Human ADAM Metallopeptidase Domain 9 (ADAM9) ELISA Kit

Este producto es parte de ADAM9 - ADAM metallopeptidase domain 9
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546€ (96 tests)

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935106861
info@markelab.com
name
Human ADAM Metallopeptidase Domain 9 (ADAM9) ELISA Kit
category
ELISA Kits
provider
Abbexa
reference
abx250169
tested applications
ELISA

Description

Human ADAM Metallopeptidase Domain 9 (ADAM9) ELISA Kit is an ELISA Kit for the in vitro quantitative measurement of Human ADAM Metallopeptidase Domain 9 (ADAM9) concentrations in serum, plasma and other biological fluids.

Documents del producto

Instrucciones
Data sheet
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Product specifications

CategoryELISA Kits
Immunogen TargetADAM Metallopeptidase Domain 9 (ADAM9)
ReactivityHuman
Detection MethodColorimetric
Assay DataQuantitative
Assay TypeSandwich
Test Range62.5 pg/ml - 4000 pg/ml
Sensitivity37.5 pg/ml
Recommended DilutionOptimal dilutions/concentrations should be determined by the end user.
Size 196 tests
Size 25 × 96 tests
Size 310 × 96 tests
FormLyophilized
Tested ApplicationsELISA
Sample TypeSerum, plasma and other biological fluids.
AvailabilityShipped within 5-7 working days. The validity for this kit is at least 6 months. Up to 12 months validity can be provided on request.
StorageShipped at 4 °C. Upon receipt, store the kit according to the storage instruction in the kit's manual.
Dry IceNo
UniProt IDQ13443
AliasMDC9,MCMP,KIAA0021 ,CORD9,Meltrin Gamma
BackgroundElisa kits for ADAM9
StatusRUO
NoteValidity: 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 9 (ADAM9) is another member of the ADAM family of proteins, sharing structural similarities and functional properties with ADAM8. Like other ADAM proteins, ADAM9 contains 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 ADAM9 to interact with other proteins and participate in various cellular processes.ADAM9 is widely expressed in various tissues and cell types, including the brain, heart, lungs, kidneys, and reproductive organs. Its expression pattern suggests diverse roles in physiological processes.ADAM9 plays a role in cell adhesion and migration by interacting with extracellular matrix components and cell surface receptors. It can promote cell migration by cleaving adhesion molecules and releasing cell-to-cell or cell-to-matrix contacts. As a metalloprotease, ADAM9 has the ability to cleave and process various substrates, including growth factors, cytokines, cell surface receptors, and extracellular matrix proteins. This proteolytic activity allows ADAM9 to regulate signaling pathways, cell behavior, and tissue remodeling. ADAM9 is often upregulated in various cancers, including breast cancer, lung cancer, prostate cancer, and pancreatic cancer. Its overexpression is associated with tumor progression, invasion, metastasis, and angiogenesis. ADAM9 promotes cancer cell migration and invasion by cleaving extracellular matrix proteins and cell adhesion molecules.ADAM9 has been implicated in neurological disorders such as Alzheimer's disease and multiple sclerosis. Its expression in the brain suggests potential roles in synaptic plasticity, neuronal migration, and myelination.ADAM9 has also been linked to cardiovascular diseases such as atherosclerosis and cardiac remodeling. Its involvement in cell adhesion, migration, and proteolysis may contribute to vascular remodeling and plaque formation

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