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Calpains are calcium-dependent cysteine proteases involved in signal transduction in a variety of cellular processes. Additionally we are shipping Calpain 5 Antibodies (51) and Calpain 5 Kits (10) and many more products for this protein.
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The relative domain rotation of 60-100 degrees we found for mini-calpain-5 (a non-classical calpain) is significantly greater than the largest rotation previously observed for a classical calpain
CAPN5 localization at the photoreceptor synapse and with mitochondria explains the neural circuitry phenotype in human CAPN5 disease alleles.
A novel CAPN5 (c.750G>T, p.Lys250Asn) missense mutation causes uveitis and neovascular retinal detachment.
CAPN5 mutation in hereditary uveitis: the R243L mutation increases calpain catalytic activity and triggers intraocular inflammation
CAPN5 expression can be suppressed by shRNA-based RNA interference
autosomal dominant neovascular inflammatory vitreoretinopathy is due to CAPN5 gain-of-function rather than haploinsufficiency.
Calpain-5 mutations cause autoimmune uveitis, retinal neovascularization, and photoreceptor degeneration.
Results describe the cloning and characterization of rat calpain-5, which is highly homologous to human and mouse sequences.
CAPN5 polymorphisms are associated with a risk of polycystic ovary syndrome.
CAPN5 seems to influence traits related to increased risk for cardiovascular diseases and play a role as a candidate gene for metabolic syndrome
mRNA in situ hybridization experiments were performed to identify the expression of CAPN5 in the mouse eye and brain
CAPN5 is found in punctate domains associated with promyelocytic leukemia (PML (show PML Proteins)) protein within the nucleus.
Despite the numerous expression sites of Capn5, the majority of Capn5-null mice were viable and fertile and appeared healthy
calpain-derived Htt (show HTT Proteins) fragmentation has a role in Huntington's disease and aberrant activation of calpains may play a role in HD pathogenesis
Calpains are calcium-dependent cysteine proteases involved in signal transduction in a variety of cellular processes. A functional calpain protein consists of an invariant small subunit and 1 of a family of large subunits. CAPN5 is one of the large subunits. Unlike some of the calpains, CAPN5 and CAPN6 lack a calmodulin-like domain IV. Because of the significant similarity to Caenorhabditis elegans sex determination gene tra-3, CAPN5 is also called as HTRA3.
, new calpain 3
, high-temperature requirement factor A3
, calpain 5
, LOW QUALITY PROTEIN: calpain-5