placenta

Functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. In the DCX complexes, acts as a scaffolding subunit required to stabilize the complex. DDA1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 17.7 kDa and the accession number is Q9BW61.

Modulates leading keratinocyte migration and cellular adhesion to matrix proteins during a wound-healing response and promotes wound repair. May play a role during trichilemmal differentiation of the hair follicle.

INSL4 (Insulin-Like 4) is a Protein Coding gene. An important paralog of this gene is RLN1. INSL4 encodes a precursor that undergoes post-translational cleavage to produce 3 polypeptide chains, A-C, that form tertiary structures composed of either all three chains or just the A and B chains. INSL4 is a member of the insulin family, which includes insulin, IGF-I, IGF-II, relaxin, and INSL3.INSL4 distribution was tissue- and cell-specific. Indeed, INSL4 mRNA was most abundant in syncytiotrophoblast cells. In fetal tissues, INSL4 mRNA was identified in the perichondrium of all four limbs, vertebrae, and ribs. Diseases associated with INSL4 include Placenta Accreta and Chromosome 9P Deletion Syndrome.

Placental growth factor is a protein that in humans is encoded by the PGF gene. It is a secreted protein and belongs to the PDGF/VEGF growth factor family. The protein is a member of the VEGF (vascular endothelial growth factor) sub-family-a key molecule in angiogenesis and vasculogenesis, in particular during embryogenesis. The main source of PGF during pregnancy is the placental trophoblast. PGF is also expressed in many other tissues, including the villous trophoblast.

Pleckstrin Homology-Like Domain Family A Member 2 (PHLDA2) is a peripheral membrane protein that belongs to the PHLDA2 family. PHLDA2 is expressed in the placenta and adult prostate gland. In the placenta, it is present in all cells of the villous cytotrophoblast. PHLDA2 plays a role in regulating placenta growth. PHLDA2 may act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids.

Modulates leading keratinocyte migration and cellular adhesion to matrix proteins during a wound-healing response and promotes wound repair. May play a role during trichilemmal differentiation of the hair follicle. PLET1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 24.4 kDa and the accession number is Q6UQ28.

Modulates leading keratinocyte migration and cellular adhesion to matrix proteins during a wound-healing response and promotes wound repair. May play a role during trichilemmal differentiation of the hair follicle. PLET1 Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 22.3 kDa and the accession number is Q6UQ28.

PLAC9 belongs to the PLAC9 family. PLAC9 gene is a placental-enriched gene. There are other two placental-enriched genes: Plac1 and Plac8. Plac1 is strongly expressed in all trophoblast-derived cells in the placenta and has been described in 2. Plac8 expression is restricted to the spongiotrophoblast layer during development, whereas PLAC9 is weakly expressed though highly enriched in placenta. For both, cDNAs with complete open reading frames were recovered and exon-intron structures inferred from comparisons of mouse cDNA and genomic sequence. The predicted proteins both contain putative signal peptides, with a coiled-coil segment of mPLAC9 as the only other detected motif. Genomic sequence comparisons reveal that in addition to an apparent pseudogene on chromosome 1, Plac8 is expressed at mouse cytoband 5e3.

May play a role in placental development. PLAC1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 23.3 kDa and the accession number is Q9HBJ0.

Modulates leading keratinocyte migration and cellular adhesion to matrix proteins during a wound-healing response and promotes wound repair. May play a role during trichilemmal differentiation of the hair follicle.

Placental Lactogen/CSH1 Protein, Human, Recombinant (His), Biotinylated is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 23.7 kDa and the accession number is A8K6C2.

Alkaline phosphatase can be considered our favorite enzyme for reasons apparent to those who diagnose and treat metabolic bone diseases or who study skeletal biology. Few might know, however, that alkaline phosphatase likely represents the most frequently assayed enzyme in all of medicine. Elevated activity in the circulation is universally recognized as a marker for skeletal or hepatobiliary disease. Alkaline Phosphatase (Placental type) /ALPP Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 53.69 kDa and the accession number is XP_045223825.1.

Placental Lactogen/CSH1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 23.7 kDa and the accession number is A8K6C2.

Oncomodulin-1 (OM) is a small, calcium-binding protein and a macrophage-derived growth factor, which can promote axon regeneration in retinal ganglion cells. Oncomodulin-1 is constitutively secreted by activated macrophages in the vitreous and retina in response to inflammatory conditions that promote optic nerve regeneration. Oncomodulin-1 binds RGCs with high affinity in vitro, but only when cAMP is pharmacologically elevated or if the membrane is permeabilized allowing Oncomodulin-1 access to the cytosolic compartment. Oncomodulin-1 is a member of the superfamily of calmodulin proteins and is a high-affinity calcium ion-binding protein and contains 2 EF-hand domains. OM is found in early embryonic cells in the placenta and also in tumors. It has some calmodulin-like activity with respect to enzyme activation and growth regulation.

Lysosomal Pro-X Carboxypeptidase (PRCP) belongs to the peptidase S28 family. PRCP is detected in many tissues, with highest levels observed in placenta, lung, and liver. It is also present in the heart, brain, pancreas, and kidney. PRCP exists as a homodimer. PRCP cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. PRCP has been shown to be an activator of the cell matrix-associated prekallikrein.

E3 Ubiquitin-Protein Ligase CHIP is a cytoplasmic protein. CHIP is highly expressed in skeletal muscle, heart, pancreas, brain and placenta. CHIP interacts with the molecular chaperones Hsc70-Hsp70 and Hsp90 through its TPR domain; lead to in client substrate ubiquitylation and degradation by the proteasome. CHIP targets misfolded chaperone substrates towards proteasomal degradation. CHIP mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. CHIP plays a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. It also may regulate the receptor stability and activity through proteasomal degradation.

Macrophage colony-stimulating factor 1 receptor (CSF1R) is a member of the type III subfamily of receptor tyrosine kinases that also includes receptors for SCF and PDGF. These receptors each contain five immunoglobulin-like domains in their extracellular domain (ECD) and a split kinase domain in their intracellular region. CSF1R is expressed primarily on cells of the monocyte/macrophage lineage, dendritic cells, stem cells and in the developing placenta. CSF1 and its receptor (CSF1R, product of c-fms proto-oncogene) were initially implicated as essential for normal monocyte development as well as for trophoblastic implantation. It plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. It is required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.

Sedoheptulokinase (SHPK) belongs to the FGGY kinase family, and is mainly located in cytoplasm. SHPK is strongly expressed in liver, kidney and pancreas. It is expressed at lower levels in placenta and heart, and very weakly expressed in lung and brain. SHPK catalyzes the chemical reaction: ATP + sedoheptulose = ADP + sedoheptulose 7-phosphatecan, It can transform sedoheptulose to sedoheptulose 7-phosphate in the condition of ATP, and acts as a modulator of macrophage activation through control of glucose metabolism. In addition, It also can be down-regulated by LPS.

ALPP is a membrane protein and exits as a homodimer. ALPP is expressed only in normal term placenta, endocervix and fallopian tube and also in ovarian and proximal gastrointestinal tumors. It has been shown to play a role in a number of processes including cell signaling, long-term potentiation, and cell adhesion, however, the best known and most commonly studied role is implicated in Alzheimer's research.

Ribonuclease K6 (RNASE6) is a secreted protein that belongs to the pancreatic ribonuclease family. Human RNASE6 is synthesized as a 150 amino acid precursor that contains a 23 amino acid signal sequence, and a 127 amino acid mature chain. RNASE6 is expressed in many tissues, with high expression levels in the lung, with lower expression levels in the heart, placenta, kidney, pancreas, liver, brain, and skeletal muscle. It is also detected in monocytes and neutrophils. RNASE6 may have a role in host defense.

Human Zinc Finger MYND Domain-Containing Protein 19 (ZMYND19) is a protein that contains 1 MYND-Type Zinc Finger. ZMYND19 can be expressed by the brain, testis, placenta, heart, liver, skeletal muscle, kidney, and stomach. ZMYND19 interacts with GPR24/MCH-R1. It binds to the C terminus of Melanin-Concentrating Hormone Receptor-1 and the N Termini of α-Tubulin. ZMYND19 may be involved as a regulatory molecule in GPR24/MCH-R1 signaling.

WW Domain-Binding Protein 1 (WBP1) is widely expressed in many tissues, but it is lowly expressed in the lung, placenta, kidney, and liver. WBP1 contains two WW-binding motifs: WW-binding 1 and WW-binding 2 that are involved in mediating protein-protein interactions through the binding of polyproline ligands. The WW-binding domain is composed of 38 to 40 semi-conserved amino acids shared by proteins with diverse functions including structural, regulatory, and signaling proteins. In addition, WBP1 also encodes a ligand of the WW domain of the Yes kinase-associated protein. This function has not been determined.

Ubiquitin-Conjugating Enzyme E2 Z (ZUBE2Z) is a member of the E2 ubiquitin-conjugating enzyme family. ZUBE2Z is widely expressed in many tissues, with high expression found in the placenta, pancreas, spleen, and testis. It is ubiquitinates proteins that catalyze the covalent attachment of ubiquitin to other proteins. It has shown that ZUBE2Z participate in signaling pathways, and may be involved in apoptosis regulation.

Sperm Equatorial Segment Protein 1 (SPESP1) is a member of the SPESP1 family. SPESP1 is highly expressed in the testis, where it is localized to the acrosome of postmeiotic stages of spermiogenesis; it is expressed at lower levels in the placenta and fetal lung. SPESP1 is involved in the multicellular organisimal development. Disruption of SPESP1 leads to abnormal distribution of sperm proteins resulting in a detached membrane from the equatorial segment and less fertile sperm. SPESP1 may interact with IZUMO1 and MN9 antigen and it contains an N-glycosylation site as well as several cAMP-dependent kinase, protein kinase C, and casein kinase II consensus phosphorylation sites.

Human Vascular endothelial growth factor receptor 1(VEGFR-1, FLT-1) is a member of the the class III subfamily of receptor tyrosine kinases (RTKs) and Tyr protein kinase family and CSF-1/PDGF receptor subfamily. VEGFR-1 is widely expressed in human tissues including normal lung, placenta, liver, kidney, heart and brain tissues. It is specifically expressed in most of the vascular endothelial cellsand peripheral blood monocytes. VEGFR-1 contains seven Ig-like C2-type domains and one protein kinase domain. VEGFR-1is an essential receptor tyrosine kinase and plays an important role in theregulation of VEGF family-mediated vasculogenesis, angiogenesis, and lymphangiogenesis. It is also mediators of neurotrophic activity and regulators of hematopoietic development. VEGFR-1 is a receptor for VEGF, VEGFB and PGF. It has a tyrosine-protein kinase activity. Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF.It may play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells and promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. VEGFR-1 can also promote PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro).

Galectin-14 is a member of the Galectin family of carbohydrate binding proteins. The members of Galectin family contain one or two carbohydrate recognition domains, which can bind β-Galactoside. LGALS14 is expressed intracellularly in placenta and eosinophils, and is released by eosinophils following allergen stimulation. LGALS14 may be involved in the development of allergic inflammation. Two alternatively spliced transcript variants encoding distinct isoforms have been observed.

Beta-1,4-galactosyltransferase 3 (B4GALT3) belongs to the glycosyltransferase 7 family. It is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. It is highest expression in placenta, prostate, testis, ovary, intestine and muscle, and in fetal brain.

Proteoglycan 3, also known as Eosinophil major basic protein homolog, Prepro-major basic protein homolog, PRG3 and MBPH, contains one C-type lectin domain. Proteoglycans are a major component of the animal extracellular matrix. PRG3 localizes to the eosinophil secondary granule and is expressed in bone marrow, not detected in placenta. PRG3 has similar cytotoxic and cytostimulatory activities to PRG2/MBP. In vitro, PRG3 can stimulate neutrophil superoxide production and IL8 release, histamine and leukotriene C4 release from basophils.

Human sialidase 2 (NEU2) is a cytoplasmic sialidase that degrades sialyl glycoconjugates, including glycoproteins and gangliosides, via hydrolysis of terminal sialic acids to produce asialo-type molecules. It belongs to a family of glycohydrolytic enzymes that remove sialic acid residues from glycoproteins and glycolipids. NEU2 expression as assessed by quantitative real-time PCR was found to be extremely low or undetectable in many human tissues and cells, with notable exceptions like the placenta and testis. The human cytosolic sialidase NEU2 is the only mammalian enzyme structurally characterized and represents a valuable model to study the specificity of novel NA inhibitory drugs. Diseases associated with NEU2 include Galactosialidosis and Discrete Subaortic Stenosis.

NRBF2 (Nuclear Receptor Binding Factor 2) is a Protein Coding gene. The encoded protein may modulate transcriptional activation by target nuclear receptors. It is widely expressed in the appendix, placenta, and other tissues. NRBF2/Atg38 has been identified as the fifth subunit of the macroautophagy/autophagy class III phosphatidylinositol 3-kinase (PtdIns3K) complex, along with ATG14/Barkor, BECN1/Vps30, PIK3R4/p150/Vps15, and PIK3C3/Vps34. NRBF2 is a critical molecular switch of PtdIns3K and autophagy activation, and its on/off state is precisely controlled by MTORC1 through phosphorylation. NRBF2, a key component, and regulator of the PtdIns3K has been involved in APP-CTFs homeostasis in Alzheimer's disease (AD) cell models. NRBF2 plays an important role in regulating the degradation of APP-CTFs through modulating autophagy.

MESD (Mesoderm Development LRP Chaperone) is a Protein Coding gene. LDLR chaperone MESD, also known as Mesoderm development protein, Mesoderm development candidate 2, Renal carcinoma antigen NY-REN-61, and MESDC2, is a member of the MESD family. It is widely expressed in the thyroid, placenta, and other tissues. MESDC2 is a chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). The LDLR maturation activity resides in the N- and C-terminal unstructured regions. MESDC2 acts as a modulator of the Wnt pathway since some LDLRs are coreceptors for the canonical Wnt pathway. MESDC2 is essential for the specification of embryonic polarity and mesoderm induction.

Serum deprivation-response protein, also known as Phosphatidylserine-binding protein, Cavin-2 and SDPR, is a member of the PTRF / SDPR family. SDPR is highly expressed in heart and lung, and expressed at lower levels in brain, kidney, liver, pancreas, placenta, and skeletal muscle. SDPR is a new regulator of caveolae biogenesis. SDPR is up-regulated in asynchronously growing fibroblasts following serum deprivation but not following contact inhibition and Down-regulated during synchronous cell cycle re-entry. Caveolae are plasma membrane invaginations with a characteristic flask-shaped morphology. They function in diverse cellular processes, including endocytosis. Loss of SDPR causes loss of caveolae. SDPR binds directly to PTRF and recruits PTRF to caveolar membranes. Overexpression of SDPR, unlike PTRF, induces deformation of caveolae and extensive tubulation of the plasma membrane. SDPR overexpression results in increased caveolae size and leads to the formation of caveolae-derived tubules containing Shiga toxin. SDPR is a membrane curvature inducing component of caveolae, and that STB-induced membrane tubulation is facilitated by caveolae. Pleckstrin and SDPR are phosphorylated by protein kinase C (PKC), the interaction between pleckstrin and SDPR was shown to be independent of PKC inhibition or activation. SDPR may facilitate the translocation of nonphosphorylated pleckstrin to the plasma membrane in conjunction with phosphoinositides that bind to the C-terminal PH domain.

Carbonic anhydrase 5B, also known as carbonate dehydratase VB, carbonic anhydrase VB, CA-VB and CA5B, is amember of the alpha-carbonic anhydrase family. The strongest expression of CA5B / CA-VB is in heart, pancreas, kidney, placenta, lung, and skeletal muscle. It is not expressed in liver. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes first discovered in 1933 that catalyze the reversible hydration of carbon dioxide. CAs participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CAs show extensive diversity in tissue distribution and in their subcellular localization. CA5B / CA-VB is localized in the mitochondria and shows the highest sequence similarity to the other mitochondrial CA5A / CA-VA. CA5B / CA-VB has a wider tissue distribution than CA5A / CA-VA, which is restricted to the liver. The differences in tissue distribution suggest that the two mitochondrial carbonic anhydrases evolved to assume different physiologic roles. CA5A / CA-VA is activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. It is inhibited by coumarins, sulfonamide derivatives such as acetazolamide and Foscarnet (phosphonoformate trisodium salt). CA5B / CA-VB is inhibited by coumarins, sulfonamide derivatives such as acetazolamide (AZA), saccharin and Foscarnet (phosphonoformate trisodium salt).

TLR4, also known as TLR-4, is a member of the Toll-like receptor (TLR) family, which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. TLR4 is most abundantly expressed in placenta, and in myelomonocytic subpopulation of the leukocytes. TLR 4 has also been designated as CD284 (cluster of differentiation 284). It has been implicated in signal transduction events induced by lipopolysaccharide (LPS) found in most gram-negative bacteria. TLR4 Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). It acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. It is also involved in LPS-independent inflammatory responses triggered by Ni(2+).

cGMP-dependent 3',5'-cyclic phosphodiesterase, also known as cyclic GMP-stimulated phosphodiesterase and PDE2A, is a peripheral membrane protein that belongs to the cyclic nucleotide phosphodiesterase family and PDE2 subfamily. Phosphodiesterases (PDEs) comprise a family of enzymes that regulate the levels of cyclic nucleotides, key second messengers that mediate a diverse array of functions. Phosphodiesterases (PDEs) modulate signaling by cyclic nucleotides in diverse processes such as cardiac contractility, platelet aggregation, lipolysis, glycogenolysis, and smooth muscle contraction. PDE2A is an evolutionarily conserved cGMP-stimulated cAMP and cGMP PDE. PDE2A contains two GAF domains. PDE2A is expressed in brain and to a lesser extent in heart, placenta, lung, skeletal muscle, kidney and pancreas. PDE2A is a cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. PDE2A is involved in the regulation of blood pressure and fluid homeostasis by the atrial natriuretic peptide (ANP), making PDE2-type enzymes important targets for drug discovery.

Activin and inhibin are two closely related protein complexes that have almost directly opposite biological effects. The activin and inhibin protein complexes are both dimeric in structure, and, in each complex, the two monomers are linked to one another by a single disulfide bond. Activin is composed of two β subunits, βA βA (activin A), βB βB (activin B), or βA βB (activin AB). Inhibin is composed of an alpha and one of two β subunits, βA (inhibin A) or βB (inhibin B). Activins are produced in many cell types and organs, such as gonads, pituitary gland, and placenta. In the ovarian follicle, activin increases FSH binding and FSH-induced aromatization. It participates in androgen synthesis enhancing LH action in the ovary and testis. In the male, activin enhances spermatogenesis. Also, Activin plays a role in wound repair and skin morphogenesis. Activin is strongly expressed in wounded skin, and overexpression of activin in the epidermis of transgenic mice improves wound healing and enhances scar formation. Activin also regulates the morphogenesis of branching organs such as the prostate, lung, and kidney. There is also evidence showed that lack of activin during development results in neural developmental defects.

GPR37 (cathepsin Z) is an orphan receptor that belongs to the G-protein coupled receptor 1 family. G protein-coupled receptors are a large protein family comprised of transmembrane receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses. They only exist in eukaryotes, including yeast, choanoflagellates, and animals. These receptors are bonded and activated by light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters. These ligands vary in size from small molecules to peptides to large proteins. G protein-coupled receptors are involved in many diseases and are also the target of approximately 40% of all modern medicinal drugs. GPR37 is expressed in the brain and spinal cord, and at lower levels in the testis, placenta, and liver, but no detectable expression is observed in any other tissue. GPR37 may have a unique functional role in the central nervous system.

KIAA11, also known as p15(PAF), is a proliferating cell nuclear antigen-associated factor that interacts with proliferating cell nuclear antigen(PCNA). It was initially isolated in a yeast two-hybrid screen for PCNA binding partners and was shown to bind PCNA competitively with the cell cycle regulator p21(WAF). KIAA11 is localized primarily in the nucleus. It shares the conserved PCNA binding motif with several other PCNA binding proteins including CDK inhibitor p21. KIAA11 is involved in cell proliferation and plays a role in early tumor recurrence (ETR), and prognosis of hepatocellular carcinoma (HCC). KIAA11 is expressed predominantly in the liver, pancreas, and placenta. It cannot be detected in the heart or brain. It is highly expressed in some tumors, especially esophageal tumors, in anaplastic thyroid carcinomas, and non-small-cell lung cancer lines. Overexpression of KIAA11 predicts high stage, early tumor recurrence, and poor prognosis of hepatocellular carcinoma. It also may be involved in the protection of cells from UV-induced cell death.

Signal-Regulatory Protein Gamma (SIRPG) is a member of the signal-regulatory protein (SIRP) family and also belongs to the immunoglobulin superfamily. SIRPG is detected in the liver, and at very low levels in the brain, heart, lung, pancreas, kidney, placenta, and skeletal muscle. SIRPG is an immunoglobulin-like cell surface receptor. On binding with CD47, SIRPG mediates cell-cell adhesion. Engagement on T-cells by CD47 on antigen-presenting cells results in enhanced antigen-specific T-cell proliferation and costimulates T-cell activation. SIRPG as receptor-type transmembrane glycoproteins is involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes.

Human Siglec-5 are Itype(Igtype) lectins belonging to the Ig superfamily,They are characterized by an N terminal Ig-like V type domain which mediates sialic acid binding, followed by varying numbers of Ig-like C2 type domains. SIGLEC5 has also been designated CD170, they are expressed by monocytic or myeloid lineage cells, and also found at high levels in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. SIGLEC5 are expressed by monocytes and neutrophils but absent from leukemic cell lines representing early stages of myelomonocytic differentiation. Siglec5 to 11 share a high degree of sequence similarity with CD33/Siglec3 both in their extracellular and intracellular regions. They are collectively referred to as CD33 related Siglecs. One remarkable feature of the CD33 related Siglecs is their differential expression pattern within the hematopoietic system This fact, together with the presence of two conserved immunoreceptor tyrosinebased inhibition motifs (ITIMs) in their cytoplasma tails, suggests that CD33 related Siglecs are involved in the regulation of cellular activation within the immune system.

Platelet-Derived Growth Factor Subunit B (PDGFB) belongs to the PDGF/VEGF growth factor family. Platelet-derived growth factor is a potent mitogen for cells of mesenchymal origin. PDGFB can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. As growth factor，it plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. It is required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. PDGFB also plays an important role in wound healing.

Zinc Finger BED Domain-Containing Protein 1 (ZBED1) contains one BED-type zinc finger and is found in the cell nucleus. ZBED1 is widely expressed, highly in heart, skeletal muscle, spleen and placenta. The expression of ZBED1 is usually linked to the cell cycle. During the G1/S phase, the expression is increasing. During the S/G2 phage, the expression reaches to the highest, and then decreasing. ZBED1 exists in homodimer forms, which can bind to 5’-TGTCCG[CT]GA[CT]A-3’ DNA elements, that can be found in the promoter regions of a number of gene related to cell proliferation.

Myelin protein zero-like protein 1(MPZL1) is encoded by the MPZL1 gene, which is a single-pass type I membrane protein. It is widely expressed with highest levels in heart, placenta, kidney and pancreas. As cell surface receptor, it involved in signal transduction processes. MPZL1 recruits PTPN11/SHP-2 to the cell membrane and subsequently activate/phosphorylate Src kinase at Tyr426, promoting phosphorylation of cortactin and migration of HCC cells. MPZL1also is a major receptor for concanavalin-A (ConA) and involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases.

The chimeric protein binds in vitro and in vivo to a specific element upstream of LRRC15, leading to dramatic transcriptional activation.  LRRC15 encodes a leucine-rich transmembrane protein, present at the leading edge of migrating cells, the expression of which in normal tissues is restricted to the invasive cytotrophoblast layer of the placenta; small interfering (siRNA)-mediated suppression of LRRC15 expression in breast cancer cells leads to abrogation of invasiveness in vitro. LRRC15 Protein, Cynomolgus/Rhesus macaque, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 58.92 kDa and the accession number is A0A2K5UKB6.

Podoplanin is a type-1 transmembrane protein that belongs to Podoplanin family. PDPN expressed in various specialized cell types throughout the body. It highly expressed in placenta, lung, skeletal muscle and brain, weakly expressed in brain, kidney and liver. In placenta, PDPN expressed on the apical plasma membrane of endothelium, in lung, expressed in alveolar epithelium. PDPN physiological function is related to its mucin-type character. PDPN may be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, and major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. It requires for normal lung cell proliferation and alveolus formation at birth and Induces platelet aggregation. Nevertheless, it doesn’t have any effect on amino acid transport and the aquaporin-type water channels.

Ubiquitin-Associated Protein 1 (UBAP1) belongs to the UBA domain family. Members of this family are related to ubiquitin and the ubiquitination pathway. Because of their cytogenetic location, this UBA domain family member is being studied as a putative target for mutation in nasopharyngeal carcinomas. UBAP1 is highly expressed in the heart, brain, placenta, lung, skeletal muscle, liver, and pancreas. UBAP1 consists of two UBA domains and one UMA domain. The ubiquitin associated domain is throught to be a non-covalent ubiquitin binding domain, including a compact three helix bundle.

Krueppel-Like Factor 6 (KLF6) belongs to the krueppel C2H2-type zinc-finger protein family. KLF6 contains three C2H2-type zinc fingers and localizes in the nucleus. KLF6 expression is highest in the placenta followed by spleen, thymus, prostate, testis, small intestinem and colon. However, it is weakly expressed in the pancreas, lung, liver, heart, and skeletal muscle. KLF6 functions as a transcriptional activator and could play a role in B-cell growth and development. Defects in KLF6 will result in gastric cancer and prostate cancer.

Ubiquitin-like-conjugating enzyme ATG3 (ATG3), also known as Apg3L and Apg3p, functions as a regulatory component of autophagosome biogenesis necessary for autophagy. ATG3 exhibits 98% aa sequence identity with both its mouse and rat orthologs. It is widely expressed and has highly levels in heart, skeletal muscle, kidney, liver and placenta. As an E2-like enzyme, involves in autophagy and mitochondrial homeostasis. ATG3 catalyzes the conjugation of ATG8-like proteins to PE which is essential for autophagy. ATG3 also can catalyze the conjugation of ATG12 to itself which palys a role in mitochondrial homeostasis but not in autophagy.

Multiple Inositol Polyphosphate Phosphatase 1/MINPP1 is an enzyme that removes 3-phosphate from inositol phosphate substrates. MINPP1 also converts 2,3 bisphosphoglycerate (2,3-BPG) to 2-phosphoglycerate. MINPP1 is synthesized as a 487 amino acid precursor that contains an 30 amino acid signal peptide and a 457 amino aicd mature chain. MINPP1 is widely expressed with the highest levels found in kidney, liver and placenta. It acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). MINPP1 may play a role in bone development (endochondral ossification).

Low-Density Lipoprotein Receptor-Related Protein 12 (LRP12) belongs to the LDLR family. LRP12 is a type I transmembrane protein annd widely expressed in heart, skeletal muscle, brain, lung, placenta and pancreas. LRP12 contains 2 CUB domain and 5 LDL-receptor class A domain. LRP12 has been shown to interact with GNB2L1, ZFYVE9 and ITGB1BP3. LRP12 is a receptor probably, which may be involved in the internalization of lipophilic molecules and/or signal transduction. In addition, LRP12 may act as a tumor suppressor.