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identified mitochondrial proteins 4-nitrophenylphosphatase domain and non-neuronal synaptosomal associated protein 25 (show SNAP25 Proteins)-like protein homolog (NIP (show GIPC1 Proteins)-SNAP)-1 (show NIPSNAP3B Proteins) and -2 as clarithromycin-binding proteins. Production of proinflammatory cytokines induced by lipopolysaccharides and Pam3-CSK4 in epithelial cell lines BEAS-2B and T24 were suppressed by knockdown of NIP (show GIPC1 Proteins)-SNAP-1 (show NIPSNAP3B Proteins) or -2
NIP (show GIPC1 Proteins)-SNAP-1 (show NIPSNAP3B Proteins) and -2 localized in the mitochondrial inner membrane space, whereas HSP60 (show HSPD1 Proteins) localized in the matrix. Expression levels of NIP (show GIPC1 Proteins)-SNAP-1 (show NIPSNAP3B Proteins) and -2 in cells were decreased by knockdown of HSP60 (show HSPD1 Proteins), but not HSP10 (show HSPE1 Proteins). The findings indicate that HSP60 (show HSPD1 Proteins) promotes folding and maintains the stability of NIP (show GIPC1 Proteins)-SNAP-1 (show NIPSNAP3B Proteins) and -2.
GBAS mutations could not explain phenotype of patients with combined oxidative phosphorylation system deficiencies.
CHCHD10 and GBAS are involved in oxidative phosphorylation.
This gene encodes a member of the NipSnap family of proteins that may be involved in vesicular transport. The encoded protein is localized to mitochondria and plays a role in oxidative phosphorylation. A pseudogene of this gene is located on the long arm of chromosome 2. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
glioblastoma amplified sequence
, glioblastoma-amplified sequence
, protein NipSnap homolog 2
, 4-nitrophenylphosphatase domain and non-neuronal SNAP25-like 2