dominant

Polycystin-1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 69.3 kDa and the accession number is P98161.

HCV NS3 displays three enzymatic activities: serine protease, NTPase, and RNA helicase. HCV NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A, and NS5A-NS5B. HCV NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand (By similarity). Cleaves and inhibits the host antiviral protein MAVS. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. One of the HCV proteases, NS3-4A serine protease, is a non-covalent heterodimer consisting of a catalytic subunit (the N-terminal one-third of NS3 protein) and an activating cofactor (NS4A protein) and is responsible for cleavage at four sites of the HCV polyprotein.

Vesicle-associated membrane protein-associated protein B / C, also known as VAMP-B/VAMP-C, VAMP-associated protein B/C, VAP-B/VAP-C and VAPB, is a single-pass type IV membrane protein that belongs to the VAMP-associated protein (VAP) family. VAPB contains one MSP domain. VAPB may play a role in vesicle trafficking. VAPB forms a heterodimer with VAPA. VAPB interacts with VAMP1 and VAMP2. Defects in VAPB are the cause of amyotrophic lateral sclerosis type 8 ( ALS8 ) which is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Defects in VAPB are also a cause of spinal muscular atrophy autosomal dominant Finkel type (SMAF) which is characterized by proximal muscle weakness that begins in the lower limbs and then progresses to upper limbs.

ECSIT is an adapter protein of the toll-like and IL-1 receptor signaling pathway that is involved in the activation of NF-kappa-B via MAP3K1. Activation of NF-kappaB as a consequence of signaling through the Toll and IL-1 receptors is a major element of innate immune responses. ECSIT is specific for the Toll/IL-1 pathways and is a regulator of MEKK-1 processing. It bridges TRAF6 to MEKK-1. Expression of wild-type ECSIT accelerates processing of MEKK-1, whereas a dominant-negative fragment of ECSIT blocks MEKK-1 processing and activation of NF-kappaB. ECSIT is also required for normal embryonic development and efficient assembly of mitochondrial NADH:ubiquinone oxidoreductase.

Ameloblastin (AMBN) is a member of the Ameloblastin family. AMBN is a secreted protein and is specially expressed in ameloblast, localizing to the Tomes processes of secretory ameloblasts and in the sheath space between rod-interrod enamel Mutations of this protein may be associated with dentinogenesis imperfect and autosomal dominant amylogenesis imperfect. Ameloblastin may play an important role in the formation and mineralization of the enamel matrix. Biochemically, it is classified as an intrinsically disordered protein (IDP). Its biological role remains largely unknown.

Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.; Does not bind thyroid hormone and functions as a weak dominant negative inhibitor of thyroid hormone action. THRA Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 58.9 kDa and the accession number is P10827.

MEP1B (Meprin A Subunit Beta) is a Protein Coding gene. This gene encodes the beta subunit. Targeted disruption of this gene in mice affects embryonic viability, renal gene expression profiles, and distribution of the membrane-associated alpha subunit in the kidney and intestine. Meprins are cell membrane, oligomeric metalloendopeptidases composed of two distinct but evolutionarily related subunits, alpha, and beta. MEP1A is mapped to the short arm of chromosome 6 by the use of radiation and somatic cell hybrids. More specifically, it is localized between the centromere and GSTA2 in 6p11-p12. MEP1B mapped to chromosome 18, by the use of somatic cell hybrids, in 18q12.2-q12.3, proximal to the TTR/PALB gene. Diseases associated with MEP1B include Powassan Encephalitis and Deafness, Autosomal Dominant 31.

Familial exudative vitreoretinopathy (FEVR) is a hereditary blinding disorder that features defects in retinal vascular development. Mutations in FZD4 are known to cause autosomal dominant exudative vitreoretinopathy (EVR1). The mutations in FZD4 are associated with the phenotypes of retinal folds or ectopic macula in FEVR. Frizzled 4 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 17.7 kDa and the accession number is A6I5Z8.

Atlastin-1, also known as Spastic paraplegia 3 protein A, Guanine nucleotide-binding protein 3, GTP-binding protein 3, GBP3, ATL1 and SPG3A, is a multi-pass membrane protein which belongs to theGBP family and atlastin subfamily. ATL1 / SPG3A is expressed predominantly in the adult and fetal central nervous system. Expression of ATL1 / SPG3A in adult brain is at least 5-fold higher than in other tissues. ATL1 / SPG3A is detected predominantly in pyramidal neurons in the cerebral cortex and the hippocampus of the brain. ATL1 / SPG3A is also expressed in upper and lower motor neurons (at protein level). A distinguishing feature of ATL1 / SPG3A is its frequent early onset, raising the possibility that developmental abnormalities may be involved in its pathogenesis. Missense SPG3A mutant atlastin-1 proteins have impaired GTPase activity and may act in a dominant-negative, loss-of-function manner by forming mixed oligomers with wild-type atlastin-1. Defects in ATL1 / SPG3A are the cause of spastic paraplegia autosomal dominant type 3 (SPG3), also known as Strumpell-Lorrain syndrome. Spastic paraplegia is a degenerative spinal cord disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs.

Thyroid hormone receptor beta (THRB), also known as TRbeta and NR1A2, belongs to the nuclear hormone receptor family. Featuring an N-terminal transactivation domain, a central DNA-binding domain, and a hormone/ligand-binding domain, THRB isoform 1/2 expression localizes predominately to the liver and pituitary, respectively. THRB regulates the feedback of T3-dependent thyrotropin-stimulating hormone (TSH) transcription in the pituitary by binding to thyroid hormone (TH) response elements present on promoters of TH-responsive genes. Located on chromosome 3p24, THRB gene mutation has been linked to autosomal dominant resistance to TH (RTH), which is characterized by goiter and elevated levels of T3, T4, and TSH. THRB is a known pharmacological target for the treatment of non-alcoholic steatohepatitis (NASH). THRB may be a target for future cancer therapies since its knockdown enhanced the viability of endometrial cancer cells and activated the mTOR-4EBP1/eIF4G pathway.

MRTO4 (MRT4 Homolog, Ribosome Maturation Factor) is a Protein Coding gene. MRTO4, also known as MRT4, belongs to the universal ribosomal protein uL10 family. This gene encodes a protein sharing a low level of sequence similarity with ribosomal protein P0. MRTO4 is a nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes. The precise function of MRTO4 is currently unknown. It appears to be involved in mRNA turnover and ribosome assembly. MRTO4 is widely expressed in the appendix, lymph node, and other tissues. Diseases associated with MRTO4 include Bacterial Conjunctivitis and Robinow Syndrome, Autosomal Dominant 1.

Familial exudative vitreoretinopathy (FEVR) is a hereditary blinding disorder that features defects in retinal vascular development. Mutations in FZD4 are known to cause autosomal dominant exudative vitreoretinopathy (EVR1). The mutations in FZD4 are associated with the phenotypes of retinal folds or ectopic macula in FEVR. Frizzled 4 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 17.7 kDa and the accession number is Q9ULV1.

Cluster of Differentiation 80, also called B7-1, is a member of cell surface immunoglobulin superfamily which plays key, yet distinct roles in the activation of T cells. B7-1/CD80 and B7-2/CD86, together with their receptors CD28 and CTLA4, constitute one of the dominant co-stimulatory pathways that regulate T- and B- cell responses. CD80 is mostly expressed on the surface of antigen-presenting cells including activated B cells, macrophages and dendritic cells. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response.

Ectodysplasin A receptor (EDAR) is a type I transmembrane protein of the TNF-α receptor superfamily which plays a key role in ectodermal differentiation. EDAR was encoded by the mouse downless gene and defective in human dominant and recessive forms of autosomal hypohidrotic ectodermal dysplasia (EDA) syndrome. The extracellular domain of EDAR contains 14 cysteine residues, six of which approximate the TNFRSF cysteine-rich region, the cytoplasmic domain contains a region with homology to the death domains found in other TNFRSF members. EDAR has been suggested to be an early and important promoter of placode development in all ectodermal organs, such as uch as hair follicles, teeth and sweat glands. EDA-A1, the A1 isoform of EDA, is the EDAR ligand. EDA and EDA are implicated in appendage development by the cloning of a gene underlying hypohidrotic ectodermal dysplasia (HED) in mouse and human. HED is characterized by agenesis or malformation of ectoderm-derived appendages, such as teeth, sweat glands and hair follicles, while the skin itself develops normally.

Heat shock factor protein 1, also known as heat shock transcription factor 1, HSF1, and HSTF1, is a cytoplasm and nucleus protein that belongs to the HSF family. HSF1 is the major transcription factor of HSPs (heat shock proteins) in response to various stresses. Wild type HSF1 (heat shock transcriptional factor 1) is normally inactive. HSF1 / HSTF1 is a DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. HSF1 / HSTF1 protects cells and organisms against various types of stress, either by triggering a complex response that promotes cell survival or by triggering cell death when stress-induced alterations cannot be rescued. HSF1 / HSTF1 is the key protein in regulating the stress response. It can be activated under heat, oxidative, or other stress conditions. Dominant-positive and dominant-negative HSF1 are two types of HSF1 mutants. Both of them gain DNA binding activity in the absence of stress. Also, dominant-positive HSF1 acquires transcriptional activity, which dominant-negative HSF1 does not acquire. HSF1 / HSTF1 was also reported to contribute to cell resistance against genotoxic stress, such as that caused by doxorubicin, an anticancer drug in common clinical use.

UBASH3A is a member of the T-cell ubiquitin ligand (TULA) family. This family consists of two members. Both of them can negatively regulate T-cell signaling. UBASH3A can facilitate growth factor withdrawal-induced apoptosis in T cells, which may occur via its interaction with AIF, an apoptosis-inducing factor. Alternative splicing of UBASH3A gene results in multiple transcript variants. It interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. UBASH3A promotes accumulation of activated target receptors, such as T-cell receptors, EGFR and PDGFRB, on the cell surface. UBASH3A also exhibits negligigle protein tyrosine phosphatase activity at neutral pH. It may act as a dominant-negative regulator of UBASH3B-dependent dephosphorylation. It may also inhibit dynamin-dependent endocytic pathways by functionally sequestering dynamin via its SH3 domain.

Tyrosine-protein kinase Blk, also known as B lymphocyte kinase, p55-Blk and BLK, is a member of theprotein kinase superfamily, Tyr protein kinase family and SRC subfamily. BLK / p55-Blk is expressed in lymphatic organs, pancreatic islets, Leydig cells, striate ducts of salivary glands and hair follicles. BLK / p55-Blk is a src-family protein tyrosine kinase specifically expressed in B-lineage cells of mice. The early onset of Blk expression during B-cell development in the bone marrow and the high expression levels of Blk in mature B cells suggest a possible important role of Blk in B-cell physiology. It is a modulator of beta-cells function, acting through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose. Defects in BLK are a cause of maturity-onset diabetes of the young type 11 which is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.

Interleukin‑5 Receptor alpha (IL‑5 R alpha), also known as CD125, is a 60 kDa hematopoietin receptor that plays a dominant role in eosinophil biology.This is the receptor for interleukin-5. The alpha chain binds to IL5. IL-5R alpha/CD125 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 38.7 kDa and the accession number is Q01344-1.

Endoglin is a single-pass type I membrane protein which restricted to endothelial cells in all tissues except bone marrow. Endoglin as major glycoprotein of vascular endothelium, it has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Homodimer forms a heteromeric complex with the signaling receptors for transforming growth factor-beta: TGFBR1 and/or TGFBR2. It may have an important role in the binding of endothelial cells to integrins and/or other RGD receptors. Defects in ENG are the cause of hereditary hemorrhagic telangiectasia type 1 (HHT1), which is an autosomal dominant multisystemic vascular dysplasia, characterized by recurrent epistaxis, muco-cutaneous telangiectases, gastro-intestinal hemorrhage, and pulmonary (PAVM), cerebral (CAVM) and hepatic arteriovenous malformations.

Crystallins are the dominant structural components of the vertebrate eye lens.

Cathepsin V (CTSV), also known as Cathepsin L2, CTSL2, and CATL2, is a member of the peptidase C1 family. It is predominantly expressed in the thymus and testis. Cathepsin V is also expressed in corneal epithelium, and to a lesser extent in conjuctival epithelium and skin. It is a lysosomal cysteine proteinase that may play an important role in corneal physiology. It has about 75% protein sequence identity to murine cathepsin L. The fold of this enzyme is similar to the fold adopted by other members of the papain superfamily of cysteine proteases. Cathepsin V has been recently described as highly homologous to Cathepsin L and exclusively expressed in human thymus and testis. Cathepsin V is the dominant cysteine protease in cortical human thymic epithelial cells, while Cathepsin L and Cathepsin S seem to be restricted to dendritic and macrophage-like cells. Active Cathepsin V in thymic lysosomal preparations was demonstrated by active-site labeling. Recombinant Cathepsin V was capable of converting Ii into CLIP efficiently, suggesting that it is the protease that controls the generation of alphabeta-CLIP complexes in the human thymus. Cathepsin V is the third elastolytic cysteine protease which exhibits the most potent elastase activity yet described among human proteases and that it is present in atherosclerotic plaque specimens. Cathepsin L2 may play a specialized role in the thymus and testis. Expression analysis of cathepsin L2 in human tumors revealed a widespread expression in colorectal and breast carcinomas but not in normal colon or mammary gland or in peritumoral tissues. Cathepsin L2 was also expressed by colorectal and breast cancer cell lines as well as by some tumors of diverse origin, including ovarian and renal carcinomas.

Osteosarcoma (OS) is the most common type of bone tumor in children and adults. The expression of APCDD1, a Wnt antagonist, was reduced in OS tissues and cells compared to adjacent normal tissue and osteoblast cells, respectively. Mechanistically, this was due to increased levels of methylation in the promoter region of the APCDD1 gene. Consistently, the DNA methyltransferase inhibitor 5-AZA-dC, reduced DNA methylation in the APCDD1 promoter, and restored APCDD1 expression in OS tissue and cells. Moreover, DNMT3a, but not DNMT1 or DNMT3b, was the major DNA methyltransferase that facilitated hyper-methylation of DNA in the APCDD1 promoter, thus reducing APCDD1 mRNA levels in OS tissues. Importantly, ectopic expression of APCDD1 suppressed activity of the Wnt/beta-Catenin signaling pathway in OS cells and inhibited their invasion and reversed their EMT-like properties, while depletion of APCDD1 promoted invasion and metastasis of osteosarcoma cells in vitro and in vivo. That APCDD1 modulates the gene expression of Wnt- and EK-related signaling molecules at the cap stage of tooth development, and is involved in tooth cusp patterning by modulating the epithelial rearrangement in the IEE. In hair follicle cells APCDD1 inhibits the canonical WNT/beta-Catenin pathway and its inactivation is associated with an autosomal dominant form of hair loss. APCDD1 sustains the expression and activation of beta-Catenin.

Familial exudative vitreoretinopathy (FEVR) is a hereditary blinding disorder that features defects in retinal vascular development. Mutations in FZD4 are known to cause autosomal dominant exudative vitreoretinopathy (EVR1). The mutations in FZD4 are associated with the phenotypes of retinal folds or ectopic macula in FEVR. Frizzled 4 Protein, Rat, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 43.2 kDa and the accession number is Q9QZH0.

MST4, also known as mammalian STE2-like protein kinase 4, is a novel member of the germinal center kinase subfamily of human Ste2-like kinases and is closely related to MST3. The 416 amino acid full-length MST4 contains a C-terminal regulatory domain and an N-terminal kinase domain, both of which are required for full activation of the kinase. MST4 is highly expressed in the placenta, thymus, and peripheral blood leukocytes. MST4 specifically activates ERK but not JNK or p38 MAPK in transiently transfected cells or stable cell lines, and thus is biologically active in the activation of the MEK/ERK pathway mediating cell growth and transformation. Further, MST4 kinase activity is stimulated significantly by epidermal growth factor receptor (EGFR) ligands, which are known to promote the growth of certain cancer cells. Accordingly, MST4 has a potential role in signal transduction pathways involved in cancer progression. Three alternatively spliced isoforms of MST4 have been isolated, and isoform 3 lacks an exon encoding kinase domain and may function as a dominant-negative regulator of the MST4 kinase.

The two recurrent dominant mutations in RAB11B leading to a neurodevelopmental syndrome, likely caused by altered GDP/GTP binding that inactivate the protein and induce GEF binding and protein mislocalization.

CEL-maturity onset diabetes of the young (MODY), diabetes with pancreatic lipomatosis and exocrine dysfunction, is due to dominant frameshift mutations in the acinar cell carboxyl ester lipase gene (CEL). Bile-salt activated carboxylic ester lipase (CEL) is a major triglyceride, cholesterol ester and vitamin ester hydrolytic enzyme contained within pancreatic and lactating mammary gland secretions. Carboxyl ester lipase is a digestive pancreatic enzyme encoded by the CEL gene. Mutations in CEL cause maturity-onset diabetes of the young as well as pancreatic exocrine dysfunction. The enzyme carboxyl ester lipase (CEL), also known as bile salt-dependent or -stimulated lipase (BSDL, BSSL), hydrolyzes dietary fat, cholesteryl esters and fat-soluble vitamins in the duodenum. CEL is mainly expressed in pancreatic acinar cells and lactating mammary glands. The human CEL gene resides on chromosome 9q34.3 and contains a variable number of tandem repeats (VNTR) region that encodes a mucin-like protein tail.

Fibroblast growth factor 10 (FGF10) is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7. FGF10 plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. FGF10 is required for normal branching morphogenesis. It may play a role in wound healing. Defects in FGF10 are the cause of autosomal dominant aplasia of lacrimal and salivary glands (ALSG). ALSG has variable expressivity, and affected individuals may have aplasia or hypoplasia of the lacrimal, parotid, submandibular and sublingual glands and absence of the lacrimal puncta. The disorder is characterized by irritable eyes, recurrent eye infections, epiphora (constant tearing) and xerostomia (dryness of the mouth), which increases the risk of dental erosion, dental caries, periodontal disease and oral infections.

Cynomologous Cluster of Differentiation 80, also called B7-1, is a member of cell surface immunoglobulin superfamily.It is expressed on the surface of antigen-presenting cells including activated B cells, macrophages and dendritic cells.CD80 plays key, yet distinct roles in the activation of T cells. B7-1/CD80 and B7-2/CD86, together with their receptors CD28 and CTLA4, constitute one of the dominant co-stimulatory pathways that regulate T- and B- cell responses. CD80 is mostly expressed on the surface of antigen-presenting cells including activated B cells, macrophages and dendritic cells. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. CD80 is thus regarded as promising therapeutic targets for autoimmune diseases and various carcinomas.

Tropomyosin Alpha-3 Chain (TPM3) is a member of the Tropomyosin family. TPM3 exists as a heterodimer consisting of an alpha and a beta chain. TPM3 plays a central role in association with the Troponin complex and in the calcium dependent regulation of vertebrate striated muscle contraction. Defects in TPM3 are the cause of thyroid papillary carcinoma. Mutations in the TPM3 gene cause autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are linked with cancer.

Defects in SOS1 are the cause of gingival fibromatosis 1 (GGF1) [MIM:135300]; also known as GINGF1. Gingival fibromatosis is a rare overgrowth condition. Defects in SOS1 are the cause of Noonan syndrome type 4 (NS4) [MIM:610733]. NS4 is an autosomal dominant disorder characterized by dysmorphic facial features, short stature, hypertelorism, cardiac anomalies, deafness, motor delay, and a bleeding diathesis. It is a genetically heterogeneous and relatively common syndrome, with an estimated incidence of 1 in 1000-2500 live births. Rarely, NS4 is associated with juvenile myelomonocytic leukemia (JMML). SOS1 mutations engender a high prevalence of pulmonary valve disease; atrial septal defects are less common. characterized by a benign, slowly progressive, nonhemorrhagic, fibrous enlargement of maxillary and mandibular keratinized gingiva. GGF1 is usually transmitted as an autosomal dominant trait, although sporadic cases are common.

Interleukin‑5 Receptor alpha (IL‑5 R alpha), also known as CD125, is a 60 kDa hematopoietin receptor that plays a dominant role in eosinophil biology.This is the receptor for interleukin-5. The alpha chain binds to IL5. IL-5R alpha/CD125 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 38.7 kDa and the accession number is Q01344-1.

The SARS-CoV-2 spike (S) protein is the target of vaccine design efforts to end the COVID-19 pandemic. Despite a low mutation rate, isolates with the D614G substitution in the S protein appeared early during the pandemic, and are now the dominant form worldwide. Here, we analyze the D614G mutation in the context of a soluble S ectodomain construct.

A DNA-binding protein implicated in transcriptional repression (silencing). Also involved in bacterial chromosome organization and compaction. H-NS binds tightly to AT-rich dsDNA and inhibits transcription. Binds upstream and downstream of initiating RNA polymerase, trapping it in a loop and preventing transcription. Binds to hundreds of sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome. Many of these loci were horizontally transferred (HTG); this offers the selective advantage of silencing foreign DNA while keeping it in the genome in case of need. Suppresses transcription at many intragenic sites as well as transcription of spurious, non-coding RNAs genome-wide. Repression of HTG by H-NS is thought to allow their DNA to evolve faster than non-H-NS-bound regions, and facilitates integration of HTG into transcriptional regulatory networks. A subset of H-NS/StpA-regulated genes also require Hha (and/or Cnu, ydgT) for repression; Hha and Cnu increase the number of genes DNA bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex. The protein forms 2 clusters in the nucleoid which gather hns-bound loci together, bridging non-contiguous DNA, and causes DNA substantial condensation. Binds DNA better at low temperatures than at 37 degrees Celsius; AT-rich sites nucleate H-NS binding, further DNA-binding is cooperative and this cooperativity decreases with rising temperature. Transcriptional repression can be inhibited by dominant-negative mutants of StpA or itself. May effect transcriptional elongation. Can increase translational efficiency of mRNA with suboptimal Shine-Dalgarno sequences. Plays a role in the thermal control of pili and adhesive curli fimbriae production, by inducing transcription of csgD. Plays a role in flagellar function. Represses the CRISPR-cas promoters, permits only weak transcription of the crRNA precursor; its repression is antagonized by LeuO. Binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150. Overexpression suppresses secY24, a temperature-sensitive mutation. Has also been reported to activate transcription of some genes.

Familial exudative vitreoretinopathy (FEVR) is a hereditary blinding disorder that features defects in retinal vascular development. Mutations in FZD4 are known to cause autosomal dominant exudative vitreoretinopathy (EVR1). The mutations in FZD4 are associated with the phenotypes of retinal folds or ectopic macula in FEVR. Frizzled 4 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 43.3 kDa and the accession number is Q9ULV1.

Cochlin, also known as COCH-5B2 and COCH, is a secreted protein that contains one LCCL domain and two VWFA domains. It is an abundant inner ear protein expressed as multiple isoforms. Its function is also unknown, but it is suspected to be an extracellular matrix component. Cochlin and type II collagen are major constituents of the inner ear extracellular matrix, and Cochlin constitutes 70% of non-collagenous protein in the inner ear, the cochlin isoforms can be classified into three subgroups, p63s, p44s and p40s. The expression of cochlin is highly specific to the inner ear. Eleven missense mutation and one in-frame deletion have been reported in the COCH gene, causing hereditary progressive sensorineural hearing loss and vestibular dysfunction, deafness autosomal dominant type 9 (DFNA9). The co-localization of cochlin and type II collagen in the fibrillar substance in the subepithelial area indicate that cochlin may play a role in the structural homeostasis of the vestibule acting in concert with the fibrillar type II collagen bundles. Defects in COCH may contribute to Meniere disease which is an autosomal dominant disorder characterized by hearing loss associated with episodic vertigo.