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INVS encodes a protein containing multiple ankyrin domains and two IQ calmodulin-binding domains. Additionally we are shipping Inversin Kits (9) and Inversin Antibodies (6) and many more products for this protein.
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Inversin relays Frizzled-8 (show FZD8 Proteins) signals to promote proximal pronephros development.
The present study indicates that calmodulin (show Calm2 Proteins) binding sites (IQ motifs) are crucial in controlling the biological activity of both mouse and Xenopus inv proteins
Truncating mutations in NPHP2 gene is associated with nephronophthisis-related ciliopathy.
ANKS6 as a new NPHP family member that assembles a distinct module of nephronophthisis-associated proteins, encompassing NEK8 (show NEK9 Proteins), INVS and NPHP3 (show NPHP3 Proteins).
INVS mutation can cause juvenile nephronophthisis with abnormal reactivity of the Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) pathway.
has conserved ankyrin repeat and IQ domains and interacts with calmodulin (show CALM1 Proteins)
analysis of a homozygous mutation in exon 13 of inversin (INVS) (C2719T, R907X) in a patient with retinitis pigmentosa and renal failure [case report]
Thus, although considered a common variant, inv(10)(p11.2q21.2) has a single ancestral founder among northern Europeans.
Cystic kidney disease has been linked to mutations in the Invs gene in mice with an inversion of embryonic turning (inv/inv) and the INVS (NPHP2) gene in human infantile nephronophthisis (NPH).
screened 43 families with infantile nephronophthisis (ESRD less than 5 years of age) for NPHP2 and NPHP3 (show NPHP3 Proteins) mutations and determined genotype-phenotype correlations
Loss of NPHP2 causes ciliogenesis defects.
the significance of Inversin in controlling cell migration processes
Nek8 (show NEK8 Proteins) acts downstream of Inv function
Inv acts as a molecular anchor for Nphp3 (show NPHP3 Proteins) and Nek8 (show NEK8 Proteins) in the proximal segment of primary cilia.
the inv gene product functions in several cellular compartments, including the nucleus and cell-cell adhesion sites
Molecular cloning of a gene for inversion of embryo turning (inv) with cystic kidney. Deduced amino acid sequence shows 15 successive repeats of Ank (show ANKH Proteins)/Swi6 motif in its N-terminal domain. Mutation causes situs inversus and cysts in kidney in inv mutant.
inv has a role in kidney disease: inv mutant mouse has renal cysts resembling infantile NPHP2
The localization of inversin in distal tubules in the kidney and in extrarenal tissues suggests that the expression of this protein has an important function in a variety of organs.
These results indicate that a random signal of laterality (Foxj1 (show FOXJ1 Proteins)) is dominant over the reversal signal of laterality (Inv).
The function of the inv protein (show vcp Proteins) is distinct from polaris (Tg737 gene product), polycystins (pkd1 (show PKD1 Proteins) and pkd2 (show PKD2 Proteins) gene products). No difference was found in intracellular Ca2 (show CA2 Proteins)+ increases between normal and inv/inv mutant cells.
This gene encodes a protein containing multiple ankyrin domains and two IQ calmodulin-binding domains. The encoded protein may function in renal tubular development and function, and in left-right axis determination. This protein interacts with nephrocystin and infers a connection between primary cilia function and left-right axis determination. A similar protein in mice interacts with calmodulin. Mutations in this gene have been associated with nephronophthisis type 2. Multiple transcript variants encoding distinct isoforms have been identified for this gene.
, inversion of embryo turning homolog
, inversion of embryonic turning
, inversion of embryo turning protein
, nephrocystin 2