Mouse ADAM Metallopeptidase Domain 8 (ADAM8) CLIA Kit
845€ (96 tests)
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935106861
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name
Mouse ADAM Metallopeptidase Domain 8 (ADAM8) CLIA Kit
category
CLIA Kits
provider
Abbexa
reference
abx491773
tested applications
CLIA
Description
Mouse ADAM8 Chemiluminescent Immunoassay (CLIA) Kit is a Sandwich Chemiluminescent Immunoassay (CLIA) Kit for use with Serum, plasma, tissue homogenates and other biological fluids.
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | CLIA Kits |
| Immunogen Target | ADAM Metallopeptidase Domain 8 (ADAM8) |
| Reactivity | Mouse |
| Detection Method | Chemiluminescent |
| Assay Data | Quantitative |
| Assay Type | Sandwich |
| Test Range | 7.81 pg/ml - 500 pg/ml |
| Sensitivity | < 3.3 pg/ml |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Size 1 | 96 tests |
| Size 2 | 5 × 96 tests |
| Size 3 | 10 × 96 tests |
| Form | Lyophilized |
| Tested Applications | CLIA |
| Sample Type | Serum, plasma, tissue homogenates and other biological fluids. |
| Availability | Shipped within 5-20 working days. |
| Storage | Shipped at 4 °C. Upon receipt, store the kit according to the storage instruction in the kit's manual. |
| Dry Ice | No |
| Alias | MS2,CD156,CD156A,ADAM-8 |
| Background | CLIA Kits ADAM8 |
| Status | RUO |
| Note | The validity for this kit is at least 6 months. Up to 12 months validity can be provided on request. This product is for research use only. The range and sensitivity is subject to change. Please contact us for the latest product information. For accurate results, sample concentrations must be diluted to mid-range of the kit. If you require a specific range, please contact us in advance or write your request in your order comments. Please note that our ELISA and CLIA kits are optimised for detection of native samples, rather than recombinant proteins. We are unable to guarantee detection of recombinant proteins, as they may have different sequences or tertiary structures to the native protein. |
Descripción
ADAM metallopeptidase domain 8 (ADAM8), also known as CD156a, is a member of the ADAM family of proteins, which are zinc-dependent transmembrane proteins involved in various biological processes such as cell adhesion, migration, proteolysis, and signaling. ADAM8 is primarily known for its role in inflammation, immune response, and cancer progression. ADAM8 consists of several domains, including a metalloprotease domain, a disintegrin domain, a cysteine-rich domain, an EGF-like domain, a transmembrane domain, and a cytoplasmic tail. These domains enable ADAM8 to participate in cell-cell and cell-matrix interactions and to proteolytically process various substrates.ADAM8 is expressed in various tissues and cell types, including leukocytes (white blood cells), lung epithelial cells, and certain cancer cells. Its expression is often upregulated in response to inflammatory stimuli, suggesting a role in immune responses.ADAM8 is implicated in the regulation of inflammation and immune responses. It has been shown to modulate leukocyte migration, cytokine production, and antigen presentation.ADAM8 can mediate cell adhesion to extracellular matrix components such as fibronectin and collagen. It also plays a role in cell migration by cleaving cell surface proteins involved in cell adhesion and signaling.ADAM8 possesses metalloprotease activity and can cleave various substrates, including cytokines, cell surface receptors, and extracellular matrix proteins. This proteolytic activity can influence cell behavior and tissue remodeling.ADAM8 has been linked to inflammatory diseases such as asthma, rheumatoid arthritis, and multiple sclerosis. It contributes to the pathogenesis of these conditions by modulating immune cell function and inflammation. ADAM8 is also overexpressed in several cancers, including breast cancer, lung cancer, and glioblastoma. Its upregulation is associated with tumor progression, invasion, metastasis, and angiogenesis. ADAM8's proteolytic activity can facilitate cancer cell migration and invasion by cleaving extracellular matrix components and cell adhesion molecules.
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