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IGSF8 encodes a member the EWI subfamily of the immunoglobulin protein superfamily. Additionally we are shipping IGSF8 Antibodies (65) and IGSF8 Proteins (13) and many more products for this protein.
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EWI-2 negatively regulates TGF-beta (show TGFB1 ELISA Kits) signaling and its downstream events including cytostasis (in vitro and in vivo), EMT (show ITK ELISA Kits)-like changes, cell migration, CD271 (show NGFR ELISA Kits)-dependent invasion, and lung metastasis (in vivo).
Authors demonstrated that EWI-2wint promotes CD81 (show CD81 ELISA Kits) clustering and confinement in CD81 (show CD81 ELISA Kits)-enriched areas.
The EWI-2/alpha-actinin complex is involved in regulation of the actin cytoskeleton at T cell immune and virological synapses, providing a link between membrane microdomains and the formation of polarized membrane structures involved in T cell recognition.
analysis of interacting regions of CD81 (show CD81 ELISA Kits) and two of its partners, EWI-2 and EWI-2wint, and their effect on hepatitis C virus infection
EWI2/PGRL associates with the metastasis suppressor KAI1/CD82 (show CD82 ELISA Kits) and inhibits the migration of prostate cancer cells.
EWI-2-dependent reorganization of alpha4beta1-CD81 (show CD81 ELISA Kits) complexes on the cell surface is responsible for EWI-2 effects on integrin-dependent morphology and motility functions
EWI proteins EWI-2 and EWI-F (show PTGFRN ELISA Kits), alpha3beta1 and alpha6beta4 integrins, and protein palmitoylation have contrasting effects on cell surface CD9 (show CD9 ELISA Kits) organization
EWI-2 and EWI-F (show PTGFRN ELISA Kits) link the tetraspanin web to the actin cytoskeleton through their direct association with ezrin-radixin-moesin (show MSN ELISA Kits) proteins
Important functions of recently activated dendritic cells are thus critically modulated by the newly discovered HSPA8 (show HSPA8 ELISA Kits)-EWI-2 interaction.
CD81 (show CD81 ELISA Kits) partner EWI-2wint inhibits hepatitis C virus entry [EWI-2wint]
IgSF8 is present in developing olfactory sensory neuron synapses, and it interacts with Tspan CD9 (show CD9 ELISA Kits).
Igsf8-deficient eggs retain the normal level and localization of CD9 (show CD9 ELISA Kits), resulting in normal microvilli formation indicating that IGSF8 is dispensable in fertility.
This study showed that the EWI2 cytoplasmic tail actively engages with the cell membrane via phosphatidylinositol phosphate binding and palmitoylation.
Igsf8 is first expressed at E9.5 in a ventral domain of the neural tube, with dorsal expression apparent at E10.5.. From E11.5, Igsf8 occurs at the edge of the ventricular zone, in postmitotic neuroblasts, and in sensory ganglia.
Report that the expression level of EWI-2 on the Cd9 (show CD9 ELISA Kits)(-/-) oocyte surface is <10% of the wild-type level. Hence, the severe reduction in EWI-2 activity may be responsible for the loss of fusion ability.
Immunoglobulin superfamily member (show CDON ELISA Kits) IgSF8 (EWI-2) and CD9 (show CD9 ELISA Kits) in fertilisation: evidence of distinct functions for CD9 (show CD9 ELISA Kits) and a CD9 (show CD9 ELISA Kits)-associated protein in mammalian sperm-egg interaction.
This gene encodes a member the EWI subfamily of the immunoglobulin protein superfamily. Members of this family contain a single transmembrane domain, an EWI (Glu-Trp-Ile)-motif and a variable number of immunoglobulin domains. This protein interacts with the tetraspanins CD81 and CD9 and may regulate their role in certain cellular functions including cell migration and viral infection. The encoded protein may also function as a tumor suppressor by inhibiting the proliferation of certain cancers. Alternate splicing results in multiple transcript variants that encode the same protein.
immunoglobulin superfamily member 8
, immunoglobulin superfamily, member 8
, immunoglobulin superfamily member 8-like
, CD81 partner 3
, glu-Trp-Ile EWI motif-containing protein 2
, keratinocytes-associated transmembrane protein 4
, prostaglandin regulatory-like protein
, PG regulatory-like protein
, keratinocyte-associated transmembrane protein 4