381413 Results for: "single-use assemblies"

Supplier: CHI Scientific

The PrimaCell™ system has been developed for the acquisition and growth of primary cells from a variety of different tissue types. Each PrimaCell™ kit has been optimized for each cell type to produce 4-7 times the number of primary cells obtained from published literature protocols. Each kit comes with 100 ml of tissue washing medium, our optimized tissue dissociation system OptiTDS™, 500 ml of growth medium, and enough growth supplements and serum to add to the supplied medium. Kits that require a Fibroblast control system also come with our FibrOut™ kit (added to the growth medium) which reduces or eliminates Fibroblast growth after 2-3 cell growth cycles.

Supplier: CHI Scientific

The PrimaCell™ system has been developed for the acquisition and growth of primary cells from a variety of different tissue types. Each PrimaCell™ kit has been optimized for each cell type to produce 4-7 times the number of primary cells obtained from published literature protocols. Each kit comes with 100 ml of tissue washing medium, our optimized tissue dissociation system OptiTDS™, 500 ml of growth medium, and enough growth supplements and serum to add to the supplied medium. Kits that require a Fibroblast control system also come with our FibrOut™ kit (added to the growth medium) which reduces or eliminates Fibroblast growth after 2-3 cell growth cycles.

Supplier: CHI Scientific

The PrimaCell™ system has been developed for the acquisition and growth of primary cells from a variety of different tissue types. Each PrimaCell™ kit has been optimized for each cell type to produce 4-7 times the number of primary cells obtained from published literature protocols. Each kit comes with 100 ml of tissue washing medium, our optimized tissue dissociation system OptiTDS™, 500 ml of growth medium, and enough growth supplements and serum to add to the supplied medium. Kits that require a Fibroblast control system also come with our FibrOut™ kit (added to the growth medium) which reduces or eliminates Fibroblast growth after 2-3 cell growth cycles.

Supplier: Prosci

Beta-catenin associates with the cytoplasmic portion of E-cadherin, which is necessary for the function of E-cadherin as an adhesion molecule. In normal tissues, beta-catenin is localized to the membrane of epithelial cells, consistent with its role in the cell adhesion complex. In breast ductal neoplasia, it is usually localized in cellular membranes. However, in lobular neoplasia, a marked redistribution throughout the cytoplasm results in a diffuse cytoplasmic pattern. Staining with beta-catenin antibody and E-cadherin antibody helps in the accurate identification of ductal and lobular neoplasms, including a distinction between low-grade ductal carcinoma in situ (DCIS) and lobular carcinoma. Additionally, some rectal and gastric adenocarcinomas demonstrate diffuse cytoplasmic staining and a lack of membranous staining, mimicking the staining pattern observed with lobular breast carcinomas.

Supplier: Ambeed

1,10-Phenanthroline monohydrochloride monohydrate, Purity: 99%, CAS Number: 18851-33-7, Appearance: White to off-white solid, Storage: Inert atmosphere, Room Temperature, Size: 25g

Supplier: Genetex

Prostaglandins are produced by the metabolism of arachidonic acid. Prostaglandin E2 is one of the five physiologically significant prostanoids known. Its wide spectrum of physiologic and pharmacologic effects in various tissues is mediated through binding to the Prostaglandin E2 receptors (EP1, EP2, EP3 & EP4). These include effects on the immune, endocrine, cardiovascular, renal and reproductive systems as well as smooth muscle. It is also one of the most abundant of the prostanoid family in the brain where it plays an important role in many neural functions, particularly in newborn babies, and as a mediator of inflammation. Prostaglandin E2 signals through a family of G-protein coupled receptors known as EP receptors. There are 4 subtypes of EP receptors, known as EP1, EP2, EP3 and EP4. EP2 receptors are 358 amino acid proteins with a short third intracellular loop. EP2 receptors stimulate adenylyl cyclase by their coupling to Gs and do not undergo Prostaglandin E2 induced internalization. The EP2 receptors is involved with the contration and relaxation of smooth muscle tissue. These receptors are mainly localized in lung and placental tissues and in smooth muscle.

Supplier: BioVendor

A DNA sequence encoding the mature variant of ovVEGF-E isolate D1701 (Dehio et al., 1999; GenBank accession No. AF106020) was expressed in E. coli as a 132 amino acid residue fusion protein with an N-terminal His-tag sequence and a thrombin cleavage site. Recombinant VEGF-E homodimer was dimerized in vitro and has a predicted mass of approximately 35 kDa. Based on sequence similarity to VEGF-A, a gene encoding a VEGF homologue has recently been discovered in the genome of Orf virus (OV) (Lyttle et al., 1994). Different isolates of Orf virus show significant amino acid sequence similarity to VEGF-A and described as a viral virulence factor that appears to be derived from captured host genes. All eight cysteine residues of the central cysteine knot motif characteristic of members of the VEGF family are conserved among other residues in the VEGF-E proteins (Dehio et al., 1999; Wise et al., 1999). Alignment of all mammalian VEGF sequences indicated that VEGF-E is distinct from the previously described VEGFs but most closely related to VEGF-A. Like VEGF-A, VEGF-E was found to bind with high affinity to VEGF receptor-2 (KDR) resulting in receptor autophosphorylation, whilst in contrast to VEGF-A, VEGF-E can not bind to VEGF receptor-1 (Flt-1). Furthermore VEGF-E can also not bind to VEGF receptor-3 (FLT-4). Therefore VEGF-E is a potent angiogenic factor selectively binding to VEGF receptor –2/KDR.

Supplier: SenseAnywhere

The SenseAnywhere 0 - 10 V input module digitizes analogue products with a 0 - 10 V output, ensuring high-precision measurements for variables like CO₂ and dust particles. Integrated electronics with a SAB interface allow individual module calibration. Its hot-swappable feature ensures continuous, accurate monitoring without data loss.

Supplier: SenseAnywhere

The SenseAnywhere 4 - 20 mA input module transforms analogue devices with a 4 - 20 mA output into digital, accurately measuring parameters like CO₂ and dust in cleanrooms. With a SAB interface and integrated electronics, it needs self-calibration only. Its hot-swappable design guarantees continuous, loss-free data collection.

Supplier: Prosci

Gli-2 (also known as Zinc Finger Protein Gli-2, GLI-Kruppel family member GLI-2 or Tax helper protein) belongs to the C2H2-type zinc finger protein subclass of the Gli family. Members of this subclass are characterized as transcription factors that bind DNA through zinc finger motifs. These motifs contain conserved H-C links. Gli family zinc finger proteins are mediators of Sonic hedgehog (Shh) signaling, and they are implicated as potent oncogenes in the embryonal carcinoma cell. The protein encoded by this gene localizes to the cytoplasm and activates patched Drosophila homolog (PTCH) gene expression. Gli-2 is also thought to play a role during embryogenesis. The encoded protein is associated with several phenotypes: Greig cephalopolysyndactyly syndrome, Pallister-Hall syndrome, pre-axial polydactyly type IV, post-axial polydactyly types A1 and B. Expression has been reported for this mRNA in human testis, myometrium, kidney, lung, glioblastomas, and embryonal cell carcinomas. Multiple splice variants have been reported for this protein.

Supplier: Prosci

The NMDA receptor (NMDAR) plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death (Grosshans et al., 2002; Wenthold et al., 2003; Carroll and Zukin, 2002). The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits (Ishii et al., 1993). It has been shown that phosphorylation of Ser1480 disrupts the interaction of NR2B with the PDZ domains of PSD-95 and SAP102 and decreases surface NR2B expression in neurons (Chung et al., 2004).

Supplier: Rockland Immunochemical

Src homology-2 domain containing protein (SHP2) is a member of the protein tyrosine phosphatase (PTP) family, a protein family that contains signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. SHP2 contains two tandem Src homology-2 (SH2) domains, which function as phosphotyrosine binding domains either directly or through scaffolding intermediates such as the insulin-receptor substrate 1 (IRS-1). These SH2 domains mediate the interaction of SHP2 with its substrates, allowing SHP2 to dephosphorylate proteins that inhibit signaling kinases such as ERK1 and AKT. SHP2 is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Recent experiments have shown SHP2 plays a significant role in hepatoprotection and liver regeneration.

Supplier: Cayman Chemical Company

Stimulator of interferon genes (STING) is a component of the innate immune response that binds to cyclic dinucleotides, which are bacterial second messengers, leading to activation of NF-κB and transcription of immunomodulatory genes, including type I interferon (IFN). The R232 variant is the most common variant in the human population, found at a frequency of 57.9% in the 1000 Genome Project.{38697} The SNP variant H232 (Item No. 22815) is found at a 13.7% frequency. Various mutations in STING either reduce or increase its activity. Gain-of-function mutations in STING, including R284M (Item No. 23594) and V155M, lead to constitutive activation and enhancement of the type I IFN response. The V155M mutation is associated with a systemic inflammatory condition, including pulmonary fibrosis and autoimmune factors. Mutations that reduce STING activity include K224R (Item No. 23593), which reduces ubiquitination of STING thereby disrupting its localization within the cell, and the double mutation G230A, R293Q (Item No. 23592), which reduces the IFN response. A T596A mutation present in the mouse strain Goldenticket leads to a complete loss of STING protein and lack of a type I IFN response to infection by Listeria.

Supplier: Rockland Immunochemical

Histone modifications mediate changes in gene expression by altering chromatin structure or by serving as a platform to recruit other proteins. LSD1 is a recently discovered amine oxidase that catalyzes the lysine-specific demethylation of histone proteins via an FAD-dependent oxidative reaction. Methylation on histone H3-K9 is thought to play an important role in heterochromatin formation, while methylation on arginine and some lysine residues (such as H3-K4) is associated with active transcription. LSD1 associates with various proteins, including HDAC1/2, CoREST, and BHC80, that act to regulate LSD1 activity in vivo, and in a histone H3-K4-specific methylase complex that is involved in transcriptional regulation. Experiments have shown that CoREST, a SANT domain-containing corepressor acts to enhance LSD1 activity, while BHC80, a PHD domain-containing protein, inhibits CoREST/LSD1 activity in vitro. LSD1-mediated histone demethylation thus may have significant effects on gene expression.

Supplier: Prosci

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events. Receptor for LGALS9; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (By similarity). [UniProt]

Supplier: Rockland Immunochemical

The serine/threonine kinase Stk39 belongs to the STE20 family, a group of kinases that are known to interact with inflammation-related kinases (such as p38, JNK, NKCC1, PKC-theta, WNK and MLCK), and with transcription factor AP-1. The STE 20 family is involved in diverse biological phenomena, including cell differentiation, cell transformation/ proliferation, cytoskeleton rearrangement, and the regulation of ion transporters. STK39 contains an N-terminal series of proline and alanine repeats (PAPA box), followed by a serine/threonine kinase catalytic domain and is abundantly expressed in the brain. STK39 is activated in response to hypotonic stress, leading to phosphorylation of several cation-chloride-coupled co-transporters. The catalytically active kinase specifically activates the p38 MAP kinase pathway, and its interaction with p38 decreases upon cellular stress, suggesting that this kinase may serve as an intermediate in the response to cellular stress. Recent studies show that STK39 tend to be a novel candidate gene for autism and hypertension.

Supplier: Prosci

ANGPTL4 mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorgenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.

Supplier: Prosci

Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes that regulate transcription by selectively deacetylating or acetylating the eta-amino groups of lysines located near the amino termini of core histone proteins. Eight members of HDAC family have been identified in the past several years. These HDAC family members are divided into two classes, I and II. Class I of the HDAC family comprises four members, HDAC-1, 2, 3, and 8, each of which contains a deacetylase domain exhibiting from 45 to 93% identity in amino acid sequence. Class II of the HDAC family comprises HDAC-4, 5, 6, and 7, the molecular weights of which are all about twofold larger than those of the class I members, and the deacetylase domains are present within the C-terminal regions, except that HDAC-6 contains two copies of the domain, one within each of the N-terminal and C-terminal regions. Human HDAC-1, 2 and 3 were expressed in various tissues, but the others (HDAC-4, 5, 6, and 7) showed tissue-specific expression patterns. These results suggested that each member of the HDAC family exhibits a different, individual substrate specificity and function in vivo.

Supplier: Rockland Immunochemical

Immunity-related GTPases (IRG) (also known as p47 GTPases) are a family of GTPase proteins found in vertebrates, which play critical roles in mediating innate resistance to intracellular pathogens. IRG genes have been found in a number of mammals and lower species including mice, rats, zebrafish and humans. Most of the mouse genes contain interferon-stimulated response elements which mediate transcriptional activation by IFNs. In humans, only two IRG genes have been found: human IRGC encodes a full-length IRG protein that, like the mouse homologue, is constitutively expressed in testis, while human IRGM encodes a considerably truncated protein that is constitutively expressed in cultured cells including some macrophage cell lines. As the two human genes IRGC and IRGM are not subject to IFN control, it has been suggested that the host resistance mechanism supported by IRG proteins in the mouse is lacking in humans.

Supplier: Rockland Immunochemical

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. This structure consists of approximately 146 bp of DNA wrapped around a nucleosome, an octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. This gene is intronless and encodes a member of the histone H3 family. Transcripts from this gene lack polyA tails; instead, they contain a palindromic termination element. This gene is found in a histone cluster on chromosome 1. This gene is one of four histone genes in the cluster that are duplicated; this record represents the telomeric copy. Anti-Histone H3 are ideal for researchers interested in Chromatin Modifiers, Chromatin Research, Histones and Modified Histones, and Epigenetics Research.

Supplier: Prosci

Myogenin is a member of the MyoD family of myogenic basic helix-loop-helix (bHLH) transcription factors that also includes MyoD, Myf-5, and MRF4 (also known as herculinor Myf-6). MyoD family members are expressed exclusively in skeletal muscle and play a key role in activating myogenesis by binding to enhancer sequences of muscle-specific genes. The regulatory domain of MyoD is approximately 70 amino acids in length and includes both a basic DNA binding motif and a bHLH dimerization motif. MyoD family members share about 80% amino acid homology in their bHLH motifs. Myogenin antibody labels the nuclei of myoblasts in developing muscle tissue, and is expressed in tumor cell nuclei of rhabdomyosarcoma and some leiomyosarcomas. Positive nuclear staining may occur in Wilms’ tumor.

Supplier: Rockland Immunochemical

Signal transducer and activator of transcription 3 (Stat3) belongs to a family of cytoplasmic transcription factors that can be activated by phosphorylation by its cell surface receptor. Stat3 plays a key role in many cellular processes such as cell growth and apoptosis. It also mediates cellular responses to interleukins, KITLG/SCF,EGF, IFN-alpha and other growth factors and may mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Stat3 forms a homodimer or a heterodimer with a related family member (e.g. STAT1). Activation occurs through phosphorylation of tyrosine 705 and serine 727. Phosphorylation of Stat3 at Tyr705 induces Stat3 dimerization and nuclear translocation. Serine phosphorylation is important for stable DNA-binding of Stat3 homodimers and maximal transcriptional activity. Stat3 can have a dual role in cancer, it has been found that Stat3 protein can promote oncogenesis and have a tumor suppressor role depending upon the mutational background of the tumor.

Supplier: Prosci

There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The first three are located together on chromosome 2, while the tissue non-specific form is located on chromosome 1. The product of this gene is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is matrix mineralization; however, mice that lack a functional form of this enzyme show normal skeletal development. This enzyme has been linked directly to hypo-phosphatasia, a disorder that is characterized by hypercalcemia and includes skeletal defects. The character of this disorder can vary, however, depending on the specific mutation since this determines age of onset and severity of symptoms. Alternatively spliced transcript variants, which encode the same protein, have been identified for this gene.

Supplier: Genetex

Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis. The precursor form of all caspases is composed of a prodomain, and large and small catalytic subunits. The active forms of caspases are generated by several stimuli including ligand-receptor interactions, growth factor deprivation and inhibitors of cellular functions. All known caspases require cleavage adjacent to aspartates to liberate one large and one small subunit, which associate into a2b2 tetramer to form the active enzyme. Gene for Caspase 3 also known as Yama, CPP32, and apopain codes for a 32-kDa protein. Caspase 3 cleaves the death substrate poly(ADP-ribose) polymerase (PARP) to a specific 85 kDa form observed during apoptosis and is inhibitable by the CrmA protein. Other Caspase 3 substrates include DNA-PK, actin, GAS2, and procaspase-6, etc. Caspase 3 is activated by cleavage events at Asp-28/Ser-29 (between N-terminal pro-domain) and Asp-175/Ser-176 (between large and small subunits) to generate a large subunit of 17-kDa and a small subunit of 12-kDa.

Supplier: Rockland Immunochemical

The mammalian Target of Rapamycin (TOR, also known as mTOR) is an evolutionarily conserved serine/threonine kinase that regulates cell growth and cell cycle through its ability to integrate signals from nutrient levels and growth factors. Rapamycin inhibits TOR activity resulting in reduced cell growth and reduced rates of cell cycle and cell proliferation. Raptor (regulatory associated protein of TOR) is a TOR-binding protein essential for TOR signaling in vivo. It acts as a TOR scaffold protein whose binding by TOR substrates is necessary for effective TOR-catalyzed phosphorylation. These substrates include the ribosomal protein S6 kinase (RP S6K) and the eukaryotic initiation factor 4E binding protein 4EBP1, proteins necessary for cell growth and proliferation and responsive to nutrient and mitogen levels. Raptor binds these proteins through a common 5 amino acid TOR-signaling (TOS) motif; mutation of this motif prevents the TOR-dependent phosphorylation of these proteins.

Supplier: Prosci

p53 is a nuclear protein which plays an essential role in the regulation of cell cycle specifically in the transition from G0 to G1. It is found in very low levels in normal cells however in a variety of transformed cell lines in high amounts and believed to contribute to transformation and malignancy. The open reading frame of p53 is 393 amino acids long, with the central region (consisting of amino acids from about 100 to 300) containing the DNA-binding domain. This proteolysis-resistant core is flanked by a C-terminal end mediating oligomerization and an N-terminal end containing a strong transcription activation signal. p53 binds as a tetramer to a PBS (p53-Binding Site) and activates the expression of downstream genes that inhibit growth and/or invasion. p53 binds as a tetramer to a p53-binding site (PBS) and to activate the expression of adjacent genes that inhibit growth and/or invasion. Deletion of one or both p53 alleles reduces the expression of tetramers, resulting in decreased expression of the growth inhibitory genes

Supplier: Prosci

Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger.

Supplier: Rockland Immunochemical

PTPRF or leukocyte common antigen-related protein (LAR) is a widely expressed protein tyrosine phosphatase with an extracellular receptor region that resembles a cell adhesion molecule. PTPRF removes phosphate group from β-catenin, an event that may subsequently facilitate cell-cell adhesion and ensure the stability of the cadherin complex. This phosphatase has also been implicated in various cellular processes such as neurite growth, nerve regeneration, actin remodeling and regulation of insulin function (1,2,3,4). Anti-PTPRF (C-terminal) antibody is specific for the extracellular and cytoplasmic subunits of human PTPRF (approx. 210, 150 and 85 kDa). Detection of the PTPRF bands by immunoblotting is specifically inhibited by the immunizing peptide. Anti-PTPRF is ideal for researchers interested in Cell adhesion Cadherin-mediated cell adhesion pathways, PAK pathways, insulin resistance and ureterocele.

Supplier: Rockland Immunochemical

Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Histone proteins are highly post-translationally modified with Histone H3 being the most extensively modified of the five histones. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of post-translational modification that influence cellular processes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Histone H3 Antibody is ideal for investigators involved in Cell Signaling, Epigenetics, Nuclear Signaling research and Signal Transduction research.

Supplier: Rockland Immunochemical

The leucine-rich, glioma inactivated gene 4 (LGI4) is a member of the LGI family in which LGI1 is the exemplar. The LGI family consists of four of highly related proteins containing leucine-rich repeats (LRRs) which are highly similar to other transmembrane signaling molecules and receptors. LGI1 has been identified as a candidate tumor suppressor gene for glioma and plays a role in autodominant lateral temporal epilepsy (ADTLE), an epileptic syndrome characterized by focal seizures with predominant auditory symptoms. Despite its high homology with LGI1 and similar pattern of expression, mutations in LGI4 have not been found to be associated with ADTLE. However, the LGI4 gene is located in a region linked to benign familial infantile convulsions. Further study revealed that a GC-to-AT polymorphism was correlated with childhood absence epilepsy. Other studies showed that decreasing LGI4 expression in cultured cells inhibits myelination, indicating that LGI4 may play a role in neural development.