fetal kidney

Cadherin 6/CDH6 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 67.9 kDa and the accession number is A6KJN4.

Cadherin 6/CDH6 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 67.5 kDa and the accession number is XP_005556691.1.

Cadherin 6/CDH6 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 68 kDa and the accession number is P55285-1.

Cadherin 6/CDH6 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 68.7 kDa and the accession number is P97326.

This protein may be involved in regulating membrane traffic to and from trans-Golgi network. Isoform TGN46 is widely expressed. Isoform TGN51 is more abundant in fetal lung and kidney. Isoform TGN48 is barely expressed in embryonic kidney and promyelocytic cells.

WAP, kazal, immunoglobulin, kunitz and NTR domain-containing protein 2, also known as Growth and differentiation factor-associated serum protein 1, WAP, follistatin, immunoglobulin, kunitz and NTR domain-containing-related protein, WFIKKN-related protein, WFIKKN2 and GASP1, is a secreted protein that belongs to the WFIKKN family. WFIKKN2 contains two BPTI/Kunitz inhibitor domains, one Ig-like C2-type (immunoglobulin-like) domain, one Kazal-like domain, one NTR domain and one WAP domain. WFIKKN2 is primarily expressed in ovary, testis and brain, but not in liver. In fetal tissues, it is primarily expressed in brain, skeletal muscle, thymus and kidney. WFIKKN2 is a protease-inhibitor that contains multiple distinct protease inhibitor domains. It probably has serine protease- and metalloprotease-inhibitor activity. It inhibits the biological activity of mature myostatin, but not activin. WFIKKN2 protein binds mature GDF8/myostatin and myostatin propeptide and inhibits the biological activity of myostatin.

A brain-enriched secreting signal peptide, NELL2, has been suggested to play multiple roles in the development, survival, and activity of neurons in the mammal. NELL2 is an abundant glycoprotein containing an EGF-like domain in the neural tissues where it has multiple physiological functions by interacting with protein kinase C (PKC). There are two different splicing variant forms of NELL2 identified so far. One is secreted NELL2 (sNELL2) which is a neuron-specific variant and the other is cytosolic NELL2 (cNELL2) which is a non-secreted splicing variant of NELL2. NELL2 is strongly expressed in the brain of adults and fetuses but only weakly in the fetal kidney.

Endothelial Differentiation-Related Factor 1 (EDF1) is a 148 amino acid transcriptional coactivator that contains 1 HTH cro/C1-type DNA-binding domain. It has been postulated that the protein functions as a bridging molecule that interconnects regulatory proteins and the basal transcriptional machinery, thereby modulating the transcription of genes involved in endothelial differentiation. When endothelial cells are induced to differentiate in vitro, EDF1 is downregulated, leading to inhibition of cell growth and cell polarization. EDF1 binds calmodulin thorough its IQ domain and regulates nitric oxide synthase activity through calmodulin sequestration in the cytoplasm. Though ubiquitously expressed, EDF1 is most abundant in adult liver, heart, adipose tissues, intestine and pancreas. In fetal tissues, EDF1 is most abundant in kidney. There are two isoforms of EDF1 that are produced as a result of alternative splicing events.

Human Sulfotransferase (SULT1C4) is an enzyme that in humans is encoded by the SULT1C4 gene, belongs to the sulfotransferase 1 family. SULT1C4 is expressed at high levels in fetal lung and kidney and at low levels in fetal heart, adult kidney, ovary and spinal chord. Sulfotransferase utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. It shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF). SULT1C4 plays an important role incatalyzing the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds.

Peptidoglycan recognition protein 1, also known as Peptidoglycan recognition protein short, PGRP-S, PGLYRP1, PGLYRP, PGRP and TNFSF3L, is a secreted protein that belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. PGLYRP1 / PGLYRP is highly expressed in bone marrow. It is weakly expressed in kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils. PGLYRP1 / PGLYRP is a pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. It has bactericidal activity towards Gram-positive bacteria. PGLYRP1 / PGLYRP may kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. It binds also to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Peptidoglycan recognition proteins (PGRPs or PGLYRPs) are innate immunity proteins that are conserved from insects to mammals, recognize bacterial peptidoglycan, and function in antibacterial immunity and inflammation. Mammals have four PGRPs: PGLYRP1, PGLYRP2, PGLYRP3, and PGLYRP4. They are secreted proteins expressed in polymorphonuclear leukocytes (PGLYRP1), liver (PGLYRP2), or on body surfaces, mucous membranes, and in secretions (saliva, sweat) (PGLYRP3 and PGLYRP4). All PGRPs recognize bacterial peptidoglycan. The PGRPs likely play a role both in antibacterial defenses and several inflammatory diseases. They modulate local inflammatory responses in tissues (such as arthritic joints) and there is evidence for association of PGRPs with inflammatory diseases, such as psoriasis.

Sulfotransferase 1C2 (SULT1C2) is a cytosolic enzyme member of the Sulfotransferase 1 family. Human SULT1C2 is primarily expressed in the adult stomach, kidney and thyroid gland, and in the fetal kidney and liver. SULT1C2 catalyzes the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. SULT1C2 may be involved in the activation of carcinogenic hyroxylamines. It shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF).

Frizzled-1, also known as FZD1, belongs to theG-protein coupled receptor Fz/Smo family. FZD1 contains a signal peptide, a cysteine-rich domain in the N-terminal extracellular region, 7 transmembrane domains, and a C-terminal PDZ domain-binding motif. FZD1 is expressed in adult heart, placenta, lung, kidney, pancreas, prostate, and ovary and in fetal lung and kidney. Frizzled is a family of G protein-coupled receptor proteins that serve as receptors in the Wnt signaling pathway and other signaling pathways. When activated, Frizzled leads to activation of Dishevelled in the cytosol. Frizzled proteins and the genes encoding them have been identified in an array of animals, from sponges to humans. Frizzled proteins play key roles in governing cell polarity, embryonic development, formation of neural synapses, cell proliferation, and many other processes in developing and adult organisms. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes.

Death domain-containing protein CRADD, also known as Caspase and RIP adapter with death domain, RIP-associated protein with a death domain, CRADD and RAIDD, is a protein which is constitutively expressed in most tissues, with particularly high expression in adult heart, testis, liver, skeletal muscle, fetal liver and kidney. CRADD / RAIDD contains oneCARD domain and onedeath domain. CRADD / RAIDD contains a death domain involved in the binding of RIP protein. The CARD domain mediates the interaction with caspase-2. FADD / MORT1 is a death domain (DD)-containing adaptor / signaling molecule that interacts with the intracellular DD of FAS / APO-I ( CD95 ) and tumor necrosis factor receptor 1 and the prodomain of caspase-8 ( Mch5 / MACH / FLICE). CRADD / RAIDD has a dual-domain structure similar to that of FADD. CRADD / RAIDD has an NH2-terminal caspase homology domain that interacts with caspase-2 and a COOH-terminal DD that interacts with RIP. CRADD / RAIDD could play a role in regulating apoptosis in mammalian cells. CRADD / RAIDD is a apoptotic adaptor molecule specific for caspase-2 and FASL / TNF receptor-interacting protein RIP. In the presence of RIP and TRADD, CRADD / RAIDD recruits caspase-2 to the TNFR-1 signalling complex.

C12orf53 is mainly expressed in adult brain and cerebellum. It also can be detected in fetal brain and virtually no expression in spleen, heart, kidney, liver and dorsal ganglion relative to brain. C12orf53 acts as a ligand for PILRA in neural tissues, where it may be involved in immune regulation. Chromosome 12 encodes over 1,100 genes within 132 million bases. A number of skeletal deformities are linked to chromosome 12 including hypochondrogenesis, achondrogenesis and Kniest dysplasia. Noonan syndrome, which includes heart and facial developmental defects among the primary symptoms, is caused by a mutant form of PTPN11 gene product, SH-PTP2. Chromosome 12 is also home to a homeobox gene cluster which encodes crucial transcription factors for morphogenesis, and the natural killer complex gene cluster encoding C-type lectin proteins which mediate the NK cell response to MHC class I interaction.

Suppressor of cytokine signaling 3, also known as SOCS-3, Cytokine-inducible SH2 protein 3, CIS-3, STAT-induced STAT inhibitor 3, SOCS3 and CIS3, is a protein which is widely expressed with high expression in heart, placenta, skeletal muscle, peripheral blood leukocytes, fetal and adult lung, and fetal liver and kidney. SOCS3 / CIS3 contains one SH2 domain and one SOCS box domain. SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 / CIS3 is involved in negative regulation of cytokines that signal through the JAK / STAT pathway. SOCS3 / CIS3 inhibits cytokine signal transduction by binding to tyrosine kinase receptors including gp13, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity. SOCS3 / CIS3 suppresses fetal liver erythropoiesis. It regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells. SOCS3 / CIS3 regulates IL-6 signaling. SOCS3 / CIS3 interacts with multiple activated proteins of the tyrosine kinase signaling pathway including IGF1 receptor, insulin receptor and JAK2. SOCS3 / CIS3 could be used as a possible therapeutic agent for treating rheumatoid arthritis.

DCX (doublecortin, N-GST chimera)contains 2 doublecortin domains and belongs to the doublecortin family. It is highly expressed in neuronal cells of fetal brain, but not expressed in other fetal tissues. In the adult, it is highly expressed in the brain frontal lobe, but very low expression in other regions of brain, and not detected in heart, placenta, lung, liver, skeletal muscles, kidney and pancreas. DCX is a microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. It may act by competing with the putative neuronal protein kinase DCAMKL1 in binding to a target protein. DCX may in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. It may be part with LIS-1 of a overlapping, but distinct, signaling pathways that promote neuronal migration. Defects in DCX are the cause of lissencephaly X-linked type 1 and subcortical band heterotopia X-linked.

Death Domain-Containing Protein CRADD (CRADD) is widely expressed in most tissues, with particularly high expression in the adult heart, testis, liver, skeletal muscle, fetal liver, and kidney. CRADD contains one CARD domain that mediates the interaction with caspase-2, and one death domain involved in the binding of RIP protein. CRADD functions as an apoptotic adaptor molecule specific for caspase-2 and FASL/TNF receptor-interacting protein RIP. CRADD induces cell apoptosis/cell death in numerous tissues. Defects in CRADD will result in mental retardation.