FU-resistant cervical cancer stem-like cells by down-regulating Nectin-4 via ADAM-17 mediated NOTCH deregulation. Cellular Oncology, 42(2), 157-171.

Erin, N., Türker, S., Elpek, Ö., & Yildirim, B. (2018). ADAM proteases involved in inflammation are differentially altered in patients with gastritis or ulcer. Experimental and therapeutic medicine, 15(2), 1999-2005.

Motani, K., & Kosako, H. (2018). Activation of stimulator of interferon genes (STING) induces ADAM17-mediated shedding of the immune semaphorin SEMA4D. Journal of Biological Chemistry, 293(20), 7717-7726.

Grötzinger, J., Lorenzen, I., & Düsterhöft, S. (2017). Molecular insights into the multilayered regulation of ADAM17: the role of the extracellular region. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1864(11), 2088-2095.

González-Foruria, I., Santulli, P., Chouzenoux, S., Carmona, F., Chapron, C., & Batteux, F. (2017). Dysregulation of the ADAM17/Notch signalling pathways in endometriosis: from oxidative stress to fibrosis. MHR: Basic science of reproductive medicine, 23(7), 488-499.

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

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