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identified mitochondrial proteins 4-nitrophenylphosphatase domain and non-neuronal synaptosomal associated protein 25-like protein homolog (NIP-SNAP)-1 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-SNAP-1 or -2
NIP-SNAP-1 and -2 localized in the mitochondrial inner membrane space, whereas HSP60 localized in the matrix. Expression levels of NIP-SNAP-1 and -2 in cells were decreased by knockdown of HSP60, but not HSP10. The findings indicate that HSP60 promotes folding and maintains the stability of NIP-SNAP-1 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