目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-04123 | CEACAM1 Protein, Human, Recombinant (His & hFc) | Human | HEK293 | ||
The carcinoembryonic-antigen-related cell-adhesion molecule (CEACAM) family of proteins has been implicated in various intercellular-adhesion and intracellular-signalling-mediated effects that govern the growth and differentiation of normal and cancerous cells. CEACAM1, also known as biliary glycoprotein I (BGP I) and CD66a, is a member of the carcinoembryonic antigen (CEA) gene family which belongs to the immunoglobulin superfamily. The highly glycosylated CEACAM1 contains one N-terminal V-type Ig-like domain and three C2-type Ig-like domains within its ECD, and one ITIM motif and a calmodulin binding site in the cytoplasmic region. CEACAM1 is a surface glycoprotein expressed on various blood cells, epithelial cells, and vascular cells. It was described as an adhesion molecule mediating cell adhesion via both homophilic and heterophilic manners, and was detected on leukocytes, epithelia, and endothelia. Studies have revealed that CEACAM1 performs actions in multiple cellular processes including tissue differentiation, angiogenesis, apoptosis, metastasis, as well as the modulation of innate and adaptive immune responses.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: ICC AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPJ-00808 | CD45RA Protein, Human, Recombinant (His) | Human | Human Cells | ||
Protein tyrosine phosphatase, receptor type C (CD45), also known as PTPRC is a member of the protein tyrosine phosphatase (PTP) family which is known for its function to serve as signaling molecules and to regulate a variety of cellular processes such as cell proliferation, differentiation, mitotic cycle and oncogenic transformation. It is a variably glycosylated 180-220 kDa transmembrane protein that is abundantly expressed on all nucleated cells of hematopoietic origin. CD45 has several isoforms, expressed according to cell type, developmental stage and antigenic exposure. CD45 has been best studied in T cells, where it determines T cell receptor signaling thresholds. CD45 is moved into or out of the immunological synapse (IS) membrane microdomain depending on the relative influence of interaction with the extracellular galectin lattice or the intracellular actin cytoskeleton. Galectin interaction can be fine-tuned by varying usage of the heavily O-glycosylated spliced regions and sialylation of N-linked carbohydrates. Within the IS, CD45 dephosphorylates and negatively regulates the src family kinase, LCK. In other leukocytes, CD45 influences differentiation and links immunoreceptor signaling with cytokine secretion and cell survival, partially overlapping in function with DEP-1/CD148. CD45 deletion causes in severe immunodeficiency, while point mutations may be associated with autoimmune disorders.
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TMPY-00717 | CEACAM1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
The carcinoembryonic-antigen-related cell-adhesion molecule (CEACAM) family of proteins has been implicated in various intercellular-adhesion and intracellular-signalling-mediated effects that govern the growth and differentiation of normal and cancerous cells. CEACAM1, also known as biliary glycoprotein I (BGP I) and CD66a, is a member of the carcinoembryonic antigen (CEA) gene family which belongs to the immunoglobulin superfamily. The highly glycosylated CEACAM1 contains one N-terminal V-type Ig-like domain and three C2-type Ig-like domains within its ECD, and one ITIM motif and a calmodulin binding site in the cytoplasmic region. CEACAM1 is a surface glycoprotein expressed on various blood cells, epithelial cells, and vascular cells. It was described as an adhesion molecule mediating cell adhesion via both homophilic and heterophilic manners, and was detected on leukocytes, epithelia, and endothelia. Studies have revealed that CEACAM1 performs actions in multiple cellular processes including tissue differentiation, angiogenesis, apoptosis, metastasis, as well as the modulation of innate and adaptive immune responses.Cancer ImmunotherapyCo-inhibitory Immune Checkpoint TargetsImmune CheckpointImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint Detection: ICC AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: WB AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsImmunotherapyTargeted Therapy
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TMPJ-00828 | Tau-F Protein, Human, Recombinant | Human | E. coli | ||
Tau proteins are proteins which contain four Tau/MAP repeats. They promote microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. They are abundant in neurons of the central nervous system and are less common elsewhere, but are also expressed at very low levels in CNS astrocytes and oligodendrocytes. The tau proteins are the product of alternative splicing from a single gene that in humans is designated MAPT. When tau proteins are defective, and no longer stabilize microtubules properly, they can result in several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.
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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
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TMPJ-01330 | CD299 Protein, Human, Recombinant (His & Flag) | Human | Human Cells | ||
CD299 is also known as DC-SIGNR and CLEC4M, is a type II integral membrane protein. DC-SIGNR exists as a homotetramer, and the tandem repeat domain, also called neck domain, mediates oligermerization. Multiple human DC-SIGN/CD209 splice forms exist, generating both membrane-bound and soluble forms. DC-SIGNR is ragarded as a pathogen-recognition receptor involved in peripheral immune surveillance in liver, and probably mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. DC-SIGNR appears to selectively recognize and bind many viral surface glycoproteins containing high mannose N-linked oligosaccharides in a calcium-dependent manner, including HIV-1 gp12, HIV-2 gp12, SIV gp12, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S, as well as the cellular adhesion protein ICAM3. DC-SIGN/CD209 is expressed on dendritic cells (DC) and inflammatory macrophages and contributes to antigen presentation.
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TMPY-00668 | APP/Protease nexin-II Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli.
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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
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