Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species
ADAM8 on leukocytes holds a proinflammatory function in acute lung inflammation by promoting alveolar leukocyte recruitment.
miR (show MLXIP ELISA Kits)-720 is elevated in serum of patients with ADAM8-high TNBC and, in a group with other miRNAs downstream of ADAM8, holds promise as a biomarker for early detection of or treatment response of ADAM8-positive triple-negative breast cancer
ADAM8 causes temozolomide resistance in glioblastoma cells by enhancing pAkt/PI3K, pERK1/2, and cleavage of CD44 and HGF R/c-met
ADAM8 promotes GC cell proliferation and invasion, and its expression is positively correlated with poor survival, indicating that it might be a promising target in GC therapy
ADAM8 expression is associated with increased migration and invasiveness of pancreatic ductal adenocarcinoma cells.
ADAM8 and endostatin (show COL18A1 ELISA Kits) play a role in osteosarcoma progression.
Data indicate that fibronectin fragments (FN-fs) are present in adult ntervertebral disc (IVD) from adult subjects, and ADAM-8, known to cleave FN, is present at the pericellular matrix of disc cells.
Results show that ADAM8 is overexpressed in colorectal cancer and promotes cell growth.
N-glycosylation is essential for processing, localization, stability, and activity of ADAM8.
ADAM8 expression is increased in both severe asthma and COPD (show ARCN1 ELISA Kits) and associated with sputum total cell count and neutrophils. ADAM8 may facilitate neutrophil migration to the airways in severe asthma and COPD (show ARCN1 ELISA Kits).
The important role of ADAM8 in the progression of hepatocellular carcinoma induced by diethylnitrosamine in mice
ADAM8 mediates an enhanced invasiveness of neutrophils into injured muscle fibers by the removal of their adhesiveness to blood vessels after infiltration into interstitial tissues.
ADAM8 has anti-inflammatory activities during allergic airway inflammation in mice
overexpression of PrP(C (show PRNP ELISA Kits)) led to up-regulation of ADAM8, suggesting that PrP(C (show PRNP ELISA Kits)) may regulate its own alpha-cleavage through modulating ADAM8 activity.
ADAM-8 appears to favour allergen-induced acute airway inflammation by promoting dendritic cell recruitment and CCL11 (show CCL11 ELISA Kits) and CCL22 (show CCL22 ELISA Kits) production.
ADAM8 knockout mice did not display a bone phenotype in vivo but they did not increase RANKL (show TNFSF11 ELISA Kits) production, OCL (show OCLN ELISA Kits) formation, or calvarial fibrosis in response to tumor necrosis factor alpha (TNF-alpha (show TNF ELISA Kits)) in vivo.
ADAM8 is involved in T cell maturation in the medulla but has a relatively minor impact on T cell development.
The results of this study indicated an essential role for ADAM8 in modulating TNF-alpha (show TNF ELISA Kits) signaling in CNS diseases
The study finds an increase in retinal re-vascularization but fewer neovascular tufts in the oxygen-induced retinopathy model and increased growth of heterotopically injected tumor cells in Adam8-/- mice compared with wild-type controls.
This gene encodes 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 biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene may be involved in cell adhesion during neurodegeneration, and it is thought to be a target for allergic respiratory diseases, including asthma. Alternative splicing results in multiple transcript variants.
a disintegrin and metalloproteinase domain 8
, cell surface antigen MS2
, disintegrin and metalloproteinase domain-containing protein 8
, human leukocyte differentiation antigen
, ADAM 8
, a disintegrin and metalloprotease domain (ADAM) 8
, a disintegrin and metalloprotease domain 8
, macrophage cysteine-rich glycoprotein
, gamma-tubulin complex component 2
, ADAM metallopeptidase domain 8
, a disintegrin and metallopeptidase domain 8
, disintegrin and metalloproteinase domain-containing protein 8-like