目录号 | 产品详情 | 靶点 | |
---|---|---|---|
TP1309 | Antibacterial Antibiotic | ||
Gastric mucin 是一种能保护胃肠道免受酸、蛋白酶、致病微生物和机械创伤影响的糖蛋白。 | |||
T38976 | |||
MUC1, mucin core is a type I transmembrane glycoprotein that is characterized by its overexpression and abnormal glycosylation in carcinoma cells. It specifically binds to domain 1 of ICAM-1. | |||
T4S0969 | Antioxidant NF-κB | ||
Obtusifolin 是分离自决明子的种子中,能够抑制NF-kB 通路,调节气道上皮细胞中 MUC5AC 粘蛋白的基因表达和产生。它通过靶向甲状旁腺激素相关蛋白来抑制邻苯二甲酸酯诱导的乳腺癌骨转移。 | |||
T1481 | Others | ||
Fudosteine 是一种半胱氨酸衍生物和粘液活性剂。它能够抑制 MUC5AC 基因表达,阻碍 MUC5AC 粘蛋白过度分泌。 | |||
T12282 | Others | ||
Benzyl-α-GalNAc (O-glycosylation-IN-1) 是 O-糖基化的有效抑制剂,用于减少细胞表面粘蛋白的含量。它抑制人胰腺癌细胞模型黏蛋白 O-糖基化的合成。 | |||
T4S0878 | ERK Dehydrogenase NF-κB | ||
Prunetin (Prunusetin) 是一种O-甲基化异黄酮,具有抗炎的作用。它是人醛脱氢酶的有效抑制剂。 | |||
T3821 | Others HCV Protease | ||
Deapioplatycodin D 是从桔梗中分离出的一种三萜皂苷,具有抗丙型肝炎病毒活性。 | |||
TN2089 | HCV Protease NF-κB | ||
Platycodin D3 是桔梗中有抗HCV 活性的一种三萜皂苷类天然产物。 | |||
T2S2108 | Others Antibacterial | ||
Coixol (MBOA) 是一种从薏苡仁中提取的多酚,有抗菌和抗肿瘤作用。 | |||
T4503 | Chloride channel COX N-Acetylglucosaminyltransferase Anion Exchanger | ||
Talniflumate (Somalgen) 是一种钙激活氯离子通道 (hCLCA1/mCLCA3) 阻滞剂,可减少动物模型和细胞培养中的粘蛋白合成和释放。它通过抑制环氧合酶,并抑制 Cl-/HCO3- 交换活性,具有抗炎作用。它还增加了远端肠梗阻综合征囊性纤维化小鼠模型的存活率。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPY-02005 | Mucin-1/MUC1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Mucin 1, cell surface-associated (MUC1) or polymorphic epithelial mucin (PEM) is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach, and pancreas. MUC-1/CC1/CD227 Exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. After endocytosis, internalized, and recycled to the cell membrane. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. The alpha subunit has cell adhesive properties. MUC-1/CC1/CD227 Can act both as an adhesion and an anti-adhesion protein. This protein May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. MUC-1/CC1/CD227 participated in modulates signaling in ERK, SRC, and NF-kappa-B pathways. In the activated T-cells, MUC-1/CC1/CD227 influences directly or indirectly the Ras/MAPK pathway. MUC-1/CC1/CD227 Promotes tumor progression and regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|
|||||
TMPY-04340 | Mucin-1/MUC1 Protein, Human, Recombinant | Human | HEK293 | ||
Mucin 1, cell surface-associated (MUC1) or polymorphic epithelial mucin (PEM) is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach, and pancreas. MUC-1/CC1/CD227 Exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. After endocytosis, internalized, and recycled to the cell membrane. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. The alpha subunit has cell adhesive properties. MUC-1/CC1/CD227 Can act both as an adhesion and an anti-adhesion protein. This protein May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. MUC-1/CC1/CD227 participated in modulates signaling in ERK, SRC, and NF-kappa-B pathways. In the activated T-cells, MUC-1/CC1/CD227 influences directly or indirectly the Ras/MAPK pathway. MUC-1/CC1/CD227 Promotes tumor progression and regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|
|||||
TMPJ-00565 | Mucin-15/MUC15 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Mucin-15 is a single-pass type I membrane protein member of the Mucin family. Mucins are a family of high molecular weight, heavily glycosylated proteins (glycoconjugates) produced by epithelial tissues in most metazoans. A key characteristic of Mucins is their ability to form gels. Therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers. Mucin-15 is expressed in many tissues. Mucin-15 is highly glycosylated (N- and O-linked carbohydrates). Mucin-15 may play a role in the cell adhesion to the extracellular matrix.
|
|||||
TMPY-05581 | TIM-4/TIMD4 Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
A type I transmembrane protein called TIM4 (T-cell immunoglobulin- and mucin-domain-containing molecule; also known as TIMD4), which belongs to the immunoglobulin superfamily and TIM family. TIM4 is involved in regulating T-cell proliferation and lymphotoxin signaling. It is a ligand for HAVCR1/TIMD1. Recent reports indicate that dendritic cell (DC)-derived T-cell immunoglobulin and mucin domain molecule (TIM)-4, which is expressed on dendritic cells and macrophages, plays an important role in the initiation of T(H)2 polarization. TIM4 bound apoptotic cells by recognizing phosphatidylserine via its immunoglobulin domain. The expression of TIM4 in fibroblasts enhanced their ability to engulf apoptotic cells. TIM4 is phosphatidylserine receptor for the engulfment of apoptotic cells, and may also be involved in intercellular signalling in which exosomes are involved. Modulation of TIM4 production in dendritic cells (DCs) represents a novel therapeutic approach for the treatment of peanut allergy. The interaction of TIM1/TIM4 played a critical role in sustaining the polarization status of Th2 cells in allergic rhinitis (AR) patients. Cross-linking FcgammaRI by antigen/IgG complexes increased the production of TIM4 by dendritic cells via upregulating tumor necrosis factor-alpha in DCs. Specific immunotherapy (SIT) suppresses the skewed Th2 responses via disrupting the interaction of TIM1/TIM4 in antigen-specific Th2 cells.
|
|||||
TMPJ-01456 | Mucin-17/MUC17 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Mucins are key components of the mucosal barrier in the stomach that protects epithelia from carcinogenic effects of chronic inflammation. Analysis of The Cancer Genome Atlas database indicated that mucin17 (MUC17) was more highly expressed in gastric cancer (GC) specimens, with favourable prognosis for patients. And that p38 signalling is a key factor involved in MUC17-mediated inhibition of GC cell proliferation and protection against inflammatory stimulation, MUC17 upregulates the expression of MYH9 and p53, and activates the p38 pathway in GC cells through RhoA signalling.
|
|||||
TMPJ-00155 | Mucin-1/MUC1 Protein, Human, Recombinant (hFc&Avi), Biotinylated | Human | Human Cells | ||
Mucin-1, is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach and pancreas. MUC-1 exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. MUC-1 can act both as an adhesion and an anti-adhesion protein. This protein may provide a protective layer on epithelial cells against bacterial and enzyme attack. MUC-1 participated in modulates signaling in ERK, SRC and NF-kappa-B pathways. In activated T-cells, MUC-1 influences directly or indirectly the Ras/MAPK pathway. MUC-1 promotes tumor progression and regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response.
|
|||||
TMPY-06832 | Mucin-1/MUC1 Protein, Human, Recombinant (aa 1-380, His) | Human | HEK293 | ||
Mucin 1, cell surface-associated (MUC1) or polymorphic epithelial mucin (PEM) is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach, and pancreas. MUC-1/CC1/CD227 Exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. After endocytosis, internalized, and recycled to the cell membrane. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. The alpha subunit has cell adhesive properties. MUC-1/CC1/CD227 Can act both as an adhesion and an anti-adhesion protein. This protein May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. MUC-1/CC1/CD227 participated in modulates signaling in ERK, SRC, and NF-kappa-B pathways. In the activated T-cells, MUC-1/CC1/CD227 influences directly or indirectly the Ras/MAPK pathway. MUC-1/CC1/CD227 Promotes tumor progression and regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|
|||||
TMPY-02871 | Mucin-1/MUC1 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
Mucin 1, cell surface-associated (MUC1) or polymorphic epithelial mucin (PEM) is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach, and pancreas. MUC-1/CC1/CD227 Exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. After endocytosis, internalized, and recycled to the cell membrane. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. The alpha subunit has cell adhesive properties. MUC-1/CC1/CD227 Can act both as an adhesion and an anti-adhesion protein. This protein May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. MUC-1/CC1/CD227 participated in modulates signaling in ERK, SRC, and NF-kappa-B pathways. In the activated T-cells, MUC-1/CC1/CD227 influences directly or indirectly the Ras/MAPK pathway. MUC-1/CC1/CD227 Promotes tumor progression and regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|
|||||
TMPY-06833 | Mucin-1/MUC1 Protein, Human, Recombinant (aa 890-1158, His) | Human | HEK293 | ||
Mucin 1, cell surface-associated (MUC1) or polymorphic epithelial mucin (PEM) is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach, and pancreas. MUC-1/CC1/CD227 Exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. After endocytosis, internalized, and recycled to the cell membrane. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. The alpha subunit has cell adhesive properties. MUC-1/CC1/CD227 Can act both as an adhesion and an anti-adhesion protein. This protein May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. MUC-1/CC1/CD227 participated in modulates signaling in ERK, SRC, and NF-kappa-B pathways. In the activated T-cells, MUC-1/CC1/CD227 influences directly or indirectly the Ras/MAPK pathway. MUC-1/CC1/CD227 Promotes tumor progression and regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|
|||||
TMPY-06707 | Mucin-1/MUC1 Protein, Human, Recombinant (aa 1-173, His) | Human | HEK293 | ||
Mucin 1, cell surface-associated (MUC1) or polymorphic epithelial mucin (PEM) is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach, and pancreas. MUC-1/CC1/CD227 Exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. After endocytosis, internalized, and recycled to the cell membrane. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. The alpha subunit has cell adhesive properties. MUC-1/CC1/CD227 Can act both as an adhesion and an anti-adhesion protein. This protein May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. MUC-1/CC1/CD227 participated in modulates signaling in ERK, SRC, and NF-kappa-B pathways. In the activated T-cells, MUC-1/CC1/CD227 influences directly or indirectly the Ras/MAPK pathway. MUC-1/CC1/CD227 Promotes tumor progression and regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|
|||||
TMPK-00828 | Mucin-1/MUC1 Isoform Y Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
MUC1, the transmembrane glycoprotein Mucin 1, is usually found to be overexpressed in a variety of epithelial cancers playing an important role in disease progression. MUC1 isoforms such as MUC1/Y, which lacks the entire variable number of tandem repeat region, are involved in oncogenic processes by enhancing tumour initiation. MUC1/Y is therefore considered a promising target for the identification and treatment of epithelial cancers.
|
|||||
TMPY-00573 | MUCL1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
MUCL1 Protein, Human, Recombinant (His) is expressed in HEK293 with His tag. The predicted molecular weight is 8.4 kDa. Accession number: Q96DR8
|
|||||
TMPY-02124 | TIM-4/TIMD4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
A type I transmembrane protein called TIM4 (T-cell immunoglobulin- and mucin-domain-containing molecule; also known as TIMD4), which belongs to the immunoglobulin superfamily and TIM family. TIM4 is involved in regulating T-cell proliferation and lymphotoxin signaling. It is a ligand for HAVCR1/TIMD1. Recent reports indicate that dendritic cell (DC)-derived T-cell immunoglobulin and mucin domain molecule (TIM)-4, which is expressed on dendritic cells and macrophages, plays an important role in the initiation of T(H)2 polarization. TIM4 bound apoptotic cells by recognizing phosphatidylserine via its immunoglobulin domain. The expression of TIM4 in fibroblasts enhanced their ability to engulf apoptotic cells. TIM4 is phosphatidylserine receptor for the engulfment of apoptotic cells, and may also be involved in intercellular signalling in which exosomes are involved. Modulation of TIM4 production in dendritic cells (DCs) represents a novel therapeutic approach for the treatment of peanut allergy. The interaction of TIM1/TIM4 played a critical role in sustaining the polarization status of Th2 cells in allergic rhinitis (AR) patients. Cross-linking FcgammaRI by antigen/IgG complexes increased the production of TIM4 by dendritic cells via upregulating tumor necrosis factor-alpha in DCs. Specific immunotherapy (SIT) suppresses the skewed Th2 responses via disrupting the interaction of TIM1/TIM4 in antigen-specific Th2 cells.
|
|||||
TMPJ-01432 | CA125/MUC16 Protein, Human, Recombinant (hFc & AVI), Biotinylated | Human | Human Cells | ||
MUC16, also known as the CA125 antigen, is a mucin protein that may be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy. MUC16 is over-expressed by tumor cells including ovarian and mesothelial cancers. The transmembrane form can adhere to mesothelin in the peritoneum, facilitating metastasis of ovarian cancer to the peritoneal cavity. MUC16 also binds galectin-1 on immune cells and enhances its expression on tumor cells. MUC16-expressing tumors adhere to NK cells, down-regulate CD16 and suppress NK response, which may promote immune evasion. MUC16 is also cyclically expressed in the endometrium and may contribute to immune privilege during pregnancy. In the eye, MUC16 and other mucins protect the cornea and keep it hydrated. It is altered on the conjunctival epithelium of patients with non-Sjogren dry eye syndrome.
|
|||||
TMPJ-00189 | TIM-3/KIM-3/HAVCR2 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | Human Cells | ||
T cell immunoglobulin and mucin domain 3 is a member of the TIM family of immune regulating molecules. Mature cynomolgus TIM3 consists of a 182 amino acid (aa)extracellular domain (ECD), a 21 aa transmembrane segment, and a 78 aa cytoplasmic tail. TIM3 is up-regulated on several populations of activated myeloid cells (macrophage, monocyte, dendritic cell, microglia, mast cell) and T cells (Th1, CD8+, NK, Treg). Its binding to Galectin9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity. TIM3 ligation attenuates CD8+ and Th1 cell responses and promotes the activity of Treg and myeloid derived suppressor cells. TIM3 interactions with Galectin-9 can trigger immune stimulatory effects, such as the coactivation of NK cell cytotoxicity.
|
|||||
TMPY-01072 | CCL5 Protein, Human, Recombinant (His & mucin) | Human | HEK293 | ||
Chemokines are a family of small chemotactic cytokines, or proteins secreted by cells. Chemokines share the same structure similarities such as small size, and the presence of four cysteine residues in conserved locations in order to form their 3-dimensional shape. Some of the chemokines are considered pro-inflammatory which can be induced to recruit cells of the immune system to a site of infection during an immune response, while others are considered homeostatic and are implied in controlling the migration of cells during normal processes of tissue maintenance and development. There are four members of the chemokine family: C-C kemokines, C kemokines, CXC kemokines and CX3C kemokines. The C-C kemokines have two cysteines nearby the amino terminus. There have been at least 27 distinct members of this subgroup reported for mammals, called C-C chemokine ligands-1 to 28. Chemokin ligand 5(CCL5) is chemotactic for T cells, basophils and eosinophils. Chemokin ligand 5(CCL5) has been considered a HIV-supressor secreted by CD8+T cells and other immune cells. Chemokin ligand 5(CCL5) is a key to activating recruit leukocytes into inflammatory sites and in the presence of particular cytokines released by T cells, it can change the NK cells into CHAK cells.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|
|||||
TMPY-00133 | PARM-1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
PARM-1 Protein, Human, Recombinant (His) is expressed in HEK293 with His tag. The predicted molecular weight is 25.7 kDa. Accession number: AAH13294.1
|
|||||
TMPJ-00174 | TIM-3/KIM-3/HAVCR2 Protein, Mouse, Recombinant (aa 20-193, His) | Mouse | Human Cells | ||
T cell immunoglobulin and mucin domain-3 (TIM3), also called hepatitis A virus cellular receptor 2 (HAVCR2), is a transmembrane glycoprotein of the TIM family of immune regulating molecules and plays an important role in the Th1-mediated immune response. TIM3 is expressed on the Th1 cells, CD8 T-cells, monocytes, and dendritic cells, but not on Th2 cells. TIM3 expressed by monocytes and dendritic cells facilitates phagocytosis of apoptotic cells and up-regulates cross-presentation of apoptotic cell-associated antigens through interaction with phosphatidylserine. Engagement of TIM3 by its ligand galectin-9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity. Stimulation of TIM3 with an agonistic antibody promotes inflammation through the activation of innate immune cells. TIM3 is also regarded as a potential target molecule for immunotherapy. TIM3 and programmed cell death 1 (PD-1) as two important coinhibitory regulators of T cell responses, have been implicated with the T-cell dysfunction or exhaustion associated with chronic HBV infection including HBV-related HCC.
|
|||||
TMPJ-00624 | TIM-3/KIM-3/HAVCR2 Protein, Marmoset, Recombinant (His) | Marmoset | Human Cells | ||
T cell immunoglobulin and mucin domain-3 (TIM3), also called hepatitis A virus cellular receptor 2 (HAVCR2), is a transmembrane glycoprotein of the TIM family of immune regulating molecules and plays an important role in the Th1-mediated immune response. TIM3 is expressed on the Th1 cells, CD8 T-cells, monocytes, and dendritic cells, but not on Th2 cells. TIM3 expressed by monocytes and dendritic cells facilitates phagocytosis of apoptotic cells and up-regulates cross-presentation of apoptotic cell-associated antigens through interaction with phosphatidylserine. Engagement of TIM3 by its ligand galectin-9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity. Stimulation of TIM3 with an agonistic antibody promotes inflammation through the activation of innate immune cells. TIM3 is also regarded as a potential target molecule for immunotherapy. TIM3 and programmed cell death 1 (PD-1) as two important coinhibitory regulators of T cell responses, have been implicated with the T-cell dysfunction or exhaustion associated with chronic HBV infection including HBV-related HCC.
|
|||||
TMPH-01708 | Mucin-2/MUC2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Coats the epithelia of the intestines, airways, and other mucus membrane-containing organs. Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. Major constituent of both the inner and outer mucus layers of the colon and may play a role in excluding bacteria from the inner mucus layer.
|
|||||
TMPH-01706 | Mucin-16/MUC16 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.
|
|||||
TMPH-01705 | Mucin-1/MUC1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Mucin-1/MUC1 Protein, Human, Recombinant (His) is expressed in E. coli with N-terminal 6xHis tag. The predicted molecular weight is 31.2 kDa. Accession number: P15941-8
|
|||||
TMPY-01375 | TIM-4/TIMD4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
A type I transmembrane protein called TIM4 (T-cell immunoglobulin- and mucin-domain-containing molecule; also known as TIMD4), which belongs to the immunoglobulin superfamily and TIM family. TIM4 is involved in regulating T-cell proliferation and lymphotoxin signaling. It is a ligand for HAVCR1/TIMD1. Recent reports indicate that dendritic cell (DC)-derived T-cell immunoglobulin and mucin domain molecule (TIM)-4, which is expressed on dendritic cells and macrophages, plays an important role in the initiation of T(H)2 polarization. TIM4 bound apoptotic cells by recognizing phosphatidylserine via its immunoglobulin domain. The expression of TIM4 in fibroblasts enhanced their ability to engulf apoptotic cells. TIM4 is phosphatidylserine receptor for the engulfment of apoptotic cells, and may also be involved in intercellular signalling in which exosomes are involved. Modulation of TIM4 production in dendritic cells (DCs) represents a novel therapeutic approach for the treatment of peanut allergy. The interaction of TIM1/TIM4 played a critical role in sustaining the polarization status of Th2 cells in allergic rhinitis (AR) patients. Cross-linking FcgammaRI by antigen/IgG complexes increased the production of TIM4 by dendritic cells via upregulating tumor necrosis factor-alpha in DCs. Specific immunotherapy (SIT) suppresses the skewed Th2 responses via disrupting the interaction of TIM1/TIM4 in antigen-specific Th2 cells.
|
|||||
TMPJ-00173 | TIM-3/KIM-3/HAVCR2 Protein, Mouse, Recombinant (aa 20-191, His) | Mouse | Human Cells | ||
T cell immunoglobulin and mucin domain-3 (TIM3), also called hepatitis A virus cellular receptor 2 (HAVCR2), is a transmembrane glycoprotein of the TIM family of immune regulating molecules and plays an important role in the Th1-mediated immune response. TIM3 is expressed on the Th1 cells, CD8 T-cells, monocytes, and dendritic cells, but not on Th2 cells. TIM3 expressed by monocytes and dendritic cells facilitates phagocytosis of apoptotic cells and up-regulates cross-presentation of apoptotic cell-associated antigens through interaction with phosphatidylserine. Engagement of TIM3 by its ligand galectin-9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity. Stimulation of TIM3 with an agonistic antibody promotes inflammation through the activation of innate immune cells. TIM3 is also regarded as a potential target molecule for immunotherapy. TIM3 and programmed cell death 1 (PD-1) as two important coinhibitory regulators of T cell responses, have been implicated with the T-cell dysfunction or exhaustion associated with chronic HBV infection including HBV-related HCC.
|
|||||
TMPH-01709 | Mucin-5B/MUC5B Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Gel-forming mucin that is thought to contribute to the lubricating and viscoelastic properties of whole saliva and cervical mucus.
|
|||||
TMPY-00199 | Ebola virus EBOV (Subtype Sudan, strain Gulu) Glycoprotein/GP1 (mucin domain deleted) Protein (aa 1-320, His) | EBOV | Baculovirus-Insect Cells | ||
The fourth gene of the EBOV genome encodes a 16-kDa envelope-attached glycoprotein (GP) and a 11 kDa secreted glycoprotein (sGP). Both GP and sGP have an identical 295-residue N-terminus, however, they have different C-terminal sequences. Recently, great attention has been paid to GP for vaccines design and entry inhibitors isolation. GP is a class I fusion protein which assembles as trimers on viral surface and plays an important role in virus entry and attachment. Mature GP is a disulfide-linked heterodimer formed by two subunits, GP1 and GP2, which are generated from the proteolytical process of GP precursor (pre-GP) by cellular furin during virus assembly . The GP1 subunit contains a mucin domain and a receptor-binding domain (RBD); the GP2 subunit has a fusion peptide, a helical heptad-repeat (HR) region, a transmembrane (TM) domain, and a 4-residue cytoplasmic tail. The RBD of GP1 mediates the interaction of EBOV with cellular receptor (e.g. DC-SIGN/LSIGN, TIM-1, hMGL, NPC1, β-integrins, folate receptor-α, and Tyro3 family receptors), of which TIM1 and NPC1 are essential for EBOV entry; the mucin domain having N- and O-linked glycans enhances the viral attachment to cellular hMGL, and participates in shielding key neutralization epitopes, which helps the virus evades immune elimination. There are large conformation changes of GP2 during membrane fusion, which enhance the insertion of fusion loop into cellular membrane and facilitate the release of viral nucleocapsid core to cytoplasm.
|
|||||
TMPJ-00599 | TIM-3/KIM-3/HAVCR2 Protein, Human, Recombinant (hFc & His) | Human | Human Cells | ||
Hepatitis A virus cellular receptor 2(HAVCR2)is a single-pass type I membrane protein and it contains 1 Ig-like V-type (immunoglobulin-like) domain. The protein belongs to the immunoglobulin superfamily, and TIM family of proteins. The protein regulates macrophage activation. It inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance. It may be also involved in T-cell homing and it is receptor for LGALS9. CD4 (MIM 186940)-positive T helper lymphocytes can be divided into types 1 (Th1) and 2 (Th2) on the basis of their cytokine secretion patterns. Th1 cells and their associated cytokines are involved in cell-mediated immunity to intracellular pathogens and delayed-type hypersensitivity reactions, whereas Th2 cells are involved in the control of extracellular helminthic infections and the promotion of atopic and allergic diseases. The 2 types of cells also cross-regulate the functions of the other. TIM3 is a Th1-specific cell surface protein that regulates macrophage activation and enhances the severity of experimental autoimmune encephalomyelitis in mice.
|
|||||
TMPH-00044 | RuvC Protein, Akkermansia muciniphila, Recombinant (His & Myc) | Akkermansia muciniphila | E. coli | ||
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
|
|||||
TMPY-03531 | PSGL-1/CD162 Protein, Human, Recombinant (His) | Human | HEK293 | ||
P-selectin glycoprotein ligand-1 (PSGL-1), also known as SELPLG or CD162, is the high affinity ounter-receptor for P-selectin on expressed on activated endothelial cells and platelets. PSGL-1 is a mucin-type glycoprotein, expressed on leukocytes and platelets as a homodimer of two disulfide-linked subunits of ~12 kD. As cell adhesion molecules, multiple studies have shown that PSGL-1/ P-selectin interaction is required for the normal recruitment of leukocytes during inflammatory reactions, and also participates in hemostatic responses. PSGL-1 protein requires two distinct posttranslational modifications for the Ca2+-dependent recognition by the lectin domain of P-selectin, that is tyrosine sulfation and specific O-linked glycosylation (sialic acid and fucose). PSGL-1 can also bind to other two members of the selectin family, E-selectin (endothelial) and L-selectin (leukocyte), but binds best to P-selectin.
|
|||||
TMPY-05013 | PSGL-1/CD162 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
P-selectin glycoprotein ligand-1 (PSGL-1), also known as SELPLG or CD162, is the high affinity ounter-receptor for P-selectin on expressed on activated endothelial cells and platelets. PSGL-1 is a mucin-type glycoprotein, expressed on leukocytes and platelets as a homodimer of two disulfide-linked subunits of ~12 kD. As cell adhesion molecules, multiple studies have shown that PSGL-1/ P-selectin interaction is required for the normal recruitment of leukocytes during inflammatory reactions, and also participates in hemostatic responses. PSGL-1 protein requires two distinct posttranslational modifications for the Ca2+-dependent recognition by the lectin domain of P-selectin, that is tyrosine sulfation and specific O-linked glycosylation (sialic acid and fucose). PSGL-1 can also bind to other two members of the selectin family, E-selectin (endothelial) and L-selectin (leukocyte), but binds best to P-selectin.
|
|||||
TMPY-01730 | CD24 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
The cluster of differentiation (CD) system is commonly used as cell markers in Immunophenotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Cluster of differentiation 24, also known as signal transducer CD24 or heat stable antigen CD24 (HSA), is a mucin-type glycosylphosphatidylinositol-linked glycoprotein expressed on the surface of B-cells, differentiating neuroblasts and many tumors. It is involved in molecular adhesion and metastatic tumor spread and serve as a normal receptor for P-selectin. The CD24 / P-selectin pathway could be important in disseminating tumor cells by facilitating the interaction with platelet and endothelial cells. It has also been considered as a tumor marker. High rate of CD24 expressions have been found in epithelial ovarian cancer, breast cancer, non-small cell lung cancer, prostate cancer and pancreatic cancer.
|
|||||
TMPY-03016 | CD24 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
The cluster of differentiation (CD) system is commonly used as cell markers in Immunophenotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Cluster of differentiation 24, also known as signal transducer CD24 or heat stable antigen CD24 (HSA), is a mucin-type glycosylphosphatidylinositol-linked glycoprotein expressed on the surface of B-cells, differentiating neuroblasts and many tumors. It is involved in molecular adhesion and metastatic tumor spread and serve as a normal receptor for P-selectin. The CD24 / P-selectin pathway could be important in disseminating tumor cells by facilitating the interaction with platelet and endothelial cells. It has also been considered as a tumor marker. High rate of CD24 expressions have been found in epithelial ovarian cancer, breast cancer, non-small cell lung cancer, prostate cancer and pancreatic cancer.
|
|||||
TMPY-01621 | TIM-3/KIM-3/HAVCR2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Hepatitis A virus cellular receptor 2 (HAVCR2), formerly known as T cell immunoglobulin and mucin domain-3 (TIM-3), is a transmembrane glycoprotein expressed on the surface of terminally differentiated Th1 cells but not on Th2 cells. It was the first surface molecule that specifically identifies Th1 cells in both the mouse and human. Recently, the identification of Galectin-9 as a ligand for TIM-3 has established the TIM-3-Galectin-9 pathway as an important regulator of Th1 immunity and tolerance induction. Engagement of Tim-3 by its ligand galectin-9 negatively regulates IFN-gamma secretion and influences the ability to induce T cell tolerance in both mice and man. It suggests a novel paradigm in which dysregulation of the TIM-3-galectin-9 pathway could underlie chronic autoimmune disease states, such as multiple sclerosis. Recent work has explored the role of TIM-3 in systemic lupus erythematosus (SLE), and their results indicate that TIM-3 may represent a novel target for the treatment of SLE. Numerous studies have demonstrated that Tim-3 influences autoimmune diseases, including diabetes and multiple sclerosis, and its role in other inflammatory diseases including allergies and cancer is beginning to become clear. In the tumor rejection model, the soluble form of Tim-3 (sTim-3) significantly impaired T cell antitumor immunity, evidenced by decreased antitumor CTL activity and reduced amount of tumor-infiltrating lymphocytes in the tumor. sTim-3 as an immunoregulatory molecule that may be involved in the negative regulation of T cell-mediated immune response.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IP AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
|
|||||
TMPY-05227 | TIM-3/KIM-3/HAVCR2 Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
Hepatitis A virus cellular receptor 2 (HAVCR2), formerly known as T cell immunoglobulin and mucin domain-3 (TIM-3), is a transmembrane glycoprotein expressed on the surface of terminally differentiated Th1 cells but not on Th2 cells. It was the first surface molecule that specifically identifies Th1 cells in both the mouse and human. Recently, the identification of Galectin-9 as a ligand for TIM-3 has established the TIM-3-Galectin-9 pathway as an important regulator of Th1 immunity and tolerance induction. Engagement of Tim-3 by its ligand galectin-9 negatively regulates IFN-gamma secretion and influences the ability to induce T cell tolerance in both mice and man. It suggests a novel paradigm in which dysregulation of the TIM-3-galectin-9 pathway could underlie chronic autoimmune disease states, such as multiple sclerosis. Recent work has explored the role of TIM-3 in systemic lupus erythematosus (SLE), and their results indicate that TIM-3 may represent a novel target for the treatment of SLE. Numerous studies have demonstrated that Tim-3 influences autoimmune diseases, including diabetes and multiple sclerosis, and its role in other inflammatory diseases including allergies and cancer is beginning to become clear. In the tumor rejection model, the soluble form of Tim-3 (sTim-3) significantly impaired T cell antitumor immunity, evidenced by decreased antitumor CTL activity and reduced amount of tumor-infiltrating lymphocytes in the tumor. sTim-3 as an immunoregulatory molecule that may be involved in the negative regulation of T cell-mediated immune response.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IP AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
|
|||||
TMPK-01272 | TIM-4/TIMD4 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Tim4 is a transmembrane protein as the phosphatidylserine (PS) receptor, known as T cell immunoglobulin and mucin domain containing protein-4. It is expressed highly in macrophages, and macrophage Tim-4 inhibits inflammation under various conditions of immune activation.
|
|||||
TMPK-01141 | TIM-4/TIMD4 Protein, Human, Recombinant (aa 25-314, His) | Human | HEK293 | ||
Tim4 is a transmembrane protein as the phosphatidylserine (PS) receptor, known as T cell immunoglobulin and mucin domain containing protein-4. It is expressed highly in macrophages, and macrophage Tim-4 inhibits inflammation under various conditions of immune activation.
|
|||||
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.
|
|||||
TMPY-05801 | Podoplanin Protein, Human, Recombinant (His) | Human | HEK293 | ||
Podoplanin, also known as PDPN, is a type-I integral membrane glycoprotein with diverse distribution in human tissues. The physiological function of this protein may be related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor. The specific function of this protein has not been determined. Alternatively spliced transcript variants encoding different isoforms have been identified.PDPN is a mucin-type glycoprotein negatively charged by extensive O-glycosylation and a high content of sialic acid, which expresses the adhesive property. It is selectively expressed in lymphatic endothelium as well as lymphangiomas, Kaposi sarcomas, and in a subset of angiosarcomas with probable lymphatic differentiation. PDPN may contribute to form odontoblastic fiber or function as the anchorage to the tooth development and in proliferating epithelial cells of cervical loop and apical bud. The intensity of podoplanin expression is negatively correlated with the expression of CD34 and factor VIII. Podoplanin would be useful as a diagnostic marker for epithelioid hemangioendothelioma in liver tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|
|||||
TMPK-00286 | Siglec-9 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Siglec-9 is a sialic-acid-binding lectin expressed predominantly on myeloid cells. Aberrant glycosylation occurs in essentially all types of cancers and results in increased sialylation. Thus, when the mucin MUC1 is expressed on cancer cells, it is decorated by multiple short, sialylated O-linked glycans (MUC1-ST).
|
|||||
TMPK-00287 | Siglec-9 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Siglec-9 is a sialic-acid-binding lectin expressed predominantly on myeloid cells. Aberrant glycosylation occurs in essentially all types of cancers and results in increased sialylation. Thus, when the mucin MUC1 is expressed on cancer cells, it is decorated by multiple short, sialylated O-linked glycans (MUC1-ST).
|
|||||
TMPK-01365 | CA125/MUC16 Protein, Human, Recombinant (aa 12783-13467, His & AVI), Biotinylated | Human | HEK293 | ||
MUC16, also known as the CA125 antigen, is a mucin protein that may be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy.Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.Binding to MSLN mediates heterotypic cell adhesion. This may contribute to the metastasis of ovarian cancer to the peritoneum by initiating cell attachment to the mesothelial epithelium via binding to MSLN.
|
|||||
TMPK-01394 | CA125/MUC16 Protein, Human, Recombinant (aa 12783-13467, His) | Human | HEK293 | ||
MUC16, also known as the CA125 antigen, is a mucin protein that may be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy.Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.Binding to MSLN mediates heterotypic cell adhesion. This may contribute to the metastasis of ovarian cancer to the peritoneum by initiating cell attachment to the mesothelial epithelium via binding to MSLN.
|
|||||
TMPK-01359 | CA125/MUC16 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
MUC16, also known as the CA125 antigen, is a mucin protein that may be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy.Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.Binding to MSLN mediates heterotypic cell adhesion. This may contribute to the metastasis of ovarian cancer to the peritoneum by initiating cell attachment to the mesothelial epithelium via binding to MSLN.
|
|||||
TMPY-00555 | Podoplanin Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
Podoplanin, also known as PDPN, is a type-I integral membrane glycoprotein with diverse distribution in human tissues. The physiological function of this protein may be related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor. The specific function of this protein has not been determined. Alternatively spliced transcript variants encoding different isoforms have been identified.PDPN is a mucin-type glycoprotein negatively charged by extensive O-glycosylation and a high content of sialic acid, which expresses the adhesive property. It is selectively expressed in lymphatic endothelium as well as lymphangiomas, Kaposi sarcomas, and in a subset of angiosarcomas with probable lymphatic differentiation. PDPN may contribute to form odontoblastic fiber or function as the anchorage to the tooth development and in proliferating epithelial cells of cervical loop and apical bud. The intensity of podoplanin expression is negatively correlated with the expression of CD34 and factor VIII. Podoplanin would be useful as a diagnostic marker for epithelioid hemangioendothelioma in liver tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|
|||||
TMPY-01311 | Podoplanin Protein, Human, Recombinant (His & hFc) | Human | HEK293 | ||
Podoplanin, also known as PDPN, is a type-I integral membrane glycoprotein with diverse distribution in human tissues. The physiological function of this protein may be related to its mucin-type character. The homologous protein in other species has been described as a differentiation antigen and influenza-virus receptor. The specific function of this protein has not been determined. Alternatively spliced transcript variants encoding different isoforms have been identified.PDPN is a mucin-type glycoprotein negatively charged by extensive O-glycosylation and a high content of sialic acid, which expresses the adhesive property. It is selectively expressed in lymphatic endothelium as well as lymphangiomas, Kaposi sarcomas, and in a subset of angiosarcomas with probable lymphatic differentiation. PDPN may contribute to form odontoblastic fiber or function as the anchorage to the tooth development and in proliferating epithelial cells of cervical loop and apical bud. The intensity of podoplanin expression is negatively correlated with the expression of CD34 and factor VIII. Podoplanin would be useful as a diagnostic marker for epithelioid hemangioendothelioma in liver tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
|
|||||
TMPY-00041 | Ebola virus EBOV (subtype Zaire, strain H.sapiens-wt/GIN/2014/Kissidougou-C15) Glycoprotein/GP1 Protein (His) | EBOV | Baculovirus-Insect Cells | ||
The fourth gene of the EBOV genome encodes a 16-kDa envelope-attached glycoprotein (GP) and a 11 kDa secreted glycoprotein (sGP). Both GP and sGP have an identical 295-residue N-terminus, however, they have different C-terminal sequences. Recently, great attention has been paid to GP for vaccines design and entry inhibitors isolation. GP is a class I fusion protein which assembles as trimers on viral surface and plays an important role in virus entry and attachment. Mature GP is a disulfide-linked heterodimer formed by two subunits, GP1 and GP2, which are generated from the proteolytical process of GP precursor (pre-GP) by cellular furin during virus assembly . The GP1 subunit contains a mucin domain and a receptor-binding domain (RBD); the GP2 subunit has a fusion peptide, a helical heptad-repeat (HR) region, a transmembrane (TM) domain, and a 4-residue cytoplasmic tail. The RBD of GP1 mediates the interaction of EBOV with cellular receptor (e.g. DC-SIGN/LSIGN, TIM-1, hMGL, NPC1, β-integrins, folate receptor-α, and Tyro3 family receptors), of which TIM1 and NPC1 are essential for EBOV entry; the mucin domain having N- and O-linked glycans enhances the viral attachment to cellular hMGL, and participates in shielding key neutralization epitopes, which helps the virus evades immune elimination. There are large conformation changes of GP2 during membrane fusion, which enhance the insertion of fusion loop into cellular membrane and facilitate the release of viral nucleocapsid core to cytoplasm.
|
|||||
TMPY-00071 | Ebola virus EBOV (subtype Zaire, strain Ebola virus H.sapiens-wt/SLE/2014/ManoRiver-G3686.1) Glycoprotein/EBOV-G Protein (His) | EBOV | HEK293 | ||
The fourth gene of the EBOV genome encodes a 16-kDa envelope-attached glycoprotein (GP) and a 11 kDa secreted glycoprotein (sGP). Both GP and sGP have an identical 295-residue N-terminus, however, they have different C-terminal sequences. Recently, great attention has been paid to GP for vaccines design and entry inhibitors isolation. GP is a class I fusion protein which assembles as trimers on viral surface and plays an important role in virus entry and attachment. Mature GP is a disulfide-linked heterodimer formed by two subunits, GP1 and GP2, which are generated from the proteolytical process of GP precursor (pre-GP) by cellular furin during virus assembly . The GP1 subunit contains a mucin domain and a receptor-binding domain (RBD); the GP2 subunit has a fusion peptide, a helical heptad-repeat (HR) region, a transmembrane (TM) domain, and a 4-residue cytoplasmic tail. The RBD of GP1 mediates the interaction of EBOV with cellular receptor (e.g. DC-SIGN/LSIGN, TIM-1, hMGL, NPC1, β-integrins, folate receptor-α, and Tyro3 family receptors), of which TIM1 and NPC1 are essential for EBOV entry; the mucin domain having N- and O-linked glycans enhances the viral attachment to cellular hMGL, and participates in shielding key neutralization epitopes, which helps the virus evades immune elimination. There are large conformation changes of GP2 during membrane fusion, which enhance the insertion of fusion loop into cellular membrane and facilitate the release of viral nucleocapsid core to cytoplasm.
|
|||||
TMPK-00190 | TIM-3/KIM-3/HAVCR2 Protein, Human, Recombinant (aa 22-200, His) | Human | HEK293 | ||
Hepatitis A virus cellular receptor 2 (HAVCR2), also known as T-cell immunoglobulin and mucin-domain containing-3 (TIM-3), is a protein that in humans is encoded by the HAVCR2 gene.TIM3 is an immune checkpoint and together with other inhibitory receptors including programmed cell death protein 1 (PD-1) and lymphocyte activation gene 3 protein (LAG3) mediate the CD8 T-cell exhaustion. TIM3 has also been shown as a CD4 Th1-specific cell surface protein that regulates macrophage activation and enhances the severity of experimental autoimmune encephalomyelitis in mice.
|
|||||
TMPK-01366 | CA125/MUC16 Protein, Human, Recombinant (aa 12660-12923, His & AVI), Biotinylated | Human | HEK293 | ||
MUC16, also known as the CA125 antigen, is a mucin protein that may be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy.Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces.Binding to MSLN mediates heterotypic cell adhesion. This may contribute to the metastasis of ovarian cancer to the peritoneum by initiating cell attachment to the mesothelial epithelium via binding to MSLN.
|
|||||
TMPJ-01151 | MAdCAM-1 Protein, Human, Recombinant (hFc) | Human | Human Cells | ||
Mucosal addressin cell adhesion molecule-1 (MAdCAM-1) is an approximately 60 kDa type 1 transmembrane glycoprotein. It is an endothelial cell adhesion molecule that belongs to the immunoglobulin (Ig) superfamily of proteins. The Ig domains of MAdCAM-1 are critical to alpha (4) beta (7) binding, and the mucin domain has activity in L Selectin binding. MAdCAM-1 expression is up-regulated by TNF-alpha and IL 1 beta. Mucosal addressin cell adhesion molecule (MAdCAM-1) plays a pivotal role in T-lymphocyte homing to the gut. MAdCAM 1 expression is also dramatically increased in chronic inflammatory and disease states, including inflammatory bowel disease (Crohn’s disease and ulcerative colitis), sclerosing cholangitis, and diabetes, and may play an important role in these conditions.
|