mice

Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active against both mammals and insects. Tb2-II Protein, Tityus bahiensis, Recombinant (E. coli, His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 12.0 kDa and the accession number is P60276.

Beta-mammal insect toxin Ts1 Protein, Tityus serrulatus, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 10.8 kDa and the accession number is P15226.

Beta-mammal insect toxin Ts1 Protein, Tityus serrulatus, Recombinant (E. coli, His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 14.3 kDa and the accession number is P15226.

Alpha-mammal toxin Ts2 Protein, Tityus serrulatus, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 10.9 kDa and the accession number is P68410.

Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active against both mammals and insects. Tb2-II Protein, Tityus bahiensis, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 10.8 kDa and the accession number is P60276.

Hemicentin-1 Protein, Human, Recombinant (His) is expressed in E. coli.

Transforming growth factor beta 2 (TGF-β2) is a member of TGF-beta superfamily that shares a characteristic cysteine knot structure. Mice with TGF-β2 gene deletion show defects in development of cardiac, lung, craniofacial, limb, spinal column, eye, inner ear and urogenital systems. All TGF-β isoforms signal via the same heteromeric receptor complex, consisting of a ligand binding TGF-β receptor type II (TβR-II), and a TGF-β receptor type I (TβR-I). Signal transduction from the receptor to the nucleus is mediated via SMADs. TGF-β expression is found in cartilage, bone, teeth, muscle, heart, blood vessels, haematopoitic cells, lung, kidney, gut, liver, eye, ear, skin, and the nervous system.

Butyrophilin-like 6 (BTNL6) is a member of the BTN MOG Ig-superfamily and functions with BTNL1 as a regulator of immune cell proliferation. The Btnl6 gene is found only in mice. BTNL6 expression is coordinated as a heteromeric protein with BTNL1, and the presence of this complex is correlated with expansion of gamma δ T cells, especially those containing V gamma 7Vδ4 TCR. Btnl6 shows striking sequence similarity to Skint1; is also largely restricted to an epithelial tissue (the small intestine) replete with T cells. Our in-house studies showed BTNL6 co-inhibited anti-CD3 induced IL-2 secretion on CD3+ cells.

TGF-beta RI, also called ALK-5, is an approximately 55 kDa type I transmembrane serine threonine receptor kinase. In the presence of TGF-beta, TGF-beta RI forms a complex with, and is phosphorylated by, TGF-beta RII. Phosphorylated TGF-beta RI can then transiently bind and phosphorylate Smad2 and Smad3. TGF-beta functions as a tumor suppressor by inhibiting the cell cycle in the G1 phase. Administration of TGF-beta is able to protect against mammary tumor development in transgenic mouse models in vivo. Disruption of the TGF-beta SMAD pathway has been implicated in a variety of human cancers, with the majority of colon and gastric cancers being caused by an inactivating mutation of TGF-beta RII. TGF-beta RI is likely important during development, since mice deficient for TGF-beta RI die at midgestation with severe defects in vascular development of the yolk sac and placenta, and an absence of circulating red blood cells. Furthermore, TGF-beta RI appears to be involved in proper lymphatic network development.

Pentraxin-2 (PTX-2), also known as serum amyloid P component (SAP APCS), is a constitutive, antiinflammatory, innate immune plasma protein whose circulating level is decreased in chronic human fibrotic recombinant human PTX-2 (rhPTX-2) retards progression of chronic kidney disease in Col4a3 mutant mice with Alport syndrome, reducing blood markers of kidney failure, enhancing lifespan by 20%, and improving histological signs of disease. diseases. Pentraxin 2 SAP Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 50 kDa and the accession number is P02743.

Hepatitis A virus cellular receptor 2（HAVCR2）is a single-pass type I membrane protein and it contains 1 Ig-like V-type (immunoglobulin-like) domain. The protein belongs to the immunoglobulin superfamily, and TIM family of proteins. The protein regulates macrophage activation. It inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. It may be also involved in T-cell homing and it is receptor for LGALS9. CD4 (MIM 186940)-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells and their associated cytokines are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. The 2 types of cells also cross-regulate the functions of the other. TIM3 is a Th1-specific cell surface protein that regulates macrophage activation and enhances the severity of experimental autoimmune encephalomyelitis in mice.

Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. As IL-17 shares properties with IL-1 and TNF-alpha, it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis, and produced by rheumatoid arthritis synovium. It increases IL-6 production, induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.

Fibroblast Growth Factor 21 (FGF21) is a growth factor that belongs to the FGF family. FGF family proteins play a central role during prenatal development and postnatal growth and regeneration of mamy tissues, by promoting cellular proliferation and differentiation. FGF21 is a potent activator of glucose uptake on adipocytes, protects animal from diet-induced obesity when overexpression in transgenic mice, and lower blood glucose and triglyceride levels when therapeutically adiministered to diabetic redents. FGF21 is produced by hepatocytes in reponse to free fatty acid stimulation of a PPARa RXR dimeric complex. This situation occurs clinically during starvation, or following the ingestionof a highly-fat low-carbohydrate diet. Upon FGF21 secretion, white adipose tissue is induced to release free fatty acids from triglyceride stores. Once free fatty acid reach hepatocytes, they are oxidized and reduced to acetyl-CoA. The acetyl-CoA is recombined into 4-carbon ketone bodies, release, and transported to peripheral tissue for TCA processing and energy generation.

Cytokines were the first modern immunotherapies to produce durable responses in patients with advanced cancer,components of the interleukin-18 (IL-18) pathway are upregulated on tumour-infiltrating lymphocytes, suggesting that IL-18 therapy could enhance anti-tumour immunity. IL-18BP, a high-affinity IL-18 decoy receptor, is frequently upregulated in diverse human and mouse tumours and limits the anti-tumour activity of IL-18 in mice. IL-18BP Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 20.5 kDa and the accession number is O95998-2.

A cecal ligation and puncture-induced sepsis mouse model was established to determine the expression of mast cell expression membrane protein 1 (MCEMP1). MCEMP1 in T lymphocytes isolated from sepsis mice were up- or downregulated by exogenous transfection in an attempt to investigate their effects on the release of inflammatory factors, the expression of immunoglobulins, the activity of T cell subsets and natural killer (NK) cells, as well as T lymphocyte apoptosis.

Lactoylglutathione lyase, also known as Methylglyoxalase, Aldoketomutase, Glyoxalase I, Ketone-aldehyde mutase, S-D-lactoylglutathione methylglyoxal lyase and GLO1, is a member of the glyoxalase I family. GLO1 Glyoxalase I is a ubiquitous cellular defense enzyme involved in the detoxification of methylglyoxal, a cytotoxic byproduct of glycolysis. Accumulative evidence suggests an important role of GLO1 expression in protection against methylglyoxal-dependent protein adduction and cellular damage associated with diabetes, cancer, and chronological aging. GLO1 Glyoxalase I has been implicated in anxiety-like behavior in mice and in multiple psychiatric diseases in humans. GLO1 Glyoxalase I catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. GLO1 Glyoxalase I exists in three separable isoforms which originate from two alleles in the genome. These correspond to two homodimers and one heterodimer composed of two subunits showing different electrophoretic properties. GLO1 upregulation may play a functional role in glycolytic adaptations of cancer cells.

Dickkopf-like 1 (DKKL1) or soggy 1, is a glycoprotein unique to mammals that is expressed primarily in developing spermatocytes and localized in the acrosome of mature sperm. It is also expressed in the trophectoderm placental lineage. This glycoprotein is secreted by postmeiotic male germ cells. DKKL1 is a member of the Dickkopf (DKK) family, a group of proteins that are characterized as secreted antagonists of Wnt signal transduction proteins. In mammals, embryos lacking DKKL1 protein developed into viable, fertile adults. DKKL1, either directly or indirectly, facilitates the ability of sperm to penetrate the zona pellucid. DKKL1 is related to the sperm apoptotic procession. Molecular analyses identified the Fas death ligand (FasL) as a target for DkkL1 pro-apoptotic activity in adult mice. DKKL1 is considered as a negative regulator of adult testic homeostasis and identifies a novel, DKKL1 FasL- dependent, regulation that specifically controls the number of postpubertal spermatocytes.

PON3 was enriched in the mitochondria-associated membrane fraction of hepatocytes. PON3 deficiency resulted in impaired mitochondrial respiration, increased mitochondrial superoxide levels, and increased hepatic expression of inflammatory genes. PON3 deficiency did not influence atherosclerosis development on an apolipoprotein E null hyperlipidemic background, but it did lead to a significant 60% increase in atherosclerotic lesion size in Pon3KO mice on the C57BL 6J background when fed a cholate-cholesterol diet.

CALCB, also known as CGPR and calcitonin 2, belongs to the calcitonin family. CALCB is a calcitonin (CT) peptide which may play a role in the mediation of human inflammatory diseases. It is highly expressed in the skin, blood, and cerebrospinal fluid. CGRP immunolabeling (IL) was detected in epidermal keratinocytes at levels that were especially high and widespread in the skin of humans from locations afflicted with postherpetic neuralgia (PHN) and complex region pain syndrome type 1 (CRPS), of monkeys infected with simian immunodeficiency virus, and of rats subjected to L5 L6 spinal nerve ligation, sciatic nerve chronic constriction, and subcutaneous injection of complete Freund's adjuvant. Increased CGRP-IL was also detected in epidermal keratinocytes of transgenic mice with keratin-14 promoter driven overexpression of noggin, an antagonist to BMP-4 signaling. CGPR dilates a variety of vessels including the coronary, cerebral and systemic vasculature.

Ca2+ calmodulin-dependent protein kinase2A (CAMK2A) belongs to the serine threonine protein kinase family and, together with other 28 different isoforms, belongs to the Ca2+ calmodulin-dependent protein kinase subfamily. CaM kinase Ⅱ is thought to be an important mediator of learning and memory and is also necessary for Ca2+homeostasis and reuptake in cardiomyocytes chloride transport in epithelia, positive T-cell selection, and CD8 T-cell activation. CAMKIIA is one of the major forms of CAMKII. It has been found to play a critical role in sustaining activation of CAMKII at the postsynaptic density. Studies have found that knockout mice without CAMKIIA demonstrate a low frequency of LTP. Additionally, these mice do not form persistent, stable place cells in the hippocampus.

Tumor protein p63 is a protein also known as transformation-related protein 63, TP63, and p63. Tumor protein p63 p63 is a member of the p53 family of transcription factors whose members P53, p63, and p73 have similar features in their gene structures and functions. An animal model, p63- - mice has been useful in difining the role p63 plays in the development and maintenance of stratified epithelial tissues. This p63 encoding protein p63 has a dramatic impact on replenishment of cutaneous epithelial stem cells and on ovarian germ cell survival. Although these two fundamental roles of p63 attest to its powerful place in development, its other functions, specifically the apparent capacity of p63, is to supervise the emergence of new cell populations in the breast, prostate, cervix, and upper reproductive tract. P63- - mice have several development defects which include the lack of limbs and other tissues, such as teeth and mammary glands, which develop as a result of interactions between mesenchyme and epithelium. Mutations in this protein are associated with ectodermal dysplasia, and cleft lip palate syndrome 3, ADULT syndrome (acro-dermato-ungual-lacrimal-tooth), limb-mammary syndrome, et al.

Scavenger Receptor Class B Member 2 (SCARB2) is a type III multi-pass membrane glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes on all tissues and cell types so far examined. Earlier studies in mice and rat suggested that this protein may participate in membrane transportation and the reorganization of endosomal lysosomal compartment. The protein deficiency in mice was reported to impair cell membrane transport processes and cause pelvic junction obstruction, deafness, and peripheral neuropathy. Further studies in human showed that this protein is identified as a receptor for EV71 (human enterovirus species A, Enterovirus 71) and CVA16 (coxsackievirus A16) which are most frequently associated with hand, foot and mouth disease (HFMD). Mutations in this gene caused an autosomal recessive progressive myoclonic epilepsy-4 (EPM4), also known as action myoclonus-renal failure syndrome (AMRF). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. In addition, SCARB2 also has been shown to bind thrombospondin-1, may contribute to the pro-adhesive changes of activated platelets during coagulation, and inflammation.

Tumor necrosis factor receptor superfamily member 9(TNFRSF9) is a member of the tumor necrosis factor (TNF) receptor family. It can be induced by lymphocyte activation (ILA) and is expressed by activated T cells, but to a larger extent on CD8 than on CD4 T cells. In addition, TNFRSF9 expression is found on dendritic cells, follicular dendritic cells, natural killer cells, granulocytes and cells of blood vessel walls at sites of inflammation. As receptor for TNFSF9 4-1BBL, it can activate T cells and the cross-linking of this protein can enhance T cell proliferation, IL-2 secretion survival and cytolytic activity. Further, it can enhance immune activity to eliminate tumors in mice.

Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. Today, IL-17 represents a family of structurally related cytokines that share a highly conserved C-terminal region but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17F also regulates cartilage matrix turnover and inhibits angiogenesis.

Human Interleukin 31 (IL-31) is a cytokine containing a four-helix bundle structure. It shares several structural and functional characteristics with IL-6, Oncostatin M, LIF, and Cardiotrophin-1. Human IL-31 cDNA encodes a 164 amino acid precursor that contains a 23 amino acid signal peptide and a 141 amino acid mature protein. Human and mouse IL-31 share 24% sequence identity in the mature region. IL-31 is mainly associated with activated T cells and is preferentially expressed by type 2 helper T cells (Th2). IL-31 signals via a heterodimeric receptor complex composed of a gp130 related molecule termed IL-31RA (also GPL and GLMR) and an Oncostatin M receptor (OSM Rβ). The IL-31 receptor is constitutively expressed by keratinocytes and upregulated by IFNγ on monocytes. GPL OSMR signaling is a strong activator of STAT3 and STAT5, and can also activate STAT1, Jak1, and Jak2 signaling pathways. IL-31 regulated immune responses have been implicated in skin physiology and inflammatory skin diseases. Studies have shown that IL31 induces severe pruritis (itching) and dermatitis in transgenic mice.

Follistatin 288 is a secreted glycoprotein that was first identified as a follicle-stimulating hormone inhibiting substance in ovarian follicular fluid . Human follistatin 288 cDNA encodes a 317 amino acid (aa) protein with a 29 aa signal sequence, and a 288 aa mature region. Follistatin shows the highest affinity for activins due to its extended configuration. Genetic deletion of follistatin in mice, or expression of only the Follistatin form, is perinatally lethal due to defects of lung, skin and musculoskeletal system. Follistatins also regulate hematopoietic stem cell adhesion to fibronectin via FS2.

Myeloperoxidase (MPO) is a hemecontaining enzyme belonging to the XPO subfamily of peroxidases. It is an abundant neutrophil and monocyte glycoprotein that catalyzes the hydrogen peroxidedependent conversion of chloride, bromide, and iodide to multiple reactive species. MPO activity results in protein nitrosylation and the formation of 3-chlorotyrosine and dityrosine crosslinks. Modification of ApoB100, as well as the lipid and cholesterol components of LDL and HDL, promotes the development of atherosclerosis. MPO is also associated with a variety of other diseases, and inhibits vasodilation in inflammation by depleting the levels of NO. Serum albumin functions as a carrier protein during MPO movement to the basolateral side of epithelial cells. MPO is stored in neutrophil azurophilic granules. Upon cellular activation, it is deposited into pathogencontaining phagosomes. While mice lacking MPO are impaired in clearing select microbial infections,MPO deficiency in humans does not necessarily result in heightened susceptibility to infections.

Serpin E2 is a member of the Serpin superfamily. It is differentially expressed during neuronal differentiation and is able to transform human embryonic kidney cells into neuronlike cells. Its over-expression in mice leads to progressive neuronal and motor dysfunction in these animals. It is also over-expressed in the majority of pancreatic carcinoma as well as gastric and colorectal cancer samples whereas it is weakly expressed in all normal pancreas and chronic pancreatitis tissue samples. Serpin E2 is a potent inhibitor of thrombin, trypsin, urokinase, plasmin and plasminogen activators. It plays an important role in controlling male fertility because its knockout male mice show a marked impairment in fertility from the onset of sexual maturity and its abnormal expression is found in the semen of men with seminal dysfunction.

Exostosin-like 2 (EXTL2) is a member of the exostosin (EXT)-related family which contains five members: EXT1, EXT2, EXTL1, EXTL2, and EXTL3. Studies have shown that EXT gene family members have the activities of heparan sulfate-synthesizing glycosyltransferases. EXT1 and EXT2, which have been identified as causal genes for hereditary multiple exostoses, have HS-GlcAT-II and GlcNAcT-II activities. EXTL1 has GlcNAcT-II activity and EXTL3 has GlcNAcT-I and -II activities. EXTL2 has GlcNAcT-I and N-acetylgalactosaminyltransferase activities, and transfers a GlcNAc residue to the tetrasaccharide linkage region when this region is phosphorylated by a xylose kinase 1 (FAM20B) and thereby terminate chain elongation. In mice, lack of EXTL2 causes glycosaminoglycan (GAG) overproduction and structural changes of GAGs associated with pathological processes.

Recent studies have implicated chemokines in microglial activation and pathogenesis of neuropathic pain. C-X-C motif chemokine 13 (CXCL13) is a B lymphocyte chemoattractant that activates CXCR5. Using the spinal nerve ligation (SNL) model of neuropathic pain, CXCL13 was persistently upregulated in spinal cord neurons after SNL, resulting in spinal astrocyte activation via CXCR5 in mice. CXCL13 BCA-1 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with N-hFc tag. The predicted molecular weight is 37.6 kDa and the accession number is O43927.

SLAMF6 (signaling lymphocyte activation molecule 6) (Ly108 in mice, NTB-A or SF2000 in humans) is a homophilic receptor belonging to the superfamily immunoglobulin (Ig) domain-containing molecules. It is known to be widely and exclusively expressed on hematopoietic cells. The SLAMF6 intracellular portion is characterized by two ITSMs that act as binding sites for adaptor molecules such as SAP and EAT-2. SLAMF6 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 26 kDa and the accession number is Q96DU3-1.

CD43 is a large transmembrane protein involved in T cell activation. Previous studies of CD43- - mice in viral models have demonstrated a role for CD43 in Th1 Th2 skewing, activation of Foxp3 Treg, and T cell apoptosis. CD43 (leukosialin) is a large sialoglycoprotein abundantly expressed on the surface of most cells from the hematopoietic lineage. CD43 is directly involved in the contact between cells participating in a series of events such as signaling, adherence and host parasite interactions.

Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface. SEZ6 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 98.8 kDa and the accession number is Q7TSK2.

LOX-1 is a transmembrane glycoprotein that binds to and internalizes ox-LDL.LOX-1 gene deletion in mice and anti-LOX-1 therapy has been shown to decrease inflammation, oxidative stress and atherosclerosis. LOX-1 deletion also results in damage from ischemia, making LOX-1 a promising target of therapy for atherosclerosis and related disorders. In this article we focus on the different mechanisms for regulation, signaling and the various effects of LOX-1 in contributing to atherosclerosis.

CD93 has been shown critical roles in inflammatory and immune diseases. CD93 silencing increased IL-6 and TSLP, but not IL-33 levels in culture supernatants. HDM-induced asthma mice showed significant airway hyperresponsiveness and inflammation with Th2 cytokine activation, along with decreased CD93 expression in bronchial epithelial cells and lung homogenates but increased serum CD93 levels.

SLAMF6 (signaling lymphocyte activation molecule 6) (Ly108 in mice, NTB-A or SF2000 in humans) is a homophilic receptor belonging to the superfamily immunoglobulin (Ig) domain-containing molecules. It is known to be widely and exclusively expressed on hematopoietic cells. The SLAMF6 intracellular portion is characterized by two ITSMs that act as binding sites for adaptor molecules such as SAP and EAT-2. SLAMF6 Protein, Mouse, Recombinant (aa 31-239, His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 24.03 kDa and the accession number is Q9ET39-1.

Cyclin A1 is a member of the highly conserved cyclin family that is characterized by a dramatic periodicity in protein abundance, and belongs to the A-type cyclin subfamily. The mammalian A-type cyclin family consists of two members: cyclin A1 and cyclin A2. Different cyclins exhibit distinct expression. Cyclin A1 is expressed in mice exclusively in the germ cell lineage and high rate of cyclinA1 is found in human testis and certain myeloid leukaemia cells. Cyclin A1 is primarily function in the control of meiosis. It serves as regulator subunits binding to cyclin-dependent kinase 1 (Cdk1) and cyclin-dependent kinase 2 (Cdk2), which give two different kinase activities, one appearing in S phase, the other in G2. Through this, cyclin A1 operate the entry and progression in cell cycle. High frequency of cyclin A1 overexpression has been observed in acute myelocytic leukemias, especially those that are at the promyelocyte and myeloblast stages of development.

The placental anticoagulant protein Annexin A5 (ANXA5) is a multifunctional protein that is highly expressed on the apical surfaces of syncytiotrophoblasts, and plays an important role in haemostatic regulations, maintaining blood fluidity of the placenta. Annexin A5 (ANXA5) is a protein abundantly expressed in normal placenta where it contributes to the healthy outcome of a pregnancy. Lower ANXA5 levels have been observed in M2 ANXA5 haplotype carrying chorion. The association found between the maternal carriage of the M2 ANXA5 haplotype and an elevated risk of IUGR and or PE supports the hypothesis that carrier status of this haplotype and the consequently reduced placental ANXA5 expression might be responsible, at least partially, for the onset of these gestational vascular complications. ANXA5 could be used as a biomarker for the early detection of PE and for the prediction of its severity. ANXA5 as an embryonic anticoagulant that appears deficient in contiguous specter of thrombophilia-related pregnancy complications culminating more frequently in miscarriage in a maternal M2 carrier background. As a potential indicator for malignancy and lymphatic metastasis, ANXA5 overexpression increases in vitro migration and invasion of Hca-P cell, promotes in vivo malignancy, LNM rate and level of Hca-P-transplanted mice. Hereditary thrombophilias can impair vascular placental functions and predispose to the birth of small-for-gestational age (SGA) babies. The placental anticoagulant protein annexin A5 (ANXA5) may contribute to this process. A functional haplotype (M2) within the ANXA5 gene is associated with fetal loss and venous thrombosis.

The metabolites of fatty acyl-Coenzyme A (CoA) and metabolic enzymes contribute to lipid biosynthesis, signal transduction, and gene transcription. Members of the acyl-CoA thioesterase (Acot) gene family hydrolyze fatty acyl-CoAs, but their biological functions remain incompletely understood. Thioesterase superfamily member 2 (Them2; synonym Acot13) is enriched in oxidative tissues, associated with mitochondria, and relatively specific for long chain fatty acyl-CoA substrates. Using Them2(- -) mice, we have demonstrated key roles for Them2 in regulating hepatic glucose and lipid metabolism. Members of the acyl-CoA thioesterase (Acot) gene family catalyze the hydrolysis of fatty acyl-CoAs, but their biological functions remain unknown. Thioesterase superfamily member 2 (Them2; synonym Acot13) is a broadly expressed mitochondria-associated Acot. Them2 was previously identified as an interacting protein of phosphatidylcholine transfer protein (PC-TP).

IDO2 belongs to the indoleamine 2,3-dioxygenase family. Indoleamine 2,3-dioxgyenase (IDO), is a cytosolic haem protein which, together with the hepatic enzyme tryptophan 2,3-dioxygenase, catalyzes the conversion of tryptophan and other indole derivatives to kynurenines. In addition to classic IDO (IDO1), a new variant, IDO2, has recently been described. IDO2 is expressed in the liver, small intestine, spleen, placenta, thymus, lung, brain, kidney, and colon. IDO is widely distributed in human tissues, its physiological role is not fully understood but is of great interest. IDO can be up-regulated via cytokines such as interferon-gamma, and can thereby modulate the levels of tryptophan, which is vital for cell growth. In humans and mice, the IDO1 and IDO2 genes are present tandemly in a tail-to-head arrangement on chromosome 8. In lower vertebrates such as zebrafish and toads, only a single IDO gene may be present that may be more IDO2-like in structure. This closer relationship to IDO2 suggests that IDO2 may be the ancestor of the better characterized IDO1 gene and that IDO1 might have been generated by gene duplication of IDO2 before the origin of tetrapods in mammalian evolutionary history. IDO2 catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism.

SAA4 is a member of the SAA family. SAA proteins are family of apolipoproteins of high density lipoprotein (HDL). They can be separated into two distinct groups. First group (SAA1, SAA2, and SAA3) consists of acute phase reactant whose expression level increase in the blood in a response to trauma, infection, inflammation, and neoplasia. These acute phase SAAs associates with HDL during inflammation and remodel the HDL particle by displacing Apo-A1. The second distinct group consists of SAA4 and SAA5 which exist as the minor apolipoproteins on HDL, but this group of SAA constitutes more than 90% of all the SAA during homeostasis, and it is thought to play a role in the normal functioning of the HDL particle. SAA4 is a constitutively expressed protein which expressed only in humans and mice. It is connected almost completely with lipoproteins of the high density range. The physiological function of SAA4 is unknown, and its serum concentration has no association with those of other major apolipoproteins.

BLBP, also known as FABP7, is a brain fatty acid binding protein. Fatty acid binding proteins (FABPs) are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP7 binds DHA with the highest affinity among all of the FABPs. FABPs may play roles in fatty acid uptake, transport, and metabolism. BLBP is expressed, during development, in radial glia by the activation of notch receptors. It was shown that reelin induces FABP7 expression in neural progenitor cells via notch-1 activation. BLBP variation is linked to weak prepulse inhibition(PPI) in mice and deficit in PPI is an endophenotypic trait observed in schizophrenia patients and their relatives.

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.

Synapse-associated protein 1 (SYAP1), also known as PRO3113 and BSTA, belongs to the synapse-associated BSD domain family, featuring three α-helices and two conserved tryptophan and phenylalanine residues located at the C-terminus. Expressed near neuronal Golgi and synaptic regions of cerebellar Purkinje cells, SYAP1 has been linked to intact sensorimotor control and general vesicular trafficking in neurons. SYAP1-deficient mice display impaired locomotor activity. In cultured adipocytes, SYAP1 facilitates mTORC2-mediated phosphorylation of protein kinase Akt1 and adipocyte differentiation. Chromosomal band Xp22.2 houses the human SYAP1 gene, a region associated with developmental delay and autism spectrum disorder. SYAP 1 may be a target for future cancer therapies as it was induced by tamoxifen in breast cancer cells sensitive to tamoxifen growth inhibition.

Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface. SEZ6 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 98.9 kDa and the accession number is Q53EL9-1.

Lymphocyte cytosolic protein 2（LCP2）contains a SAM domain and a SH2 domain. It is highly expressed in spleen, thymus and peripheral blood leukocytes, T-cell and monocytic cell lines, but expressed at lower level in B-cell lines. LCP2 was originally identified as a substrate of the ZAP-70 protein tyrosine kinase following T cell receptor (TCR) ligation in the leukemic T cell line Jurkat. It is phosphorylated after T-cell receptor activation by ZAP70, ITK and TXK, which leads to the up-regulation of Th1 preferred cytokine IL-2 during post-translational modification. Studies using LCP2-deficient T cell lines or mice have provided strong evidence that SLP-76 plays a positive role in promoting T cell development and activation as well as mast cell and platelet function.

Lysosome membrane protein II (LIMPII)，also known as SCARB2, is a type III multi-pass membrane glycoprotein that is located primarily in limiting membranes of lysosomes and endosomes on all tissues and cell types so far examined. Earlier studies in mice and rat suggested that this protein may participate in membrane transportation and the reorganization of endosomal lysosomal compartment. The protein deficiency in mice was reported to impair cell membrane transport processes and cause pelvic junction obstruction, deafness, and peripheral neuropathy. Further studies in human showed that this protein is identified as a receptor for EV71 (human enterovirus species A, Enterovirus 71) and CVA16 (coxsackievirus A16) which are most frequently associated with hand, foot and mouth disease (HFMD). Mutations in this gene caused an autosomal recessive progressive myoclonic epilepsy-4 (EPM4), also known as action myoclonus-renal failure syndrome (AMRF). Alternatively spliced transcript variants encoding different isoforms have been found for this gene. In addition, LIMPII also has been shown to bind thrombospondin-1, may contribute to the pro-adhesive changes of activated platelets during coagulation, and inflammation.

The type I transmembrane protein 15-leucine-rich repeat containing membrane protein (LRRC15) is a member of the LRR superfamily. The LRR family is a structural module for protein-protein and protein-matrix interactions used for molecular recognition process such as cell adhesion, signal transduction, DNA repair, and RNA processing. The LRRC15 is also a transmembrane protein demonstrated to play important roles in cancer. LRRC15 expression was notably increased 4.6-fold in cariesdiseased pulpal tissue. Remarkably, LRRC15 was relatively abundant in mineralized tissues. That LRRC15 was significantly induced after osteogenic differentiation, while in the MSCs from bone marrow of ovariectomized mice the expression of LRRC15 was remarkably decreased and LRRC15 regulated osteogenic differentiation in a p65-dependent manner.