ADAM23
- Known as:
- ADAM23
- Catalog number:
- Y214167
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ADAM23
Related genes to: ADAM23
- Gene:
- ADAM23 NIH gene
- Name:
- ADAM metallopeptidase domain 23
- Previous symbol:
- -
- Synonyms:
- MDC3
- Chromosome:
- 2q33.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-01
- Date modifiied:
- 2016-10-05
- Gene:
- ADAM28 NIH gene
- Name:
- ADAM metallopeptidase domain 28
- Previous symbol:
- -
- Synonyms:
- eMDCII, MDC-Lm, MDC-Ls, ADAM23
- Chromosome:
- 8p21.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-07-29
- Date modifiied:
- 2019-03-22
Related products to: ADAM23
Related articles to: ADAM23
- The development of breast cancer resistance to endocrine therapies may result from an increase in cellular plasticity, permitting the emergence of a hormone-independent tumor. ADAM proteins are multidomain transmembrane proteins that have a diverse array of functions in both natural physiology and disease. A number of ADAM proteins have been implicated in the occurrence of breast cancer, including ADAM 9, ADAM12, ADAM15, ADAM17, ADAM22, and ADAM28. ADAM22 expression is driven by the coactivator protein SRC-1 in response to tamoxifen treatment in the resistant setting. ADAM22 is an ER-independent predictor of disease-free survival. LGI1 is a neuropeptide that binds ADAM22 in the nervous system. In addition to being a ligand for ADAM11, ADAM22, and ADAM23, LGI1 may play a role as a tumor suppressor. Furthermore, LGI1 may act to reduce cell migration and may impair proliferation. Therapies based on LGI1 may provide a building block for future therapies in ADAM22-positive breast cancer. - Source: PubMed
Bolger Jarlath CYoung Leonie S - The ADAM (a disintegrin and metalloproteinases) and the related ADAMTSÂ (a disintegrin and metalloproteinases with thrombospondin) motifs metalloproteinases are membrane-anchored and secreted proteins exhibiting key roles in mediating cell adhesion, proteolytic shedding, and cell signaling. Dysregulation of these proteins has been observed in some pathologic states, including cancers. Their contribution to multiple myeloma, a plasma-cell neoplasia strongly dependent on bone marrow environment, has been poorly characterized. - Source: PubMed
Publication date: 2011/03/03
Bret CarolineHose DirkReme ThierryKassambara AlboukadelSeckinger AnjaMeissner TobiasSchved Jean-FrançoisKanouni TarikGoldschmidt HartmutKlein Bernard