ADAM15 ELISA Kit
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- Target See all ADAM15 ELISA Kits
- ADAM15 (ADAM Metallopeptidase Domain 15 (ADAM15))
- Binding Specificity
- AA 207-696
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Reactivity
- Human
- Detection Method
- Colorimetric
- Method Type
- Sandwich ELISA
- Application
- ELISA
- Purpose
- Sandwich High Sensitivity ELISA kit for Quantitative Detection of Human ADAM15
- Brand
- PicoKine™
- Analytical Method
- Quantitative
- Specificity
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Expression system for standard: NSO
Immunogen sequence: D207-T696 - Cross-Reactivity (Details)
- There is no detectable cross-reactivity with other relevant proteins.
- Characteristics
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Tissue Specificity: Expressed in colon and small intestine. Expressed in airway smooth muscle and glomerular mesangial cells (at protein level). Ubiquitously expressed. Overexpressed in atherosclerotic lesions. Constitutively expressed in cultured endothelium and smooth muscle. Expressed in chondrocytes. Expressed in airway smooth muscle and glomerular mesangial cells. .
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- Plate
- Pre-coated
- Restrictions
- For Research Use only
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- Storage
- 4 °C,-20 °C
- Storage Comment
- Store at 4°C for 6 months, at -20°C for 12 months. Avoid multiple freeze-thaw cycles(Shipped with wet ice.)
- Expiry Date
- 12 months
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- Target See all ADAM15 ELISA Kits
- ADAM15 (ADAM Metallopeptidase Domain 15 (ADAM15))
- Alternative Name
- ADAM15 (ADAM15 Products)
- Synonyms
- ADAM15 ELISA Kit, mdc15 ELISA Kit, MDC15 ELISA Kit, metargidin ELISA Kit, tMDCVI ELISA Kit, ADAM metallopeptidase domain 15 ELISA Kit, ADAM metallopeptidase domain 15 L homeolog ELISA Kit, a disintegrin and metallopeptidase domain 15 (metargidin) ELISA Kit, ADAM15 ELISA Kit, adam15.L ELISA Kit, adam15 ELISA Kit, Adam15 ELISA Kit
- Background
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Protein Function: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. .
Background: Disintegrin and metalloproteinase domain-containing protein 15 is an enzyme that in humans is encoded by the ADAM15 gene. The protein encoded by this gene is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I transmembrane glycoproteins known to be involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. This protein contains multiple functional domains including a zinc-binding metalloprotease domain, a disintegrin-like domain, as well as an EGF-like domain. Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein-tyrosine kinases in a phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed.
Synonyms: Disintegrin and metalloproteinase domain-containing protein 15,ADAM 15,3.4.24.-,Metalloprotease RGD disintegrin protein,Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15,MDC-15,Metargidin,ADAM15,MDC15,
Full Gene Name: Disintegrin and metalloproteinase domain-containing protein 15
Cellular Localisation: Endomembrane system, Single-pass type I membrane protein . Cell junction, adherens junction . Cell projection, cilium, flagellum . Cytoplasmic vesicle, secretory vesicle, acrosome . The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity).. - UniProt
- Q13444
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