目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T12316 | Others | ||
Oral antiplatelet agent 1 is a potent antiplatelet agent with an IC50 of 2.94 μM in vitro. | |||
T19858 | DHFR Antibacterial | ||
Brodimoprim 是甲氧苄啶的一种类似物,是口服有效的二氢叶酸还原酶抑制剂,对广谱革兰氏阴性和革兰氏阳性细菌具有高度的抑制作用。 | |||
T9680 | Antibacterial | ||
Irloxacin 是一种口服活性的喹诺酮类抗菌剂,在酸性条件下具有更强大的活性。在体外,Irloxacin 对革兰氏阳性菌和革兰氏阴性菌都具有良好的抗菌谱。 | |||
T22341 | Others | ||
GSK 114 是口服有活性的、高选择性的TNNI3K 抑制剂 (IC50= 25 nM)。其中TNNI3K (又称 CARK) 是酪氨酸样激酶家族的成员,选择性在心脏组织中表达。它对 TNNI3K 的选择性是 B-Raf 激酶的 40 倍 (IC50= 1 µM)。 | |||
T31976 | Others | ||
Glymidine sodium 是口服有活性的抗糖尿病药物,也是肝脂肪分解的抑制剂。它通过抑制葡萄糖的形成,也对由于内源性脂质动员抑制而导致的丙酮酸氧化升高具有抑制作用。 | |||
T20525 | Antibacterial Antibiotic | ||
Chloramphenicol palmitate 是一种广谱抗生素,对革兰氏阳性和革兰氏阴性细菌具有活性。 Chloramphenicol palmitate 可用于在含有氯霉素抗性基因的转化细胞中作为细菌选择剂的研究。 | |||
T5477 | Parasite | ||
ELQ-300 是一种有口服生物活性的抗疟疾剂,可作为细胞色素 bc1 复合物的还原位点的抑制剂 | |||
T9452 | GPR | ||
PW0787 是一种可透过血脑屏障的,口服具有活性的GPR52选择性激动剂 (EC50=135 nM)。它能够抑制精神刺激行为。 | |||
T16777 | Apoptosis Autophagy | ||
ROC-325 是一种有效的口服活性自噬抑制剂,具有抗癌活性。 ROC-325 诱导肾细胞癌凋亡并表现出良好的特异性。 | |||
T7436 | FXR Autophagy | ||
Cilofexor 是一种法尼醇 X 受体激动剂,EC50为 43 nM。它抑制合成肽的结合,具有抗炎和抗纤维化作用。它可用于原发性硬化性胆管炎和非酒精性脂肪性肝炎的研究。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPY-05081 | Notch 1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
NOTCH1 is one of the four mammalian Notch receptors, which is involved in the Notch signaling pathway. Specifically, NOTCH1 promotes the proliferation of myogenic precursor cells, and the NICD domain of NOTCH1 can impair the regeneration of skeletal muscles.NOTCH1 is a prevalent signaling pathway in T cell acute lymphoblastic leukemia (T-ALL). The NOTCH signaling pathway is a conserved signaling cascade that regulates many aspects of development and homeostasis in multiple organ systems. The proto-oncogene NOTCH1 is frequently mutated in around 10% of patients with chronic lymphocytic leukemia (CLL). NOTCH1 mutations in oral squamous cell carcinoma (OSCC) frequently occur near the ligand-binding region. These mutations change the domain structure of this protein and affect the ligand-binding activity. When NOTCH1 is activated by ligand binding, the NOTCH1 intracellular domain (NICD) is cleaved from the cell membrane.
|
|||||
TMPY-02785 | Tetranectin Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Tetranectin (TN), also known as C-type lectin domain family 3, member B (CLEC3B) is a member of the C-type lectin Family. It is plasminogen kringle 4 binding protein and regulates fibrinolysis and proteolytic processes via binding to plasminogen. Tetranectin has been suggested to play a role in tissue remodeling, due to its ability to stimulate plasminogen activation and its expression in developing tissues such as developing bone and muscle. Tetranectin enhances plasminogen activation by a tissue-type plasminogen activator so that it has been suggested to play a role in tissue remodeling. Tetranectin may play a role in the wound healing process. Tetranectin may play a role in neurological diseases and may serve as a diagnostic aid in multiple sclerosis (MS). Tetranectin was found significantly under-expressed in both serum and saliva of metastatic oral squamous cell carcinoma (OSCC) compared to primary OSCC. Tetranectin is thought to enhance proteolytic processes enabling tumor cells to invade and metastasize.
|
|||||
TMPY-01061 | FGF-10 Protein, Human, Recombinant | Human | E. coli | ||
Fibroblast growth factor 10 (FGF10) is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7. FGF10 plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. FGF10 is required for normal branching morphogenesis. It may play a role in wound healing. Defects in FGF10 are the cause of autosomal dominant aplasia of lacrimal and salivary glands (ALSG). ALSG has variable expressivity, and affected individuals may have aplasia or hypoplasia of the lacrimal, parotid, submandibular and sublingual glands and absence of the lacrimal puncta. The disorder is characterized by irritable eyes, recurrent eye infections, epiphora (constant tearing) and xerostomia (dryness of the mouth), which increases the risk of dental erosion, dental caries, periodontal disease and oral infections.
|
|||||
TMPY-01882 | HE4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
WAP four-disulfide core domain protein 2, also known as Epididymal secretory protein E4, Major epididymis-specific protein E4, Putative protease inhibitor WAP5, WFDC2 and HE4, is a secreted protein that contains two WAP domains. WFDC2 / HE4 is a member of a family of stable 4-disulfide core proteins that are secreted at high levels. It is expressed in a number of normal tissues, including male reproductive system, regions of the respiratory tract and nasopharynx. It is highly expressed in a number of tumors cells lines, such ovarian, colon, breast, lung and renal cells lines. Initially described as being exclusively transcribed in the epididymis. WFDC2 may be a component of the innate immune defences of the lung, nasal and oral cavities and suggest that WFDC2 functions in concert with related WAP domain containing proteins in epithelial host defence. WFDC2 re-expression in lung carcinomas may prove to be associated with tumour type and should be studied in further detail. Mammary gland expression of tammar WFDC2 during the course of lactation showed WFDC2 was elevated during pregnancy, reduced in early lactation and absent in mid-late lactation. WFDC2 / HE4 can undergo a complex series of alternative splicing events that can potentially yield five distinct WAP domain containing protein isoforms.
|
|||||
TMPJ-00042 | TSLP Protein, Human, Recombinant | Human | E. coli | ||
Thymic stromal lymphopoietin (TSLP) is a novel member of the hemopoietic cytokine family that promotes the development of B cells and shares overlapping activity with IL-7. The human TSLP protein comprises a 28 amino acids (aa) signal sequence and 131 aa mature region. Human TSLP has two isoforms lfTSLP and sfTSLP produced by alternative splicing . lfTSLP is expressed in a number of tissues including heart, liver and prostate, and sfTSLP (63aa) is predominantly expressed in keratinocytes of oral mucosa, skin and in salivary glands. In aa sequence level, Human TSLP displays about 43% identity with mouse TSLP.TSLP is a cytokine that functions mainly on myeloid cells; it induces the release of T cell-attracting chemokines from monocytes and enhances the maturation of CD11c(+) dendritic cells.TSLP has proliferative effects on the myeloid cell line and may initiate asthma or atopic dermatitis responses by directly activating mast cells . TSLP signals cells via the interleukin-7 receptor-α chain (IL-7Rα),shared with IL-7, together with the TSLP receptor (TSLPR) subunit. Recent studies indicate that TSLP and its receptor are novel therapeutic targets for rheumatoid arthritis,for increased intraarticular TSLP concentrations in patients has caused chemotaxis and activation of arthritogenic T cells.
|
|||||
TMPY-05157 | TGFBR2 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. TGFBR2 has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is increased in oral squamous cell carcinoma cells. Its expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity.
|
|||||
TMPY-02919 | Cadherin 17/CDH17 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Cadherin-17 or LI-cadherin is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Cadherin-17/LI-cadherin is a cadherin-like protein consisting of an extracellular region, 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing of the encoding gene results in multiple transcript variants. Cadherin-17/LI-cadherin preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin-17 may thus contribute to the sorting of heterogeneous cell types and have a role in the morphological organization of liver and intestine. It's also involved in intestinal peptide transport. Experiments have reported the association between Cadherin-17/LI-cadherin and gastric cancer. Cadherin-17/LI-cadherin expression was detected in 63/94 of gastric adenocarcinomas in addition to intestinal metaplasia. The expression of Cadherin-17 tended to be associated with intestinal type carcinoma, and carcinomas with Cadherin-17 expression was significantly more frequent in advanced stage cases than in early stage. Cadherin-17 is also a useful immunohistochemical marker for diagnosis of adenocarcinomas of the digestive system.
|
|||||
TMPY-05352 | Cadherin 17/CDH17 Protein, Cynomolgus, Recombinant (hFc) | Cynomolgus | HEK293 | ||
Cadherin-17 or LI-cadherin is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Cadherin-17/LI-cadherin is a cadherin-like protein consisting of an extracellular region, 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing of the encoding gene results in multiple transcript variants. Cadherin-17/LI-cadherin preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin-17 may thus contribute to the sorting of heterogeneous cell types and have a role in the morphological organization of liver and intestine. It's also involved in intestinal peptide transport. Experiments have reported the association between Cadherin-17/LI-cadherin and gastric cancer. Cadherin-17/LI-cadherin expression was detected in 63/94 of gastric adenocarcinomas in addition to intestinal metaplasia. The expression of Cadherin-17 tended to be associated with intestinal type carcinoma, and carcinomas with Cadherin-17 expression was significantly more frequent in advanced stage cases than in early stage. Cadherin-17 is also a useful immunohistochemical marker for diagnosis of adenocarcinomas of the digestive system.
|
|||||
TMPY-01912 | Cadherin 17/CDH17 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Cadherin-17 or LI-cadherin is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Cadherin-17/LI-cadherin is a cadherin-like protein consisting of an extracellular region, 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing of the encoding gene results in multiple transcript variants. Cadherin-17/LI-cadherin preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin-17 may thus contribute to the sorting of heterogeneous cell types and have a role in the morphological organization of liver and intestine. It's also involved in intestinal peptide transport. Experiments have reported the association between Cadherin-17/LI-cadherin and gastric cancer. Cadherin-17/LI-cadherin expression was detected in 63/94 of gastric adenocarcinomas in addition to intestinal metaplasia. The expression of Cadherin-17 tended to be associated with intestinal type carcinoma, and carcinomas with Cadherin-17 expression was significantly more frequent in advanced stage cases than in early stage. Cadherin-17 is also a useful immunohistochemical marker for diagnosis of adenocarcinomas of the digestive system.
|
|||||
TMPH-02336 | TAS2R10 Protein, Human, Recombinant (His & KSI) | Human | E. coli | ||
Gustducin-coupled strychnine receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
|
|||||
TMPY-03225 | VSIG8 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
V-set and immunoglobulin domain containing 8 (VSIG8) is essential in hair cycle, oral mucosa, and the nail matrix. Moreover, VSIG8 also has an important role in proper epithelial differentiation and function in the upper alimentary tract.
|
|||||
TMPY-03851 | BPIFB1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
BPIFB1, also known as LPLUNC1, belongs to the BPI/LBP/Plunc superfamily, plunc family. BPIFB1 may be involved in the innate immune response to bacterial exposure in the mouth, nasal cavities, and lungs. BPIFB1 is expressed in the upper respiratory tract and oral cavity, which may function in host defence. The expression of BPIF proteins is associated with CF lung disease in humans and mice. It is unclear if this elevation of protein production, which results from phenotypic alteration of the cells within the diseased epithelium, plays a role in the pathogenesis of the disease. BPIFB1 is an abundant, secreted product of goblet cells and minor mucosal glands of the respiratory tract and oral cavity and suggest that the protein functions in the complex milieu that protects the mucosal surfaces in these locations.
|
|||||
TMPJ-00157 | CD82 Protein, Human, Recombinant (hFc) | Human | Human Cells | ||
CD82 antigen, also known as Kai-1, is a widely expressed palmitoylated molecule of the tetraspanin superfamily. KAI1/CD82 is localized on cell membrane and form interactions with other tetraspanins, integrins and chemokines which are respectively responsible for cell migration, adhesion and signaling. CD82/Kai-1 is a component of the promiscuous TIMP-1 interacting protein complex on the cell surface of human adenocarcinoma cells and gives insight into tumorigenic metastatic potential. CD82/Kai-1 suppresses EMT in prostate cancer cells adhered to fibronectin leading to reduced cell migration and invasiveness. CD82/Kai-1 function is important for muscle stem cell function in muscular disorders. Overexpression of CD82/Kai-1 suppresses growth, migration and invasion of oral cancer cells and may be considered as a potential therapeutic target in oral cancer.
|
|||||
TMPH-03155 | Lys-gingipain HG66 Protein, Porphyromonas gingivalis, Recombinant (His & Myc) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
|
|||||
TMPH-03154 | Lys-gingipain 381 Protein, Porphyromonas gingivalis, Recombinant (His) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
|
|||||
TMPH-03156 | Lys-gingipain Protein, Porphyromonas gingivalis, Recombinant (His & SUMO) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
|
|||||
TMPY-01911 | PLA2G1B Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
phospholipase A2, also known as Phosphatidylcholine 2-acylhydrolase 1B, Group IB phospholipase A2, PLA2 and PLA2G1B, is a secreted protein that belongs to the phospholipase A2 family. Phospholipase A2 / PLA2G1B catalyzes the release of fatty acids from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals. Sequences of pancreatic Phospholipase A2 / PLA2G1B enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Other forms of Phospholipase A2 / PLA2G1B have been isolated from brain, liver, lung, spleen, intestine, macrophages, leukocytes, erythrocytes, inflammatory exudates, chondrocytes, and platelets. Mice lacking in Phospholipase A2 / PLA2G1B are resistant to obesity and diabetes induced by feeding a diabetogenic high-fat/high-carbohydrate diet. Oral supplementation of a diabetogenic diet with the PLA2G1B inhibitor methyl indoxam effectively suppresses diet-induced obesity and diabetes. PLA2G1B inhibition may be a potentially effective oral therapeutic option for treatment of obesity and diabetes.
|
|||||
TMPY-01689 | PLA2G1B Protein, Human, Recombinant (His) | Human | HEK293 | ||
phospholipase A2, also known as Phosphatidylcholine 2-acylhydrolase 1B, Group IB phospholipase A2, PLA2 and PLA2G1B, is a secreted protein that belongs to the phospholipase A2 family. Phospholipase A2 / PLA2G1B catalyzes the release of fatty acids from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals. Sequences of pancreatic Phospholipase A2 / PLA2G1B enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Other forms of Phospholipase A2 / PLA2G1B have been isolated from brain, liver, lung, spleen, intestine, macrophages, leukocytes, erythrocytes, inflammatory exudates, chondrocytes, and platelets. Mice lacking in Phospholipase A2 / PLA2G1B are resistant to obesity and diabetes induced by feeding a diabetogenic high-fat/high-carbohydrate diet. Oral supplementation of a diabetogenic diet with the PLA2G1B inhibitor methyl indoxam effectively suppresses diet-induced obesity and diabetes. PLA2G1B inhibition may be a potentially effective oral therapeutic option for treatment of obesity and diabetes.
|
|||||
TMPH-02414 | Lys-gingipain W83 Protein, Porphyromonas gingivalis, Recombinant (His) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria. Has hemolytic activity; this is mediated by the adhesin domains and does not require the catalytic domain.
|
|||||
TMPH-00331 | ALS3 Protein, Candida albicans, Recombinant (B2M & His & Myc) | Candida albicans | E. coli | ||
Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the biofilm formation and pathogenesis of C.albicans infections. Necessary for C.albicans to bind to N-cadherin on endothelial cells and E-cadherin on oral epithelial cells and subsequent endocytosis by these cells. During disseminated infection, mediates initial trafficking to the brain and renal cortex and contributes to fungal persistence in the kidneys.
|
|||||
TMPH-03157 | Fimbrillin Protein, Porphyromonas gingivalis, Recombinant (His & Myc) | Porphyromonas gingivalis | E. coli | ||
Structural subunit of the major fimbriae. These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in the invasion of periodontal tissues. Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification. The sequence-based classification correlates with pathogenicity.
|
|||||
TMPJ-00860 | HTN3 Protein, Human, Recombinant | Human | E. coli | ||
HTN3 belongs to the histatin/statherin family. Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. Post-translational proteolytic processing results in many histatins: e.g., histatins 4-6 are derived from histatin 3 by proteolysis. Histatins 1 and 3 are primary products of HIS1and HIS2 alleles, respectively. Histatins are believed to have important non-immunological, anti-microbial function in the oral cavity.
|
|||||
TMPY-03971 | Statherin Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
Statherin, also known as STATH, belongs to the histatin/statherin family. Statherin may play an important role in the maintenance of oral health. It prevents calcium phospate precipitation in saliva, so maintaining a high calcium level in saliva and preventing teeth from dissolving. Statherin also inhibits spontaneous precipitation of calcium phosphate salts. Thus, statherin and PRPs may prevent build-up of harmful deposits in the salivary glands and on the tooth surfaces. Statherin is a highly stable salivary protein of low molecular mass (5,380).
|
|||||
TMPJ-00160 | EMMPRIN/CD147 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Extracellular Matrix Metalloproteinase Inducer (EMMPRIN) belongs to the immunoglobulin superfamily, which has the homology to both the immunoglobulin V domain and MHC class II antigen β-chain. EMMPRIN is a transmembrane glycoprotein with different forms, resulting from different modes of glycosylation and N-terminal sequence variants. EMMPRIN can be expressed in breast cancer, oral squamous cell carcinoma, glioma, lymphoma, lung, bladder, and melanoma carcinomas cells. EMMPRIN promotes invasion, metastasis, growth, and survival of malignants cells, serves as a receptor for extracellular cyclophilinthe, may play a role in signal transduction.
|
|||||
TMPJ-00764 | Catalase/CAT Protein, Human, Recombinant | Human | E. coli | ||
Catalase (CAT) is a member of the catalase family. It exists as a homotetramer that occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Catalase is localized in the peroxisome. Catalase promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells, and normal and transformed fibroblast cells. Defects in CAT are the cause of acatalasemia which is characterized by absence of catalase activity in red cells and is associated with ulcerating oral lesions.
|
|||||
TMPJ-01207 | UPP1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Uridinephosphorylase 1 (UPP1) is a member of the family of pentosyltransferase. UPP1 catalyses the reversible phosphorolysis of uridine to uracil. The expression levels and the enzymatic activity of UPP1 are higher in human solid tumors than in adjacent normal tissues. The high level of UPP1 expression in some tumors makes it a potential prognosticfactor for some cancers, such as oral squamous cell carcinoma. UPP1 is important for the homeostatic regulation of intracellular and plasma uridine concentratios. UPP1 plays an important role in the pyrimidine salvage pathway through its catalysis of the reversible phosphorolysis of uridine to uracil.
|
|||||
TMPY-03332 | PRTFDC1 Protein, Human, Recombinant (His) | Human | E. coli | ||
PRTFDC1 is a member of the purine/pyrimidine phosphoribosyltransferase family. It can bind GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). The epigenetic silencing of PRTFDC1 by hypermethylation of the CpG island leads to a loss of PRTFDC1 function, which might be involved in squamous cell oral carcinogenesis. PRTFDC1 is a genetic modifier of HPRT-deficiency in the mouse and has important implications for unraveling the molecular etiology of lesch-Nyhan disease(LND). LND is a severe X-linked neurological disorder caused by a deficiency of hypoxanthine phosphoribosyltransferase. PRTFDC1 has a low, barely measurable phosphoribosyltransferase activity (in vitro).
|
|||||
TMPJ-01372 | Cornulin Protein, Human, Recombinant (His) | Human | E. coli | ||
Cornulin is a member of the fused gene family of molecular chaperones. Human Cornulin contains N-terminus EF-hand domains and Ca2+ binding domains, and two glutamine- and threonine-rich 60 amino acid repeats in its C-terminus. Cornulin involves in the mucosal/epithelial immune response and epidermal differentiation. Cornulin is a survival factor that participates in the clonogenicity of squamous esophageal epithelium cell lines, attenuates deoxycholic acid (DCA)-induced apoptotic cell death and release of calcium. When Cornulin is overexpressed in oral squamous carcinoma cell lines, it regulates negatively cell proliferation by the induction of G1 arrest.
|
|||||
TMPY-04170 | DEFB1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
The DEFB1 gene, encoding for the constitutively expressed human beta-defensin 1 (hBD1) antimicrobial peptide is a potential candidate when studying genetic susceptibility to caries. DEFB1 genetic variations have been reported as contributing to hBD1 production impairment, leading to a greater susceptibility to be infected by oral pathogens, also leading to periodontitis. To counteract host immunity, Cryptosporidium parvum has evolved multiple strategies to suppress host antimicrobial defense. One such strategy is to reduce the production of the antimicrobial peptide beta-defensin 1 (DEFB1) by host epithelial cells. Beta-Defensin-1, an antimicrobial peptide encoded by the DEFB1 gene, is known to play an important role in lung mucosal immunity.
|
|||||
TMPY-00001 | CXCL14 Protein, Mouse, Recombinant | Mouse | E. coli | ||
CXCL14 is a CXC chemokine family that exhibits antimicrobial activity and contains an amphipathic cationic alpha-helical region in the C-terminus, a characteristic structure of antimicrobial peptides (AMPs). CXCL14 is involved in cell recruitment, migration, activation, and homing in liver diseases and have been shown to be upregulated during acute liver injury in animal models. The CXC chemokine ligand 14 (CXCL14) had been show highly expressed in tumor-associated stromal cells, promoting tumor cell growth, and invasion. The stimulation of dysregulated CXCL14 expression by P. gingivalis may help promote dysbiosis and the development of chronic periodontitis. The level of CXCL14 expression may be a valuable adjuvant parameter to predict the prognosis of patients with oral carcinoma and may be a potential therapeutic target.
|
|||||
TMPY-03781 | CXCL14 Protein, Human, Recombinant | Human | E. coli | ||
CXCL14 is a CXC chemokine family that exhibits antimicrobial activity and contains an amphipathic cationic alpha-helical region in the C-terminus, a characteristic structure of antimicrobial peptides (AMPs). CXCL14 is involved in cell recruitment, migration, activation, and homing in liver diseases and have been shown to be upregulated during acute liver injury in animal models. The CXC chemokine ligand 14 (CXCL14) had been show highly expressed in tumor-associated stromal cells, promoting tumor cell growth, and invasion. The stimulation of dysregulated CXCL14 expression by P. gingivalis may help promote dysbiosis and the development of chronic periodontitis. The level of CXCL14 expression may be a valuable adjuvant parameter to predict the prognosis of patients with oral carcinoma and may be a potential therapeutic target.
|
|||||
TMPY-05618 | CXCL14 Protein, Human, Recombinant, Biotinylated | Human | E. coli | ||
CXCL14 is a CXC chemokine family that exhibits antimicrobial activity and contains an amphipathic cationic alpha-helical region in the C-terminus, a characteristic structure of antimicrobial peptides (AMPs). CXCL14 is involved in cell recruitment, migration, activation, and homing in liver diseases and have been shown to be upregulated during acute liver injury in animal models. The CXC chemokine ligand 14 (CXCL14) had been show highly expressed in tumor-associated stromal cells, promoting tumor cell growth, and invasion. The stimulation of dysregulated CXCL14 expression by P. gingivalis may help promote dysbiosis and the development of chronic periodontitis. The level of CXCL14 expression may be a valuable adjuvant parameter to predict the prognosis of patients with oral carcinoma and may be a potential therapeutic target.
|
|||||
TMPY-06582 | CXCL14 Protein, Human, Recombinant (His) | Human | E. coli | ||
CXCL14 is a CXC chemokine family that exhibits antimicrobial activity and contains an amphipathic cationic alpha-helical region in the C-terminus, a characteristic structure of antimicrobial peptides (AMPs). CXCL14 is involved in cell recruitment, migration, activation, and homing in liver diseases and have been shown to be upregulated during acute liver injury in animal models. The CXC chemokine ligand 14 (CXCL14) had been show highly expressed in tumor-associated stromal cells, promoting tumor cell growth, and invasion. The stimulation of dysregulated CXCL14 expression by P. gingivalis may help promote dysbiosis and the development of chronic periodontitis. The level of CXCL14 expression may be a valuable adjuvant parameter to predict the prognosis of patients with oral carcinoma and may be a potential therapeutic target.
|
|||||
TMPJ-01173 | TFF3 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Trefoil factors (TFF) are secretory products of mucin producing cells. They play a key role in the maintenance of the surface integrity of oral mucosa and enhance healing of the gastrointestinal mucosa by a process called restitution. TFF comprises the gastric peptides (TFF1), spasmolytic peptide (TFF2), and the intestinal trefoil factor (TFF3). They have an important and necessary role in epithelial restitution within the gastrointestinal tract. Members of the trefoil family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfide bonds. They are stable secretory proteins expressed in gastrointestinal mucosa. Trefoil Factor 3(TFF3) is involved in the maintenance and repair of the intestinal mucosa. TFF3 promotes the mobility of epithelial cells in healing processes (motogen).
|
|||||
TMPY-04695 | CCL4 Protein, Rat, Recombinant (His) | Rat | Yeast | ||
CCL4 (C-C chemokine ligand 4), is a macrophage inflammatory protein with a chief effect in inflammation and immune-regulation, and was documented in cancer progression by promoting instability in the tumor environment. The inflammatory chemokine (C-C motif) ligand 4 (CCL4) plays an important role in the pathogenesis and progression of cancer. In particular, higher serum CCL4 levels in patients with oral squamous cell carcinoma (OSCC) are associated with a more advanced stage of disease. CCL4 may be a new molecular therapeutic target for inhibition of lymphangiogenesis and metastasis in OSCC. CCL3 and CCL4 loci may be marker SNPs for risk of HCV treatment outcome. CCL4 can enhance the recruitment of preosteoclasts to bone in the early stage, and the reduction of CCR5 promotes osteoclastogenesis when RANKL is prevalent.
|
|||||
TMPY-00646 | CCL4 Protein, Human, Recombinant (His) | Human | Yeast | ||
CCL4 (C-C chemokine ligand 4), is a macrophage inflammatory protein with a chief effect in inflammation and immune-regulation, and was documented in cancer progression by promoting instability in the tumor environment. The inflammatory chemokine (C-C motif) ligand 4 (CCL4) plays an important role in the pathogenesis and progression of cancer. In particular, higher serum CCL4 levels in patients with oral squamous cell carcinoma (OSCC) are associated with a more advanced stage of disease. CCL4 may be a new molecular therapeutic target for inhibition of lymphangiogenesis and metastasis in OSCC. CCL3 and CCL4 loci may be marker SNPs for risk of HCV treatment outcome. CCL4 can enhance the recruitment of preosteoclasts to bone in the early stage, and the reduction of CCR5 promotes osteoclastogenesis when RANKL is prevalent.
|
|||||
TMPH-00672 | Metalloprotease stcE Protein, E. coli O157:H7, Recombinant (His) | E. coli | E. coli | ||
Virulence factor that contributes to intimate adherence of enterohemorrhagic E.coli (EHEC) O157:H7 to host cells. Is able to cleave the secreted human mucin 7 (MUC7) and the glycoprotein 340 (DMBT1/GP340). Also cleaves human C1 inhibitor (SERPING1), a regulator of multiple inflammatory pathways, and binds and localizes it to bacterial and host cell surfaces, protecting them from complement-mediated lysis. Therefore, the current model proposes two roles for StcE during infection: it acts first as a mucinase, allowing passage of EHEC through the oral cavity by cleaving the salivary glycoproteins that are responsible for bacterial aggregation. Similarly, in the colon, StcE cleaves the glycoproteins that protect the intestinal epithelial surface, allowing EHEC to come into close contact with host cell membranes. Secondly, it acts as an anti-inflammatory agent by localizing SERPING1 to cell membranes.
|
|||||
TMPY-02391 | SUMO1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Small ubiquitin-like modifier protein (SUMO) modification is a highly dynamic process, catalyzed by SUMO-specific activating (E1), conjugating (E2) and ligating (E3) enzymes, and reversed by a family of SUMO-specific proteases (SENPs). Small ubiquitin-like modifier 1 (SUMO1) is a member of the superfamily of ubiquitin-like proteins. Despite its structural similarity with ubiquitin, SUMO1 does not seem to play any role in protein degradation. SUMO1 plays an important role in modulation of NOX activity required for ROS generation. SUMO1 haploinsufficiency results in cleft lip and palate in animal models. SUMO1 gene variation in human non-syndromic cleft lip with or without cleft palate (NSCLP) development. SUMO-1 may be useful as a novel target for therapy in oral squamous cell carcinoma (SCC) as well as a clinical indicator for tumor recurrence together with Mdm2.
|
|||||
TMPY-00415 | Notch 1 Protein, Mouse, Recombinant (hFc) | Mouse | CHO | ||
NOTCH1 is one of the four mammalian Notch receptors, which is involved in the Notch signaling pathway. Specifically, NOTCH1 promotes the proliferation of myogenic precursor cells, and the NICD domain of NOTCH1 can impair the regeneration of skeletal muscles.NOTCH1 is a prevalent signaling pathway in T cell acute lymphoblastic leukemia (T-ALL). The NOTCH signaling pathway is a conserved signaling cascade that regulates many aspects of development and homeostasis in multiple organ systems. The proto-oncogene NOTCH1 is frequently mutated in around 10% of patients with chronic lymphocytic leukemia (CLL). NOTCH1 mutations in oral squamous cell carcinoma (OSCC) frequently occur near the ligand-binding region. These mutations change the domain structure of this protein and affect the ligand-binding activity. When NOTCH1 is activated by ligand binding, the NOTCH1 intracellular domain (NICD) is cleaved from the cell membrane.
|
|||||
TMPY-02663 | Notch 1 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
NOTCH1 is one of the four mammalian Notch receptors, which is involved in the Notch signaling pathway. Specifically, NOTCH1 promotes the proliferation of myogenic precursor cells, and the NICD domain of NOTCH1 can impair the regeneration of skeletal muscles.NOTCH1 is a prevalent signaling pathway in T cell acute lymphoblastic leukemia (T-ALL). The NOTCH signaling pathway is a conserved signaling cascade that regulates many aspects of development and homeostasis in multiple organ systems. The proto-oncogene NOTCH1 is frequently mutated in around 10% of patients with chronic lymphocytic leukemia (CLL). NOTCH1 mutations in oral squamous cell carcinoma (OSCC) frequently occur near the ligand-binding region. These mutations change the domain structure of this protein and affect the ligand-binding activity. When NOTCH1 is activated by ligand binding, the NOTCH1 intracellular domain (NICD) is cleaved from the cell membrane.
|
|||||
TMPY-02140 | Tetranectin Protein, Human, Recombinant (His) | Human | HEK293 | ||
Tetranectin (TN), also known as C-type lectin domain family 3, member B (CLEC3B) is a member of the C-type lectin Family. It is plasminogen kringle 4 binding protein and regulates fibrinolysis and proteolytic processes via binding to plasminogen. Tetranectin has been suggested to play a role in tissue remodeling, due to its ability to stimulate plasminogen activation and its expression in developing tissues such as developing bone and muscle. Tetranectin enhances plasminogen activation by a tissue-type plasminogen activator so that it has been suggested to play a role in tissue remodeling. Tetranectin may play a role in the wound healing process. Tetranectin may play a role in neurological diseases and may serve as a diagnostic aid in multiple sclerosis (MS). Tetranectin was found significantly under-expressed in both serum and saliva of metastatic oral squamous cell carcinoma (OSCC) compared to primary OSCC. Tetranectin is thought to enhance proteolytic processes enabling tumor cells to invade and metastasize.
|
|||||
TMPY-03082 | TGFBR2 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. TGFBR2 has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is increased in oral squamous cell carcinoma cells. Its expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity.
|
|||||
TMPY-03199 | HE4 Protein, Canine, Recombinant (hFc) | Canine | HEK293 | ||
WAP four-disulfide core domain protein 2, also known as Epididymal secretory protein E4, Major epididymis-specific protein E4, Putative protease inhibitor WAP5, WFDC2 and HE4, is a secreted protein that contains two WAP domains. WFDC2 / HE4 is a member of a family of stable 4-disulfide core proteins that are secreted at high levels. It is expressed in a number of normal tissues, including male reproductive system, regions of the respiratory tract and nasopharynx. It is highly expressed in a number of tumors cells lines, such ovarian, colon, breast, lung and renal cells lines. Initially described as being exclusively transcribed in the epididymis. WFDC2 may be a component of the innate immune defences of the lung, nasal and oral cavities and suggest that WFDC2 functions in concert with related WAP domain containing proteins in epithelial host defence. WFDC2 re-expression in lung carcinomas may prove to be associated with tumour type and should be studied in further detail. Mammary gland expression of tammar WFDC2 during the course of lactation showed WFDC2 was elevated during pregnancy, reduced in early lactation and absent in mid-late lactation. WFDC2 / HE4 can undergo a complex series of alternative splicing events that can potentially yield five distinct WAP domain containing protein isoforms.
|
|||||
TMPY-00440 | HE4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
WAP four-disulfide core domain protein 2, also known as Epididymal secretory protein E4, Major epididymis-specific protein E4, Putative protease inhibitor WAP5, WFDC2 and HE4, is a secreted protein that contains two WAP domains. WFDC2 / HE4 is a member of a family of stable 4-disulfide core proteins that are secreted at high levels. It is expressed in a number of normal tissues, including male reproductive system, regions of the respiratory tract and nasopharynx. It is highly expressed in a number of tumors cells lines, such ovarian, colon, breast, lung and renal cells lines. Initially described as being exclusively transcribed in the epididymis. WFDC2 may be a component of the innate immune defences of the lung, nasal and oral cavities and suggest that WFDC2 functions in concert with related WAP domain containing proteins in epithelial host defence. WFDC2 re-expression in lung carcinomas may prove to be associated with tumour type and should be studied in further detail. Mammary gland expression of tammar WFDC2 during the course of lactation showed WFDC2 was elevated during pregnancy, reduced in early lactation and absent in mid-late lactation. WFDC2 / HE4 can undergo a complex series of alternative splicing events that can potentially yield five distinct WAP domain containing protein isoforms.
|
|||||
TMPY-05810 | TGFBR2 Protein, Human, Recombinant (His & hFc), Biotinylated | Human | HEK293 | ||
TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. TGFBR2 has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is increased in oral squamous cell carcinoma cells. Its expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity.
|
|||||
TMPY-05508 | TGFBR2 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. TGFBR2 has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is increased in oral squamous cell carcinoma cells. Its expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity.
|
|||||
TMPY-03171 | TGFBR2 Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
TGFBR2 is a member of the Ser/Thr protein kinase family and the TGFB receptor subfamily. It is a transmembrane protein. TGFBR2 is comprised of a C-terminal protein kinase domain and an N-terminal ectodomain. The ectodomain consists of a compact fold containing nine beta-strands and a single helix stabilized by a network of six intra strand disulfide bonds. The folding topology includes a central five-stranded antiparallel beta-sheet, eight-residues long at its centre, covered by a second layer consisting of two segments of two-stranded antiparallel beta-sheets. TGFBR2 has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is increased in oral squamous cell carcinoma cells. Its expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity.
|
|||||
TMPY-06324 | Cadherin 17/CDH17 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Cadherin-17 or LI-cadherin is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Cadherin-17/LI-cadherin is a cadherin-like protein consisting of an extracellular region, 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing of the encoding gene results in multiple transcript variants. Cadherin-17/LI-cadherin preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin-17 may thus contribute to the sorting of heterogeneous cell types and have a role in the morphological organization of liver and intestine. It's also involved in intestinal peptide transport. Experiments have reported the association between Cadherin-17/LI-cadherin and gastric cancer. Cadherin-17/LI-cadherin expression was detected in 63/94 of gastric adenocarcinomas in addition to intestinal metaplasia. The expression of Cadherin-17 tended to be associated with intestinal type carcinoma, and carcinomas with Cadherin-17 expression was significantly more frequent in advanced stage cases than in early stage. Cadherin-17 is also a useful immunohistochemical marker for diagnosis of adenocarcinomas of the digestive system.
|
|||||
TMPY-06645 | Cadherin 17/CDH17 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Cadherin-17 or LI-cadherin is a member of the cadherin superfamily, genes encoding calcium-dependent, membrane-associated glycoproteins. Cadherin-17/LI-cadherin is a cadherin-like protein consisting of an extracellular region, 7 cadherin domains, and a transmembrane region but lacking the conserved cytoplasmic domain. The protein is a component of the gastrointestinal tract and pancreatic ducts, acting as an intestinal proton-dependent peptide transporter in the first step in oral absorption of many medically important peptide-based drugs. The protein may also play a role in the morphological organization of liver and intestine. Alternative splicing of the encoding gene results in multiple transcript variants. Cadherin-17/LI-cadherin preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin-17 may thus contribute to the sorting of heterogeneous cell types and have a role in the morphological organization of liver and intestine. It's also involved in intestinal peptide transport. Experiments have reported the association between Cadherin-17/LI-cadherin and gastric cancer. Cadherin-17/LI-cadherin expression was detected in 63/94 of gastric adenocarcinomas in addition to intestinal metaplasia. The expression of Cadherin-17 tended to be associated with intestinal type carcinoma, and carcinomas with Cadherin-17 expression was significantly more frequent in advanced stage cases than in early stage. Cadherin-17 is also a useful immunohistochemical marker for diagnosis of adenocarcinomas of the digestive system.
|
|||||
TMPY-02220 | HRAS Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
HRas, also known as HRAS, belongs to the small GTPase superfamily, Ras family, and is widely expressed. It functions in signal transduction pathways. HRas can bind GTP and GDP, and they have intrinsic GTPase activity. It undergoes a continuous cycle of de- and re-palmitoylation, which regulates its rapid exchange between the plasma membrane and the Golgi apparatus. Defects in HRAS are the cause of faciocutaneoskeletal syndrome (FCSS). FCSS is a rare condition characterized by prenatally increased growth, postnatal growth deficiency, mental retardation, distinctive facial appearance, cardiovascular abnormalities, tumor predisposition, skin, and musculoskeletal abnormalities. Defects in HRAS also can cause congenital myopathy with excess of muscle spindles. HRAS deficiency may be a cause of susceptibility to Hurthle cell thyroid carcinoma. It has been shown that defects in HRAS can cause susceptibility to bladder cancer which is a malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and different sites in the bladder. Most bladder cancers are transitional cell carcinomas. They begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. Defects in HRAS are the cause of oral squamous cell carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|