目录号 | 产品详情 | 靶点 | |
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T19596 | Others | ||
UDP-GlcNAc Disodium Salt (UDP-α-D-N-Acetylglucosamine Disodium Salt) 是一种 O-GlcNAc 转移酶 (OGT) 的供体底物。 | |||
T9190 | Others | ||
NAG-thiazoline (GlcNAc-thiazoline) 是一种 O-GlcNAcase 抑制剂,Ki 值为 180 nM。它对 V. campbellii 有效,MIC 值为 0.5 µM。 | |||
T38713 | |||
Fmoc-L-Asn(beta-D-GlcNAc(Ac)3)-OH, also known as Fmoc-Asn(Ac3AcNH-beta-Glc)-OH, is a chemical compound used in the synthesis of silicon-fluoride acceptor (SiFA) derivatized octreotate derivatives. SiFA-octreotate analogues, which serve as tumor imaging agents, are valuable tools for positron emission tomography (PET) research. | |||
T37575 | Others | ||
GLcNAc1-b-PNP 是N-乙酰基-β-氨基葡萄糖酶的发色底物,可用于量化人血清和尿液中N-乙酰基-β-D-氨基葡萄糖酶的活性。 | |||
T4514 | Endogenous Metabolite | ||
N-Acetyl-D-Glucosamine (NAG) 是葡萄糖的单糖衍生物。 | |||
T83131 | |||
AMC-GlcNAc (compound 1) 作为一款高效荧光探针,主要用于β-己糖胺酶活性的检测与表征。该探针能在连续监测中开启荧光,并且在宽广pH值范围内维持稳定的荧光信号(Ex=325 nm, Em=390 nm)。AMC-GlcNAc还支持高灵敏度与低背景信号的比率荧光检测,适用于筛选大肠杆菌细胞裂解物中重组分散素B的活性。 | |||
T16409 | Others Acyltransferase | ||
OSMI-1 是一种 O-GlcNAc 转移酶 (OGT) 抑制剂 (IC50=2.7 μM),具有口服活性和细胞渗透性。OSMI-1 可以抑制蛋白质 O-GlcNA 酰化,而不会定性地改变细胞表面 N- 或 O- 连接的聚糖。 | |||
T75405 | |||
GlcNAc kinase (EcNagK) (N-Acetylglucosamine kinase) 为GlcNAc代谢过程中的关键酶。通过将ATP的γ-磷酰基转移到GlcNAc的C-6位羟基,生成GlcNAc-6-P。 | |||
T75399 | |||
GlcNAc 1-P uridyltransferase (CjGlmU) 为一种糖核苷酸转移酶,以UTP和GlcNAc-1-P为天然底物,负责合成UDP-GlcNAc。此酶展现出潜在的抗菌活性分子研究价值。 | |||
T80020 | Endogenous Metabolite | ||
UDP-3-O-acyl-GlcNAc diammonium 是一种E. coli代谢产物,涉及3-deoxy-D-manno-octulosonate (KDO) 生物合成途径。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPJ-00687 | B4GALT4 Protein, Human, Recombinant (His) | Human | Human Cells | ||
β-1,4-galactosyltransferase 4 (B4GALT4) is a single-pass type II membrane protein that belongs to the Glycosyltransferase 7 family. B4GALT4 consist of the following 2 domains: N-Acetyllactosamine Synthase and β-N-Acetylglucosaminyl-Glycolipid β-1,4-Galactosyltransferase. B4GALT4 is highly expressed in the heart, placenta, kidney, and pancreas; it is lowly expressed in the brain, colon, lung, muscle, ovary, testis, and uterus. B4GALT4 function is responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
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TMPY-04486 | CHST5 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
CHST5 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 with hFc tag. The predicted molecular weight is 70.1 kDa. Accession number: Q9QUP4
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TMPJ-01092 | MGAT2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Mannoside Acetylglucosaminyltransferase 2 (MGAT2) is a single-pass type II membrane protein that contains the typical glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain and a C-terminal catalytic domain. MGAT2 catalyzes an essential step in the conversion of oligo-mannose to complex N-glycans. Defects in MGAT2 are the cause of congenital disorder of glycosylation type 2A.
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TMPH-00009 | OGT Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Probably by glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex. Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2. O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity. Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1. Glycosylates HOXA1. O-glycosylates FNIP1.; the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.
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TMPH-02294 | UAP1 Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P.
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TMPH-01339 | Ficolin 3/FCN3 Protein, Human, Recombinant (His) | Human | E. coli | ||
May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and lipopolysaccharides from S.typhimurium and S.minnesota.
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TMPH-01361 | GAL3ST3 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Transfers a sulfate to position 3 of non-reducing beta-galactosyl residues in N-glycans and core2-branched O-glycans. Has high activity towards Gal-beta-1,4-GlcNAc, Gal-beta-1,4(Fuc-alpha-1,3)GlcNAc and lower activity towards Gal-beta-1,3(Fuc-alpha-1,4)GlcNAc.
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TMPH-02295 | UAP1 Protein, Human, Recombinant (His) | Human | Yeast | ||
Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P.
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TMPH-00590 | GlmU Protein, E. coli, Recombinant (His & Myc) | E. coli | E. coli | ||
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
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TMPH-03438 | CHS1 Protein, S. cerevisiae, Recombinant (His) | Saccharomyces cerevisiae | E. coli | ||
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer. Required for mitotic division septum formation during adverse conditions.
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TMPH-02610 | CLEC4G Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Binds mannose, N-acetylglucosamine (GlcNAc) and fucose, but not galactose, in a Ca(2+)-dependent manner.
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TMPH-02539 | MGAT3 Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains, called bisecting N-acetylglucosamine (GlcNAc). It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. The addition of this bisecting GlcNAc residue alters not only the composition, but also the conformation of the N-glycan. The introduction of the bisecting GlcNAc residue results in the suppression of further processing and elongation of N-glycans, precluding the formation of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is unable to use the bisected oligosaccharide as a substrate. Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location. Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation. In brain, addition of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal targeting in response to oxidative stress and further degradation which increases its location to early endosome and the APP cleavage.
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TMPH-02292 | B3GNT7 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
N-acetyl glucosamine (GlcNAc) transferase that catalyzes the transfer of GlcNAc via a beta1->3 linkage from UDP-GlcNAc to the non-reducing terminal galactose (Gal) in the linearly growing chain of N- and O-linked keratan sulfate proteoglycans. Cooperates with B4GALT4 galactosyltransferase and CHST6 and CHST1 sulfotransferases to construct and elongate mono- and disulfated disaccharide units [->3Galbeta1->4(6-sulfoGlcNAcbeta)1->] and [->3(6-sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer. Involved in biosynthesis of N-linked keratan sulfate proteoglycans in cornea, with an impact on proteoglycan fibril organization and corneal transparency. May play a role in the maintenance of tissue architecture by suppressing cellular motility and invasion.
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TMPH-01007 | NDST1 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Compared to other NDST enzymes, its presence is absolutely required. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response. Required for the exosomal release of SDCBP, CD63 and syndecan.
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TMPH-03714 | HAS1 Protein, Xenopus tropicalis, Recombinant (His & Myc) | Xenopus tropicalis | E. coli | ||
Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. Also able to catalyze the synthesis of chito-oligosaccharide depending on the substrate.
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TMPY-03262 | B3GNT6 Protein, Human, Recombinant (aa 44-384, His) | Human | Baculovirus-Insect Cells | ||
B3GNT6 belongs to the glycosyltransferase 31 family. B3GNT6 play s an important role in the synthesis of mucin-type O-glycans in digestive organs. It catalyzes the transfer of GlcNAc from UDP-GlcNAc to GalNAcalpha1-Ser/Thr (Tn antigen) to form the core 3 structure (GlcNAcbeta1-3GalNAcalpha1-Ser/Thr). Core 3 structure exists in O-glycan which is an important precursor in the biosynthesis of mucin-type glycoproteins. Loss of core 3 could lead to the production of secreted mucins, then bacteria would be inefficiently cleared from the system, and chronic inflammation would be developed, which eventually would result in development of cancer. B3GNT6 gene is a tumor suppressor gene.
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TMPJ-01202 | LYG2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Lysozyme G-Like Protein 2 (LYG2) is a secreted protein that belongs to the glycosyl hydrolase 23 family. LYG2 contains one SLT domain, one protein domain present in bacterial lytic transglycosylase (SLT) and in eukaryotic lysozymes (GEWL). SLT domain catalyzes the cleavage of the β-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyglucosamine (GlcNAc). LYG2 has hydrolase activity which acting on glycosyl bonds, and possess lysozyme activity.
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TMPH-02501 | FUT7 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization. In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors. However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc. Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion. Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation. May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium. May affect insulin signaling by upregulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit.
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TMPY-03663 | FUT8 Protein, Hamster, Recombinant (aa 68-575, His) | Hamster | Baculovirus-Insect Cells | ||
Alpha (1,6) fucosyltransferase 8, also known as FUT8, is a member of the glycosyltransferase family. Fucosyltransferases are the enzymes transferring fucose from GDP-Fuc to Gal in an alpha1,2-linkage and to GlcNAc in alpha1,3-linkage, alpha1,4-linkage, or alpha1,6-linkage. All fucosyltransferases utilize the same nucleotide sugar, their specificity reside in the recognition of the acceptor and in the type of linkage formed. Fucosyltransferases share some common structural and catalytic features. On the basis of protein sequence similarities, these enzymes can be classified into four distinct families: (1) the alpha-2-fucosyltransferases, (2) the alpha-3-fucosyltransferases, (3) the mammalian alpha-6-fucosyltransferases, and (4) the bacterial alpha-6-fucosyltransferases. The alpha-3-fucosyltransferases constitute a distinct family as they lack the consensus peptide, but some regions display similarities with the alpha-2 and alpha-6-fucosyltranferases.
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TMPJ-01317 | EXTL2 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
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.
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TMPY-02546 | FUT8 Protein, Human, Recombinant (aa 68-575, His) | Human | Baculovirus-Insect Cells | ||
Alpha (1,6) fucosyltransferase 8, also known as FUT8, is a member of the glycosyltransferase family. Fucosyltransferases are the enzymes transferring fucose from GDP-Fuc to Gal in an alpha1,2-linkage and to GlcNAc in alpha1,3-linkage, alpha1,4-linkage, or alpha1,6-linkage. All fucosyltransferases utilize the same nucleotide sugar, their specificity reside in the recognition of the acceptor and in the type of linkage formed. Fucosyltransferases share some common structural and catalytic features. On the basis of protein sequence similarities, these enzymes can be classified into four distinct families: (1) the alpha-2-fucosyltransferases, (2) the alpha-3-fucosyltransferases, (3) the mammalian alpha-6-fucosyltransferases, and (4) the bacterial alpha-6-fucosyltransferases. The alpha-3-fucosyltransferases constitute a distinct family as they lack the consensus peptide, but some regions display similarities with the alpha-2 and alpha-6-fucosyltranferases.
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TMPY-02727 | METAP2 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
METAP2 (Methionine aminopeptidase 2), also known as MAP2 is a protein that belongs to the peptidase M24A family. MAP2 binds 2 cobalt or manganese ions and contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. It is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. The catalytic activity of human MAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. This protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amino-terminal methionine residue from nascent protein. MAP2 protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. It also plays a critical role in the regulation of protein synthesis.
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TMPY-00018 | METAP2 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
METAP2 (Methionine aminopeptidase 2), also known as MAP2 is a protein that belongs to the peptidase M24A family. MAP2 binds 2 cobalt or manganese ions and contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. It is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. The catalytic activity of human MAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. This protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amino-terminal methionine residue from nascent protein. MAP2 protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. It also plays a critical role in the regulation of protein synthesis.
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TMPY-01852 | CHST3 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Carbohydrate sulfotransferase 3, also known as Chondroitin 6-O-sulfotransferase 1, Chondroitin 6-sulfotransferase and CHST3, is a single-pass type II membrane protein which belongs to thesulfotransferase 1 family and Gal / GlcNAc / GalNAc subfamily. CHST3 is widely expressed in adult tissues. It is expressed in heart, placenta, skeletal muscle and pancreas. CHST3 is also expressed in various immune tissues such as spleen, lymph node, thymus and appendix. CHST3 catalyzes the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. It is a chondroitin sulfate which constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. It can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. It may play a role in the maintenance of naive T-lymphocytes in the spleen. Defects in CHST3 are the cause of spondyloepiphyseal dysplasia Omani type (SED Omani type) which is an autosomal recessive disorder characterized by normal length at birth but severely reduced adult height (11-13 cm), severe progressive kyphoscoliosis, arthritic changes with joint dislocations, genu valgum, cubitus valgus, mild brachydactyly, camptodactyly, microdontia and normal intelligence. As a consequence of the arthropathy and the contractures, affected individuals develop restricted joint movement. Defects in CHST3 are also a cause of humerospinal dysostosis (HSD) which is characterized by bifurcation of the ends of the humerus, subluxation in the elbow joints, widened iliac bones, talipes equinovarus and coronal cleft vertebrae. Congenital, progressive heart disease, possibly with fatal outcome, is observed in some patients.
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