目录号 | 产品详情 | 靶点 | |
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T41175 | |||
OB 24 hydrochloride is a potent and selective heme oxygenase 1 (HO-1) inhibitor (IC50 values are 1.9 and >100 μM for HO-1 and HO-2 respectively), reduces protein carbonylation and reactive oxygen species formation in advanced prostate cancer cells (PCA). Inhibits cell proliferationin vitroand PCA tumor growth and lymph node/lung metastasesin vivo. Synergizes with Taxol. | |||
T68288 | |||
OB-24 free base is a potent and selective heme oxygenase 1 (HO-1) inhibitor. | |||
T28223 | |||
OB-1 is an inhibitor of stomatin-like protein-3 (STOML3) oligomerization. OB-1 reversibly reduces the sensitivity of mechanically gated currents in sensory neurons and silence mechanoreceptors in vivo. | |||
T28224 | |||
OB-2 is an inhibitor of stomatin-like protein-3 (STOML3) oligomerization. OB-2 reversibly reduces the sensitivity of mechanically gated currents in sensory neurons and silence mechanoreceptors in vivo. | |||
T9266 | Lipid Fatty Acid Synthase | ||
Fatostatin A 是一种SREBP 活化的特异性抑制剂,能够抑制 SREBP-1 和 SREBP-2 的活化。它与 SCAP (SREBP 裂解激活蛋白) 结合,抑制 SREBPs 的 ER-Golgi 易位。它具有抗肿瘤活性,能抑制ob/ob 小鼠的高血糖。它抑制细胞中成脂基因的转录。 | |||
T6832 | NPC1L1 Fatty Acid Synthase | ||
Fatostatin hydrobromide (Fatostatin A HBr) 是一种 SREBP 活化的特异性抑制剂,可抑制 SREBP-1 和 SREBP-2 的活化。它与 SCAP (SREBP 裂解激活蛋白) 结合,抑制 SREBPs 的 ER-Golgi 易位。它具有抗肿瘤作用,能抑制 ob/ob 小鼠的高血糖。它抑制了细胞中成脂基因的转录。 | |||
T31752 | |||
FD&C Yellow No. 4 is a dye. | |||
T71294 | |||
BMS-763534 is a potent antagonist of corticotropin-releasing factor/hormone receptor 1 (CRHR-1). | |||
T81628 | |||
OB3, 相比于Leptin,在降低小鼠模型的肥胖和糖尿病方面显示出更高效。此化合物能够降低肝癌细胞内瘦素相关的炎症及其增殖作用。 | |||
T72906 | |||
[D-Leu-4]-OB3 抑制促炎、增殖和转移基因的表达以及 PD-L1的表达。[D-Leu-4]-OB3 刺激促凋亡基因的表达。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-00875 | Leptin Protein, Human, Recombinant | Human | E. coli | ||
Leptin is one of the most important hormones secreted by adipocytes, as an adipokine that modulates multiple functions including energy homeostasis, thermoregulation, bone metabolism, endocrine, and pro-inflammatory immune responses. The circulating leptin levels serve as a gauge of energy stores, thereby directing the regulation of energy homeostasis, neuroendocrine function, and metabolism. Recent studies suggest that leptin is physiologically more important as an indicator of energy deficiency, rather than energy excess, and may mediate adaptation by driving increased food intake and directing neuroendocrine function to converse energy, such as inducing hypothalamic hypogonadism to prevent fertilization. One of these functions is the connection between nutritional status and immune competence. The adipocyte-derived hormone Leptin has been shown to regulate the immune response, innate, and adaptive response, both in normal and pathological conditions. Thus, Leptin is a mediator of the inflammatory response. Leptin has a dual effect on bone, acting by two independent mechanisms. As a signal molecule with growth factor characteristics, leptin can stimulate osteoblastic cells and inhibit osteoclast formation and activity, thus promoting osteogenesis. However, as a molecule that stimulates sympathetic neurons in the hypothalamus, leptin indirectly inhibits bone formation. This inhibitory effect of leptin mediated by activation of the sympathetic nervous system can be abrogated by the application of blood pressure-reducing beta-blockers, which also inhibit receptors of hypothalamic adrenergic neurons. Leptin appears to regulate some features defining Alzheimer's disease (AD) at the molecular and physiological level. Leptin can stimulate mitogenic and angiogenic processes in peripheral organs. Because leptin levels are elevated in obese individuals and excess body weight has been shown to increase breast cancer risk in postmenopausal women. Furthermore, a recent report clearly shows that targeting leptin signaling may reduce mammary carcinogenesis.
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TMPY-01725 | Leptin Receptor Protein, Human, Recombinant (His) | Human | HEK293 | ||
Leptin Receptor or CD295 belongs to the gp130 family of cytokine receptors that are known to stimulate gene transcription via activation of cytosolic STAT proteins. This protein is a receptor for leptin (an adipocyte-specific hormone that regulates body weight) and is involved in the regulation of fat metabolism, as well as in a novel hematopoietic pathway that is required for normal lymphopoiesis. Leptin Receptor/CD295 is transmembrane catalytic receptors found on NPY/AgRP and alpha-MSH/CART neurons in hypothalamic nuclei. Leptin receptors (Ob-Rs) are coded for by one human gene that produces six different isoforms; Ob-Ra - Ob-Rf. Ob-Rs exist as constitutive dimers at physiological expression levels. Only the Ob-Rb isoform can transduce intracellular signals and does so through activation of the JAK2/STAT3, PI 3-K, and MAPK signaling cascades. Activation of Ob-Rs mediates transcriptional regulation of the hypothalamic melanocortin pathway and downregulates endocannabinoid expression. Leptin acts via leptin receptors. Leptin resistance has been proposed as a pathophysiological mechanism of obesity. In obese individuals, Ob-Ra (which is involved in the active transport of leptin across the blood-brain barrier) expression is downregulated and the individual may be unresponsive to leptin signals. Ob-R antagonists are of great interest in the development of pharmacological treatments for obesity. Mutations in the Leptin Receptor/CD295 have been associated with obesity and pituitary dysfunction.
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TMPY-06375 | Leptin Protein, Mouse, Recombinant (mFc) | Mouse | HEK293 | ||
Leptin is one of the most important hormones secreted by adipocytes, as an adipokine that modulates multiple functions including energy homeostasis, thermoregulation, bone metabolism, endocrine, and pro-inflammatory immune responses. The circulating leptin levels serve as a gauge of energy stores, thereby directing the regulation of energy homeostasis, neuroendocrine function, and metabolism. Recent studies suggest that leptin is physiologically more important as an indicator of energy deficiency, rather than energy excess, and may mediate adaptation by driving increased food intake and directing neuroendocrine function to converse energy, such as inducing hypothalamic hypogonadism to prevent fertilization. One of these functions is the connection between nutritional status and immune competence. The adipocyte-derived hormone Leptin has been shown to regulate the immune response, innate, and adaptive response, both in normal and pathological conditions. Thus, Leptin is a mediator of the inflammatory response. Leptin has a dual effect on bone, acting by two independent mechanisms. As a signal molecule with growth factor characteristics, leptin can stimulate osteoblastic cells and inhibit osteoclast formation and activity, thus promoting osteogenesis. However, as a molecule that stimulates sympathetic neurons in the hypothalamus, leptin indirectly inhibits bone formation. This inhibitory effect of leptin mediated by activation of the sympathetic nervous system can be abrogated by the application of blood pressure-reducing beta-blockers, which also inhibit receptors of hypothalamic adrenergic neurons. Leptin appears to regulate some features defining Alzheimer's disease (AD) at the molecular and physiological level. Leptin can stimulate mitogenic and angiogenic processes in peripheral organs. Because leptin levels are elevated in obese individuals and excess body weight has been shown to increase breast cancer risk in postmenopausal women. Furthermore, a recent report clearly shows that targeting leptin signaling may reduce mammary carcinogenesis.
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TMPJ-00975 | LEPR Protein, Mouse, Recombinant (hFc) | Mouse | Human Cells | ||
The Leptin receptor is a member of the Class I cytokine receptor family. It mediates the activities of Leptin, a multi-functional hormone produced primarily by adipose tissues that plays roles in food intake, energy metabolism, angiogenesis, reproduction, hematopoiesis, bone metabolism, and immune function. The human Leptin R gene encodes 1165 amino acids (aa) including a signal peptide, an extracellular region with cytokine receptor homology (CRH), multiple fibronectin type III domains and a WSXWS motif, a transmembrane domain, and a cytoplasmic domain that supports JAK/STAT signaling. Soluble Leptin R is the primary Leptin-binding protein in blood, where it maintains a pool of available bioactive Leptin, delays Leptin clearance from circulation, and down-regulates blood-brain transmission of Leptin. In humans, soluble Leptin R levels are inversely proportional to adiposity and are elevated in females versus males. Soluble Leptin R is also found up-regulated in patients with chronic heart failure, end-stage renal disease, and anorexia.It is expressed by tumor-initiating stem cells, and is proposed as a link between cancer and obesity.
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TMPJ-00977 | LEPR Protein, Mouse, Recombinant (mFc) | Mouse | Human Cells | ||
The Leptin receptor is a member of the Class I cytokine receptor family. It mediates the activities of Leptin, a multi-functional hormone produced primarily by adipose tissues that plays roles in food intake, energy metabolism, angiogenesis, reproduction, hematopoiesis, bone metabolism, and immune function. The human Leptin R gene encodes 1165 amino acids (aa) including a signal peptide, an extracellular region with cytokine receptor homology (CRH), multiple fibronectin type III domains and a WSXWS motif, a transmembrane domain, and a cytoplasmic domain that supports JAK/STAT signaling. Soluble Leptin R is the primary Leptin-binding protein in blood, where it maintains a pool of available bioactive Leptin, delays Leptin clearance from circulation, and down-regulates blood-brain transmission of Leptin. In humans, soluble Leptin R levels are inversely proportional to adiposity and are elevated in females versus males. Soluble Leptin R is also found up-regulated in patients with chronic heart failure, end-stage renal disease, and anorexia.It is expressed by tumor-initiating stem cells, and is proposed as a link between cancer and obesity.
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TMPJ-00052 | Leptin Protein, Mouse, Recombinant | Mouse | E. coli | ||
Leptin is a hormone secreted from white adipocytes and plays important role in the regulation of food intake and energy balance. Leptin functions via signaling pathways involving OB-R in hypothalamus. Animal models have revealed the influence of Leptin in reducing body weight and regulating blood glucose level. When mutations are introduced in obese gene, mice with impaired function of leptin are massively obese and in high risk of diabetes. Leptin deficiency reduces metablic rate. Leptin deficient mice are less active and with lower body temperature than normal animals. Human Leptin shares approximately 84% sequence identity with the mouse protein. Human Leptin consists of 167 amino acid residue including a 21 amino acid residue signal sequence and 146 amino acid residue mature protein sequence.
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TMPK-00587 | CDH11 Protein, Human, Recombinant (aa 54-617, His) | Human | HEK293 | ||
CDH11 belongs to a group of transmembrane proteins that are principally located in adherens junctions. CDH11 mediates homophilic cell-to-cell adhesion, which may promote the development of cirrhosis. CDH11 expression was positively correlated with liver fibrosis in patients with cirrhosis, and could therefore be a prognostic factor in patients with liver fibrosis.
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TMPJ-00411 | LEPR Protein, Human, Recombinant (hFc) | Human | Human Cells | ||
The Leptin receptor is a member of the Class I cytokine receptor family. It mediates the activities of Leptin, a multi-functional hormone produced primarily by adipose tissues that plays roles in food intake, energy metabolism, angiogenesis, reproduction, hematopoiesis, bone metabolism, and immune function. The human Leptin R gene encodes 1165 amino acids (aa) including a signal peptide, an extracellular region with cytokine receptor homology (CRH), multiple fibronectin type III domains and a WSXWS motif, a transmembrane domain, and a cytoplasmic domain that supports JAK/STAT signaling. Soluble Leptin R is the primary Leptin-binding protein in blood, where it maintains a pool of available bioactive Leptin, delays Leptin clearance from circulation, and down-regulates blood-brain transmission of Leptin. In humans, soluble Leptin R levels are inversely proportional to adiposity and are elevated in females versus males. Soluble Leptin R is also found up-regulated in patients with chronic heart failure, end-stage renal disease, and anorexia.It is expressed by tumor-initiating stem cells, and is proposed as a link between cancer and obesity.
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TMPJ-00976 | LEPR Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
The Leptin receptor is a member of the Class I cytokine receptor family. It mediates the activities of Leptin, a multi-functional hormone produced primarily by adipose tissues that plays roles in food intake, energy metabolism, angiogenesis, reproduction, hematopoiesis, bone metabolism, and immune function. The human Leptin R gene encodes 1165 amino acids (aa) including a signal peptide, an extracellular region with cytokine receptor homology (CRH), multiple fibronectin type III domains and a WSXWS motif, a transmembrane domain, and a cytoplasmic domain that supports JAK/STAT signaling. Soluble Leptin R is the primary Leptin-binding protein in blood, where it maintains a pool of available bioactive Leptin, delays Leptin clearance from circulation, and down-regulates blood-brain transmission of Leptin. In humans, soluble Leptin R levels are inversely proportional to adiposity and are elevated in females versus males. Soluble Leptin R is also found up-regulated in patients with chronic heart failure, end-stage renal disease, and anorexia.It is expressed by tumor-initiating stem cells, and is proposed as a link between cancer and obesity.
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TMPJ-00606 | Leptin Protein, Carassius auratus, Recombinant (His) | Carassius auratus | Yeast | ||
Leptin is a hormone secreted from white adipocytes and plays important role in the regulation of food intake and energy balance. Leptin functions via signaling pathways involving OB-R in hypothalamus. In mammals, leptin is mainly produced by the adipose tissue and encodes body fat reserves, acting as a short-term satiety signal. In fish, the presence of a leptin-like peptide was first evidenced by immuno-cross-reactivity, and its existence was certainly demonstrated after the finding by synteny of a leptin sequence in the pufferfish.
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TMPJ-01267 | CDH11 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Cadherin-11 is a type II classical cadherin member of the cadherin superfamily of integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Cadherins interact with themselves in a homophilic manner in connecting cells, and thus contribute to the sorting of heterogeneous cell types. Cadherin-11 contains five cadherin domains and is mainly expressed in the brain. Mature cadherin proteins consists of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small highly conserved C-terminal cytoplasmic domain. It is shown that Cadherin-11 is a viable molecular target for therapeutic intervention in Glioblastoma multiforme.
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TMPK-00050 | Leptin Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Leptin has key roles in the regulation of energy balance, body weight, metabolism, and endocrine function. Leptin levels are undetectable or very low in patients with lipodystrophy, hypothalamic amenorrhea, and congenital leptin deficiency (CLD) due to mutations in the leptin gene.
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TMPY-00874 | Leptin Receptor Protein, Human, Recombinant (His & hFc) | Human | HEK293 | ||
Leptin Receptor or CD295 belongs to the gp130 family of cytokine receptors that are known to stimulate gene transcription via activation of cytosolic STAT proteins. This protein is a receptor for leptin (an adipocyte-specific hormone that regulates body weight) and is involved in the regulation of fat metabolism, as well as in a novel hematopoietic pathway that is required for normal lymphopoiesis. Leptin Receptor/CD295 is transmembrane catalytic receptors found on NPY/AgRP and alpha-MSH/CART neurons in hypothalamic nuclei. Leptin receptors (Ob-Rs) are coded for by one human gene that produces six different isoforms; Ob-Ra - Ob-Rf. Ob-Rs exist as constitutive dimers at physiological expression levels. Only the Ob-Rb isoform can transduce intracellular signals and does so through activation of the JAK2/STAT3, PI 3-K, and MAPK signaling cascades. Activation of Ob-Rs mediates transcriptional regulation of the hypothalamic melanocortin pathway and downregulates endocannabinoid expression. Leptin acts via leptin receptors. Leptin resistance has been proposed as a pathophysiological mechanism of obesity. In obese individuals, Ob-Ra (which is involved in the active transport of leptin across the blood-brain barrier) expression is downregulated and the individual may be unresponsive to leptin signals. Ob-R antagonists are of great interest in the development of pharmacological treatments for obesity. Mutations in the Leptin Receptor/CD295 have been associated with obesity and pituitary dysfunction.
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TMPK-00719 | Siglec-5 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Siglecs (sialic acid binding Ig-like lectins) are I-type (Ig-type) 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. Siglec 5 is putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
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TMPK-00718 | Siglec-5 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Siglecs (sialic acid binding Ig-like lectins) are I-type (Ig-type) 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. Siglec 5 is putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
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TMPK-00720 | Siglec-5 Protein (Primary Amine Labeling), Human, Recombinant (hFc), Biotinylated | Human | HEK293 | ||
Group B Streptococcus (GBS) causes invasive infections in human newborns. the GBS β-protein attenuates innate immune responses by binding to sialic acid-binding immunoglobulin-like lectin 5 (Siglec-5), an inhibitory receptor on phagocytes.the polymorphism could influence the risk of prematurity among human fetuses of mothers colonized with GBS. This first functionally proven example of a paired receptor system in the Siglec family has multiple implications for regulation of host immunity.
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TMPK-00729 | Siglec-6 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Siglecs (Sialic acid binding Ig-like Lectins) are I-type (Ig-type) lectins that belong 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.Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
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TMPY-03549 | Siglec-5 Protein, Human, Recombinant | Human | HEK293 | ||
SIGLEC5 contains 2 Ig-like C2-type (immunoglobulin-like) domains and 1 Ig-like V-type (immunoglobulin-like) domain. It belongs to the immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. SIGLEC5 is expressed by monocytic/myeloid lineage cells. It is found at high levels in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. It is also expressed by monocytes and neutrophils but absent from leukemic cell lines representing early stages of myelomonocytic differentiation. SIGLEC5 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
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TMPY-02884 | Siglec-5 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
SIGLEC5 contains 2 Ig-like C2-type (immunoglobulin-like) domains and 1 Ig-like V-type (immunoglobulin-like) domain. It belongs to the immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. SIGLEC5 is expressed by monocytic/myeloid lineage cells. It is found at high levels in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. It is also expressed by monocytes and neutrophils but absent from leukemic cell lines representing early stages of myelomonocytic differentiation. SIGLEC5 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
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TMPJ-00669 | Siglec-5 Protein, Human, Recombinant (His & Flag & hFc) | Human | Human Cells | ||
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.
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TMPJ-00516 | OBhFc1 Protein, Human, Recombinant (His) | Human | E. coli | ||
CST Complex Subunit STN1 (OBFC1) is a 368 amino acid protein that contains one OB DNA-binding domain. It is a member of the STN1 family. OBFC1 is component of the CST complex, a complex that binds to single-stranded DNA and is required to protect telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. In addition to telomere protection, the CST complex has probably a more general role in DNA metabolism at non-telomeric sites.
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