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Rabbit Anti-ADAM10 Recombinant Antibody (V2-6078) (CBMAB-0023CQ)

This product is a rabbit antibody that recognizes ADAM10. The antibody BA0390 can be used for immunoassay techniques such as: WB, IP.
See all ADAM10 antibodies
Published Data
Rabbit Anti-ADAM10 Recombinant Antibody (BA0390) (CBMAB-0023CQ) in WB
Cells were transfected with ADAM10 siRNA or control siRNA for 48 h and the expression of mRNA and protein of ADAM10 was evaluated by Q-PCR and western blot. ...View More
Lin, X., Huang, M., Xie, F., Zhou, H., Yang, J., & Huang, Q. (2016). Gemcitabine inhibits immune escape of pancreatic cancer by down regulating the soluble ULBP2 protein. Oncotarget, 7(43), 70092.

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat
Clone
V2-6078
Antibody Isotype
IgG
Application
WB, IP

Basic Information

Immunogen
A synthesized peptide derived from human ADAM10
Host Species
Rabbit
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:2,000
IP1:50

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

Buffer
PBS, pH7.4, 50% glycerol, 0.4-0.5mg/ml BSA
Preservative
0.02% sodium azide
Concentration
Batch dependent
Purity
>95% as determined by analysis by SDS-PAGE
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 10
Introduction
Members of the ADAM family are cell surface proteins with a unique structure possessing both potential adhesion and protease domains. The ADAM10 gene encodes a member of the ADAM (a disintegrin and metalloprotease) family and possesses alpha-secretase activity. Tumor necrosis factor-alpha (TNFA) is synthesized as a proinflammatory cytokine from a 233-amino acid precursor. Conversion of the membrane-bound precursor to a secreted mature protein is mediated by a protease termed TNFA convertase. Lunn et al. (1997) found that ADAM10 possesses TNFA convertase activity.
Entrez Gene ID
Human102
Mouse11487
Rat29650
UniProt ID
HumanO14672
MouseO35598
RatQ10743
Alternative Names
ADAM Metallopeptidase Domain 10; Mammalian Disintegrin-Metalloprotease; Kuzbanian Protein Homolog; EC 3.4.24.81; CDw156; MADM; Kuz; A Disintegrin And Metalloproteinase Domain 10; A Disintegrin And Metalloprotease Domain 10; CD156c Antigen; EC 3.4.24; HsT18717; ADAM 10; CD156c; AD10; AD18; RAK
Function
Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' 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 heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA. Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain. Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling.
(Microbial infection) Promotes the cytotoxic activity of S.aureus hly by binding to the toxin at zonula adherens and promoting formation of toxin pores.
Biological Process
Adherens junction organization
Amyloid-beta formation
Amyloid fibril formation
Amyloid precursor protein catabolic process
Cell-cell signaling
Cellular protein metabolic process
Cochlea development
Constitutive protein ectodomain proteolysis
Extracellular matrix disassembly
Integrin-mediated signaling pathway
In utero embryonic development
Membrane protein ectodomain proteolysis
Monocyte activation
Negative regulation of apoptotic process
Negative regulation of cell adhesion
Negative regulation of cell cycle arrest
Negative regulation of gene expression
Neutrophil degranulation
Notch receptor processing, ligand-dependent
Notch signaling pathway
Pore complex assembly
Positive regulation of apoptotic process
Positive regulation of cell growth
Positive regulation of cell migration
Positive regulation of cell population proliferation
Positive regulation of T cell chemotaxis
Postsynapse organization
Post-translational protein modification
Protein phosphorylation
Protein processing
Regulation of dendritic spine morphogenesis
Regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
Regulation of Notch signaling pathway
Regulation of vasculature development
Response to antineoplastic agent
Response to tumor necrosis factor
Spermatogenesis
Toxin transport
Cellular Location
Cytoplasm; Golgi apparatus membrane; Cell membrane; Clathrin-coated vesicle; Adherens junction. Is localized in the plasma membrane but is also expressed in the Golgi apparatus and in clathrin-coated vesicles derived likely from the Golgi. During long term depression, it is recruited to the cell membrane by DLG1. The immature form is mainly located near cytoplasmic fibrillar structures, while the mature form is predominantly located at zonula adherens and the cell membrane. The localization and clustering of mature ADAM10 to zonula adherens is regulated by AFDN, TSPAN33, PLEKHA7 and PDZD11.
Involvement in disease
Reticulate acropigmentation of Kitamura (RAK): A rare cutaneous pigmentation disorder characterized by reticulate, slightly depressed, sharply demarcated brown macules without hypopigmentation, affecting the dorsa of the hands and feet and appearing in the first or second decade of life. The macules gradually darken and extend to the proximal regions of the extremities. The manifestations tend to progress until middle age, after which progression of the eruptions stops. The pigmentary augmentation is found on the flexor aspects of the wrists, neck, patella and olecranon. Other features include breaks in the epidermal ridges on the palms and fingers, palmoplantar pits, occasionally plantar keratoderma, and partial alopecia.
Alzheimer disease 18 (AD18): A late-onset form of Alzheimer disease. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituents of these plaques are neurotoxic amyloid-beta protein 40 and amyloid-beta protein 42, that are produced by the proteolysis of the transmembrane APP protein. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products, such as C31, are also implicated in neuronal death.
Topology
Extracellular: 20-672 aa
Helical: 673-693 aa
Cytoplasmic: 694-748 aa
PTM
The precursor is cleaved by furin and PCSK7.

Persad, A., Pham, N., Moien-Afshari, F., Gormley, W., Yan, S., Mannix, R., & Taghibiglou, C. (2021). Plasma PrPC and ADAM-10 as novel biomarkers for traumatic brain injury and concussion: a pilot study. Brain injury, 1-8.

Chen, Y., Wang, Z., Li, Q., Yu, L., Zhu, Y., Wang, J., & Sun, S. (2020). oxLDL promotes podocyte migration by regulating CXCL16, ADAM10 and ACTN4. Molecular Medicine Reports, 22(3), 1976-1984.

Yang, J., LeBlanc, M. E., Cano, I., Saez-Torres, K. L., Saint-Geniez, M., Ng, Y. S., & D'Amore, P. A. (2020). ADAM10 and ADAM17 proteases mediate proinflammatory cytokine-induced and constitutive cleavage of endomucin from the endothelial surface. Journal of Biological Chemistry, 295(19), 6641-6651.

Huang, J., Pan, Y., Hu, G., Sun, W., Jiang, L., Wang, P., & Ding, X. (2020). SRC fine‐tunes ADAM10 shedding activity to promote pituitary adenoma cell progression. The FEBS journal, 287(1), 190-204.

Xie, Z., Shen, P., Qu, Y., Xu, J., Zheng, C., Gao, Y., & Wang, B. (2020). MiR‐20a inhibits the progression of human arthritis fibroblast‐like synoviocytes and inflammatory factor expression by targeting ADAM10. Environmental toxicology, 35(8), 867-878.

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.

Matthews, A. L., Koo, C. Z., Szyroka, J., Harrison, N., Kanhere, A., & Tomlinson, M. G. (2018). Regulation of leukocytes by TspanC8 tetraspanins and the “molecular scissor” ADAM10. Frontiers in immunology, 9, 1451.

Ge, X., Cui, H., Zhou, Y., Yin, D., Feng, Y., Xin, Q., ... & Zhang, Q. (2017). miR-320a modulates cell growth and chemosensitivity via regulating ADAM10 in gastric cancer. Molecular medicine reports, 16(6), 9664-9670.

Wetzel, S., Seipold, L., & Saftig, P. (2017). The metalloproteinase ADAM10: a useful therapeutic target?. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1864(11), 2071-2081.

Endres, K., & Deller, T. (2017). Regulation of alpha-secretase ADAM10 in vitro and in vivo: genetic, epigenetic, and protein-based mechanisms. Frontiers in molecular neuroscience, 10, 56.

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

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