目录号 | 产品详情 | 靶点 | |
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T36573 | Apoptosis Epigenetic Reader Domain | ||
NHWD-870 是一种有效且特异性的 BET 家族溴结构域抑制剂,仅与 BRD2、BRD3、BRD4 (IC50 = 2.7 nM) 和 BRDT 结合。 NHWD-870 具有强大的抗肿瘤功效,并通过增加肿瘤细胞凋亡和抑制肿瘤增殖来抑制癌细胞-巨噬细胞相互作用。 | |||
T10395L | Others | ||
ATM-3507 is an inhibitor of tropomyosin. In human melanoma cell lines, the IC50s are from 3.83-6.84 μM. | |||
T28206 | Apoptosis | ||
NSC49652 在神经元和黑色素瘤细胞中触发依赖于 p75NTR 和 JNK 活性的凋亡细胞死亡,并抑制黑色素瘤小鼠模型中的肿瘤生长。 | |||
T27792 | |||
L-Alaninol, an amino acid derivative, inhibits melanoma proliferation and increases cytrochrome C reductase and tau-glutamyl transpeptidase. | |||
T11854 | Others Antibacterial | ||
Lipofermata 是一种脂肪酸转运蛋白 2抑制剂,可阻止脂质转运至黑色素瘤细胞并减少黑色素瘤的生长和侵袭。 | |||
T35300 | Others | ||
Zeniplatin (Zeniplatinum) 是一种新顺铂复合物,具有抗癌活性,可用于治疗转移性黑色素瘤和肾癌。 | |||
T7712L | Others | ||
Disomotide TFA 181477-43-0(free base) 是一种用于治疗黑色素瘤的寡肽。 | |||
T28001 | Autophagy | ||
MDK-6983 (MDK-6983) 是一种自噬抑制剂,可破坏人黑色素瘤细胞中肌动蛋白细胞骨架的动力学。 | |||
T4745 | Others Endogenous Metabolite | ||
4-Carboxyquinoline (4-Quinolinecarboxylic acid) 是内源性代谢产物的一种。 | |||
T27454 | Raf | ||
GSK2008607是 一种有效的 B-RafV600E 抑制剂,具有抗癌活性,可用来研究乳腺癌、结直肠癌、黑色素瘤、甲状腺癌、卵巢癌。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPJ-01137 | MIA Protein, Human, Recombinant (His) | Human | E. coli | ||
Melanoma Inhibitory Activity Protein (MIA) is an autocrine growth regulatory protein secreted from chondrocytes and malignant melanoma cells, which was the first discovered member of a family of secreted cytokines termed the MIA/OTOR family. The four known members of this family: MIA, MIA2, OTOR and TANGO each contain a Src homology-3 (SH3)-like domain. MIA acts as a potent tumor cell growth inhibitor for malignant melanoma cells and some other neuroectodermal tumors, including gliomas, in an autocrine fashion and promotes melanoma metastasis by binding competitively to fibronectin and laminin in a manner that results in melanoma cell detachment from the extracellular matrix in vivo. The protein MIA has been shown to represent a very sensitive and specific serum marker for systemic malignant melanoma that might be useful for staging of primary melanomas, detection of progression from localized to metastatic disease during follow-up, and monitoring therapy of advanced melanomas. Elevated levels of MIA may represent a clinically useful marker for diagnosis of melanoma metastasis as well as a potential marker for rheumatoid arthritis.
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TMPY-01775 | AIM2 Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
AIM2, Absent In Melanoma 2 is a member of the interferon-inducible HIN-200 protein family that contains an amino-terminal pyrin domain and a carboxy-terminal oligonucleotide/oligosaccharide-binding domain, senses cytoplasmic DNA by means of its oligonucleotide/oligosaccharide-binding domain and interacts with ASC (apoptosis-associated speck-like protein containing a CARD) through its pyrin domain to activate caspase-1. In response to foreign cytoplasmic DNA, AIM2 forms an inflammasome, resulting in caspase activation in inflammatory cells. It had been pointed to a role of AIM2 function in both inflammation and cancer. AIM-2 antigen is expressed in a wide variety of tumor types, including neuroectodermal tumors, as well as breast, ovarian and colon carcinomas. AIM-2 could be used as a tumor antigen target for monitoring vaccine trials or to develop antigen specific active immunotherapy for glioma patients.
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TMPY-01034 | CD146/MCAM Protein, Human, Recombinant (His) | Human | HEK293 | ||
The CD146 antigen, also known as melanoma cell adhesion molecule (MCAM) and MUC18, is an integral membrane glycoprotein belonging to the immunoglobulin superfamily. CD146 contains the characteristic immunoglobulin-like domains (V-V-C2-C2-C2), a transmembrane region, and a short cytoplasmic tail. The CD146 expression is detected in endothelial cells in vascular tissue throughout the body and plays a role in cell adhesion, as well as in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. As a Ca2+-independent cell adhesion molecule involved in heterophilic cell to cell interactions and a surface receptor, CD146 triggers tyrosine phosphorylation of FYN and PTK2 and subsequently induced signal transduction, proteolysis, or immune recognition. This protein is also expressed predominantly on metastatic lesions and advanced primary tumors, and thus has been suggested to play an important role in tumor progression and the development of metastasis in certain human carcinomas.
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TMPY-00879 | CD146/MCAM Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
The CD146 antigen, also known as melanoma cell adhesion molecule (MCAM) and MUC18, is an integral membrane glycoprotein belonging to the immunoglobulin superfamily. CD146 contains the characteristic immunoglobulin-like domains (V-V-C2-C2-C2), a transmembrane region, and a short cytoplasmic tail. The CD146 expression is detected in endothelial cells in vascular tissue throughout the body and plays a role in cell adhesion, as well as in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. As a Ca2+-independent cell adhesion molecule involved in heterophilic cell to cell interactions and a surface receptor, CD146 triggers tyrosine phosphorylation of FYN and PTK2 and subsequently induced signal transduction, proteolysis, or immune recognition. This protein is also expressed predominantly on metastatic lesions and advanced primary tumors, and thus has been suggested to play an important role in tumor progression and the development of metastasis in certain human carcinomas.
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TMPY-06064 | CD146/MCAM Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
The CD146 antigen, also known as melanoma cell adhesion molecule (MCAM) and MUC18, is an integral membrane glycoprotein belonging to the immunoglobulin superfamily. CD146 contains the characteristic immunoglobulin-like domains (V-V-C2-C2-C2), a transmembrane region, and a short cytoplasmic tail. The CD146 expression is detected in endothelial cells in vascular tissue throughout the body and plays a role in cell adhesion, as well as in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. As a Ca2+-independent cell adhesion molecule involved in heterophilic cell to cell interactions and a surface receptor, CD146 triggers tyrosine phosphorylation of FYN and PTK2 and subsequently induced signal transduction, proteolysis, or immune recognition. This protein is also expressed predominantly on metastatic lesions and advanced primary tumors, and thus has been suggested to play an important role in tumor progression and the development of metastasis in certain human carcinomas.
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TMPH-01086 | CSPG4 Protein, Human, Recombinant (His & Myc) | Human | HEK293 | ||
Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades.
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TMPY-00008 | CXCL1 Protein, Rat, Recombinant | Rat | E. coli | ||
The Chemokine (C-X-C motif) Ligand 1, CXCL1, is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, GRO?, KC, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). CXCL1 already known to be important in osteoarthritis (OA), as a novel target gene of transcription factor AP-2? in chondrocytes and support the important role of AP-2? in cartilage. CXCL1 is a potent neutrophil chemoattractant with recognized roles in angiogenesis and inflammation. CXCL1 is a novel immediate PTH/PTHrP-responsive gene. CXCL1 may act as a chemoattractant for osteoclast precursors. CXCL1 may also have important pro-nociceptive effects via its direct actions on sensory neurons, and may induce long-term changes that involve protein synthesis. CXCL1 plays a critical nonredundant role in the development of experimental Lyme arthritis and carditis via CXCR2-mediated recruitment of neutrophils into the site of infection. CXCL1 functions through CXCR2 to transactivate the EGFR by proteolytic cleavage of HB-EGF, leading to activation of MAPK signalling and increased proliferation of epithelial ovarian cancer (EOC) cells. It might limit tumor growth by reinforcing senescence early in tumorigenesis. Thus, CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis.
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TMPK-01495 | HLA-A*01:01&B2M&MAGE-A3 (EVDPIGHLY) Monomer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
Melanoma antigen gene A3 (MAGE-A3) is one of the most immunogenic cancer testis antigens and is common in various types of cancers. MAGE-A3 can be considered as a predictor for poor prognosis and an option for vaccine immunotherapy in patients with PCa.
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TMPK-01493 | HLA-A*01:01&B2M&MAGE-A3 (EVDPIGHLY) Tetramer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
Melanoma antigen gene A3 (MAGE-A3) is one of the most immunogenic cancer testis antigens and is common in various types of cancers. MAGE-A3 can be considered as a predictor for poor prognosis and an option for vaccine immunotherapy in patients with PCa.
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TMPY-02502 | CD146/MCAM Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
The CD146 antigen, also known as melanoma cell adhesion molecule (MCAM) and MUC18, is an integral membrane glycoprotein belonging to the immunoglobulin superfamily. CD146 contains the characteristic immunoglobulin-like domains (V-V-C2-C2-C2), a transmembrane region, and a short cytoplasmic tail. The CD146 expression is detected in endothelial cells in vascular tissue throughout the body and plays a role in cell adhesion, as well as in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. As a Ca2+-independent cell adhesion molecule involved in heterophilic cell to cell interactions and a surface receptor, CD146 triggers tyrosine phosphorylation of FYN and PTK2 and subsequently induced signal transduction, proteolysis, or immune recognition. This protein is also expressed predominantly on metastatic lesions and advanced primary tumors, and thus has been suggested to play an important role in tumor progression and the development of metastasis in certain human carcinomas.
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TMPY-00433 | CXCL1 Protein, Mouse, Recombinant | Mouse | E. coli | ||
The Chemokine (C-X-C motif) Ligand 1, CXCL1, is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, GRO?, KC, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). CXCL1 already known to be important in osteoarthritis (OA), as a novel target gene of transcription factor AP-2? in chondrocytes and support the important role of AP-2? in cartilage. CXCL1 is a potent neutrophil chemoattractant with recognized roles in angiogenesis and inflammation. CXCL1 is a novel immediate PTH/PTHrP-responsive gene. CXCL1 may act as a chemoattractant for osteoclast precursors. CXCL1 may also have important pro-nociceptive effects via its direct actions on sensory neurons, and may induce long-term changes that involve protein synthesis. CXCL1 plays a critical nonredundant role in the development of experimental Lyme arthritis and carditis via CXCR2-mediated recruitment of neutrophils into the site of infection. CXCL1 functions through CXCR2 to transactivate the EGFR by proteolytic cleavage of HB-EGF, leading to activation of MAPK signalling and increased proliferation of epithelial ovarian cancer (EOC) cells. It might limit tumor growth by reinforcing senescence early in tumorigenesis. Thus, CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis.
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TMPK-01473 | HLA-A*24:02&B2M&MAGE-A3 (IMPKAGLLI) Monomer Protein, Human, MHC (His & Avi), Biotinylated | Human | HEK293 | ||
Melanoma antigen gene A3 (MAGE-A3) is one of the most immunogenic cancer testis antigens and is common in various types of cancers. MAGE-A3 can be considered as a predictor for poor prognosis and an option for vaccine immunotherapy in patients with PCa.
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TMPK-01472 | HLA-A*24:02&B2M&MAGE-A3 (IMPKAGLLI) Tetramer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
Melanoma antigen gene A3 (MAGE-A3) is one of the most immunogenic cancer testis antigens and is common in various types of cancers. MAGE-A3 can be considered as a predictor for poor prognosis and an option for vaccine immunotherapy in patients with PCa.
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TMPY-02026 | CXCL1 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
The Chemokine (C-X-C motif) Ligand 1, CXCL1, is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, GRO?, KC, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). CXCL1 already known to be important in osteoarthritis (OA), as a novel target gene of transcription factor AP-2? in chondrocytes and support the important role of AP-2? in cartilage. CXCL1 is a potent neutrophil chemoattractant with recognized roles in angiogenesis and inflammation. CXCL1 is a novel immediate PTH/PTHrP-responsive gene. CXCL1 may act as a chemoattractant for osteoclast precursors. CXCL1 may also have important pro-nociceptive effects via its direct actions on sensory neurons, and may induce long-term changes that involve protein synthesis. CXCL1 plays a critical nonredundant role in the development of experimental Lyme arthritis and carditis via CXCR2-mediated recruitment of neutrophils into the site of infection. CXCL1 functions through CXCR2 to transactivate the EGFR by proteolytic cleavage of HB-EGF, leading to activation of MAPK signalling and increased proliferation of epithelial ovarian cancer (EOC) cells. It might limit tumor growth by reinforcing senescence early in tumorigenesis. Thus, CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis.
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TMPY-02180 | CXCL1 Protein, Human, Recombinant (His & NusA) | Human | E. coli | ||
The Chemokine (C-X-C motif) Ligand 1, CXCL1, is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, GRO?, KC, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). CXCL1 already known to be important in osteoarthritis (OA), as a novel target gene of transcription factor AP-2? in chondrocytes and support the important role of AP-2? in cartilage. CXCL1 is a potent neutrophil chemoattractant with recognized roles in angiogenesis and inflammation. CXCL1 is a novel immediate PTH/PTHrP-responsive gene. CXCL1 may act as a chemoattractant for osteoclast precursors. CXCL1 may also have important pro-nociceptive effects via its direct actions on sensory neurons, and may induce long-term changes that involve protein synthesis. CXCL1 plays a critical nonredundant role in the development of experimental Lyme arthritis and carditis via CXCR2-mediated recruitment of neutrophils into the site of infection. CXCL1 functions through CXCR2 to transactivate the EGFR by proteolytic cleavage of HB-EGF, leading to activation of MAPK signalling and increased proliferation of epithelial ovarian cancer (EOC) cells. It might limit tumor growth by reinforcing senescence early in tumorigenesis. Thus, CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis.
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TMPY-02868 | CXCL1 Protein, Human, Recombinant | Human | E. coli | ||
The Chemokine (C-X-C motif) Ligand 1, CXCL1, is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, GRO?, KC, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). CXCL1 already known to be important in osteoarthritis (OA), as a novel target gene of transcription factor AP-2? in chondrocytes and support the important role of AP-2? in cartilage. CXCL1 is a potent neutrophil chemoattractant with recognized roles in angiogenesis and inflammation. CXCL1 is a novel immediate PTH/PTHrP-responsive gene. CXCL1 may act as a chemoattractant for osteoclast precursors. CXCL1 may also have important pro-nociceptive effects via its direct actions on sensory neurons, and may induce long-term changes that involve protein synthesis. CXCL1 plays a critical nonredundant role in the development of experimental Lyme arthritis and carditis via CXCR2-mediated recruitment of neutrophils into the site of infection. CXCL1 functions through CXCR2 to transactivate the EGFR by proteolytic cleavage of HB-EGF, leading to activation of MAPK signalling and increased proliferation of epithelial ovarian cancer (EOC) cells. It might limit tumor growth by reinforcing senescence early in tumorigenesis. Thus, CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis.
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TMPH-03526 | Cap8A Protein, S. aureus, Recombinant (His) | Staphylococcus aureus | in vitro E. coli expression system | ||
May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex.
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TMPJ-00011 | CXCL2 Protein, Mouse, Recombinant | Mouse | E. coli | ||
C-X-C motif chemokine 2 (CXCL2,MIP-2) belongs to the intercrine alpha (chemokine CxC) family. It was originally identified as a heparin-binding protein secreted from a murine macrophage cell line in response to endotoxin stimulation. The expression of mouse MIP-2 is stimulated by endotoxin. The mouse MIP-2 shares approximately 63% aa sequence identity with murine KC, another mouse alpha chemokine, which is induced by PDGF. It has been suggested that mouse KC and MIP-2 are the homologs of the human GROs and rat CINCs. Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst. The expression of MIP-2 was found to be associated with neutrophil influx in pulmonary inflammation and glomerulonephritis, suggesting that MIP-2 may contribute to the pathogenesis of inflammatory diseases.
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TMPY-03564 | TSPAN8 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Tetraspanin 8 (TSPAN8) as an important modulator of melanoma invasiveness, and several of its transcriptional regulators, which affect TSPAN8 expression during melanoma progression toward an invasive stage. p53 as a negative regulator of Tspan8 expression. p53 as a regulator of melanoma invasion and the concept that reactivating p53 could provide a strategy for modulating not only proliferative but also invasive capacity in melanoma treatment. Tetraspanin 8 (TSPAN8) is a tumor-associated antigen implicated in tumor progression and metastasis. TSPAN8 may play an important role in mCRC cell invasion. TSPAN8 was overexpressed in human gastric cancer tissues and gastric cancer cell lines compared with the normal. TSPAN8 overexpression promoted cell proliferation and invasion, while TSPAN8 suppression inhibited cell proliferation and invasion. TSPAN8 could activate the ERK MAPK pathway in gastric cancer cells, and MEK-ERK inhibition reversed the effects of TSPAN8 overexpression on cell proliferation and invasion.
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TMPY-02087 | IL-24 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interleukin-24 (IL-24) also known as Melanoma differentiation-associated gene 7 protein (MDA-7) is a member of the IL10 family of cytokines. IL-24/MDA-7/IL24 can induce apoptosis selectively in various cancer cells. Overexpression of IL-24 leads to elevated expression of several GADD family genes, which correlates with the induction of apoptosis. The phosphorylation of mitogen-activated protein kinase 14 (MAPK7/P38), and heat shock 27kDa protein 1 (HSPB2/HSP27) are found to be induced by this gene in melanoma cells, but not in normal immortal melanocytes. Human IL-24/MDA-7/IL24 is secreted by activated peripheral blood mononuclear cells and is the ligand for two heterodimeric receptors, IL-22R1/IL-20R2 and IL-20R1/IL-20R2. Northern blot analysis revealed IL-24/MDA-7/IL24 expression in human tissues associated with the immune system such as the spleen, thymus, peripheral blood leukocytes, and normal melanocytes. IL-24/MDA-7/IL24 binding to either its endogenous receptors on human keratinocytes or to ectopically expressed receptors on baby hamster kidney cells leads to activation of the signal transducers and activators of transcription.
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TMPY-02234 | CXCL9 Protein, Human, Recombinant | Human | E. coli | ||
Chemokine (C-X-C motif) ligand 9 (CXCL9), also known as Monokine induced by gamma interferon (MIG), is a small cytokine belonging to the CXC chemokine family. The function of this chemokine has not been specifically defined; however, it is thought to be involved in T cell trafficking. CXCL9/MIG functions as one of the three ligands of chemokine receptor CXCR3 which is a G protein-coupled receptor found predominantly on T cells. CXCL9/MIG, together with CXCL10 and CXCL11, may activate CXCR3 by binding to it. CXCL9 serves as a cytokine that affects the growth, movement, or activation state of cells that participate in immune and inflammatory response. It has been observed that tumour endothelial cells secrete high levels of CXCL9 in all, and CXCL10 in most melanoma metastases. Experiment data represent novel mechanisms by which tumour cells in melanoma metastases might use the chemokine-expressing endothelium to leave the tumour and eventually to form additional metastases at distinct sites. Experiment results also improved that CXCL9/MIG plays an important role in CD4+ T lymphocyte recruitment and development of CAV, MOMA-2+ macrophages are the predominant recipient-derived source of CXCL9/MIG, and recipient CD4 lymphocytes are necessary for sustained CXCL9/MIG production and CAV development in this model. Neutralization of the chemokine CXCL9/MIG may have therapeutic potential for the treatment of chronic rejection after heart transplantation.
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TMPY-00775 | DKK1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Dickkopf (DKK) family proteins, consisting of DKK-1, DKK-2, DKK-3 and DKK-4, function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5/6. DKK-1, DKK-2, and DKK-4 also bind cell surface Kremen-1 or Kremen-2 and promote the internalization of LRP5/6. Dickkopf related protein 1 (DKK-1) was initially identified as an inducer of head formation in Xenopus embryos. DKK-1 protein modulates Wnt signaling pathway during embryonic development. Increased levels of DKK-1 are found in the majority of lung cancers, esophageal squamous cell carcinomas, and hormone-resistant breast cancers, while DKK-1 expression is decreased in malignant melanoma and colorectal cancers.
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TMPY-04333 | LRRC15 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
LRRC15 (Leucine-Rich Repeat Containing 15) is a Protein Coding gene. 2 alternatively spliced human isoforms have been reported. The tumor antigen 15-leucine-rich repeat-containing membrane protein (LRRC15) is a transmembrane protein demonstrated to play important roles in cancer. LRRC15 is highly expressed in multiple solid tumor indications with limited normal tissue expression. It was expressed on stromal fibroblasts in many solid tumors (e.g., breast, head, and neck, lung, pancreatic) as well as directly on a subset of cancer cells of mesenchymal origin (e.g., sarcoma, melanoma, glioblastoma). The tumor antigen LRRC15, which is frequently overexpressed in multiple tumor types, as a repressor of cell death due to adenoviral p53.
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TMPY-04811 | DKK1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Dickkopf (DKK) family proteins, consisting of DKK-1, DKK-2, DKK-3 and DKK-4, function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5/6. DKK-1, DKK-2, and DKK-4 also bind cell surface Kremen-1 or Kremen-2 and promote the internalization of LRP5/6. Dickkopf related protein 1 (DKK-1) was initially identified as an inducer of head formation in Xenopus embryos. DKK-1 protein modulates Wnt signaling pathway during embryonic development. Increased levels of DKK-1 are found in the majority of lung cancers, esophageal squamous cell carcinomas, and hormone-resistant breast cancers, while DKK-1 expression is decreased in malignant melanoma and colorectal cancers.
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TMPY-01174 | DKK1 Protein, Rhesus, Recombinant (N256Q, His) | Rhesus | HEK293 | ||
Dickkopf (DKK) family proteins, consisting of DKK-1, DKK-2, DKK-3 and DKK-4, function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5/6. DKK-1, DKK-2, and DKK-4 also bind cell surface Kremen-1 or Kremen-2 and promote the internalization of LRP5/6. Dickkopf related protein 1 (DKK-1) was initially identified as an inducer of head formation in Xenopus embryos. DKK-1 protein modulates Wnt signaling pathway during embryonic development. Increased levels of DKK-1 are found in the majority of lung cancers, esophageal squamous cell carcinomas, and hormone-resistant breast cancers, while DKK-1 expression is decreased in malignant melanoma and colorectal cancers.
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TMPY-00502 | Glypican 3/GPC3 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Glypican-3, also known as Intestinal protein OCI-5, GPC3, and OCI5, is a member of the glypican family. It belongs to the glypican family and is highly expressed in the lung, liver, and kidney. It is a heparan sulfate proteoglycan, which is overexpressed in various neoplasms such as hepatocellular carcinoma, malignant melanoma, and testicular yolk sac tumor, and plays an important role in cell growth and differentiation. GPC3 function is tissue-dependent. In some tissues, GPC3 acts as a tumor suppressor gene, whereas in others, it acts as an oncofetal protein. Studies have shown that GPC3 is a reliable marker for hepatocellular carcinoma. The sensitivity and specificity exceed both alpha-fetoprotein and hepatocyte-paraffin1. GPC3 immunohistochemistry can aid in the differentiation of testicular germ cell tumors, being expressed in all yolk sac tumors but not in seminomas. GPC3 expression has also been identified in some squamous cell carcinomas of the lung and clear cell carcinomas of the ovary. The role of GPC3 in melanomas is still controversial. Thus, Glypican-3 is currently regarded as a tumor marker and potential target for immunotherapy.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01283 | Glypican 3/GPC3 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Glypican-3, also known as Intestinal protein OCI-5, GPC3, and OCI5, is a member of the glypican family. It belongs to the glypican family and is highly expressed in the lung, liver, and kidney. It is a heparan sulfate proteoglycan, which is overexpressed in various neoplasms such as hepatocellular carcinoma, malignant melanoma, and testicular yolk sac tumor, and plays an important role in cell growth and differentiation. GPC3 function is tissue-dependent. In some tissues, GPC3 acts as a tumor suppressor gene, whereas in others, it acts as an oncofetal protein. Studies have shown that GPC3 is a reliable marker for hepatocellular carcinoma. The sensitivity and specificity exceed both alpha-fetoprotein and hepatocyte-paraffin1. GPC3 immunohistochemistry can aid in the differentiation of testicular germ cell tumors, being expressed in all yolk sac tumors but not in seminomas. GPC3 expression has also been identified in some squamous cell carcinomas of the lung and clear cell carcinomas of the ovary. The role of GPC3 in melanomas is still controversial. Thus, Glypican-3 is currently regarded as a tumor marker and potential target for immunotherapy.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04962 | FAP Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Seprase, also known as 17 kDa melanoma membrane-bound gelatinase , Fibroblast activation protein alpha, Integral membrane serine protease and FAP, is a single-pass type II membrane protein which belongs to thepeptidase S9B family. Seprase / FAP is found in cell surface lamellipodia, invadopodia and on shed vesicles. Seprase / FAP appears to act as a proteolytically active 17-kDa dimer, consisting of two 97-kDa subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. Seprase / FAP colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Seprase / FAP colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. In association with DPP4, Seprase / FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. Seprase / FAP has a dual function in tumour progression. The proteolytic activity of Seprase has been shown to promote cell invasiveness towards the ECM and also to support tumour growth and proliferation. Seprase / FAP may have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02154 | FAP Protein, Human, Recombinant (His) | Human | HEK293 | ||
Seprase, also known as 17 kDa melanoma membrane-bound gelatinase , Fibroblast activation protein alpha, Integral membrane serine protease and FAP, is a single-pass type II membrane protein which belongs to thepeptidase S9B family. Seprase / FAP is found in cell surface lamellipodia, invadopodia and on shed vesicles. Seprase / FAP appears to act as a proteolytically active 17-kDa dimer, consisting of two 97-kDa subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. Seprase / FAP colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Seprase / FAP colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. In association with DPP4, Seprase / FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. Seprase / FAP has a dual function in tumour progression. The proteolytic activity of Seprase has been shown to promote cell invasiveness towards the ECM and also to support tumour growth and proliferation. Seprase / FAP may have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04922 | FAP Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
Seprase, also known as 17 kDa melanoma membrane-bound gelatinase , Fibroblast activation protein alpha, Integral membrane serine protease and FAP, is a single-pass type II membrane protein which belongs to thepeptidase S9B family. Seprase / FAP is found in cell surface lamellipodia, invadopodia and on shed vesicles. Seprase / FAP appears to act as a proteolytically active 17-kDa dimer, consisting of two 97-kDa subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. Seprase / FAP colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Seprase / FAP colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. In association with DPP4, Seprase / FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. Seprase / FAP has a dual function in tumour progression. The proteolytic activity of Seprase has been shown to promote cell invasiveness towards the ECM and also to support tumour growth and proliferation. Seprase / FAP may have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01923 | CD25/IL2R alpha Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05584 | CD25/IL2R alpha Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05090 | CD25/IL2R alpha Protein, Rat, Recombinant (His) | Rat | Baculovirus-Insect Cells | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01103 | CD25/IL2R alpha Protein, Human, Recombinant (His) | Human | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03776 | CD25/IL2R alpha Protein, Cynomolgus, Recombinant | Cynomolgus | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03644 | CD25/IL2R alpha Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05644 | CD25/IL2R alpha Protein, Rhesus, Recombinant (His & Avi), Biotinylated | Rhesus | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02457 | IL-2 Protein, Rat, Recombinant | Rat | E. coli | ||
Interleukin-2, also known as a T-cell growth factor, TCGF, Aldesleukin, and IL2, is a secreted protein that belongs to the IL-2 family. Interleukin-2 / IL-2 was the first interleukin molecule to be discovered. Interleukin-2 / IL-2 molecule was first purified to homogeneity by immunoaffinity chromatography by Kendall Smith and his team at Dartmouth Medical School. Interleukin-2 / IL-2 was also the first cytokine shown to mediate its effects via a specific IL-2 receptor, and it was also the first interleukin to be cloned and expressed from a complementary DNA (cDNA) library. Interleukin-2 / IL-2 was designated number 2 because Smith's data at the time indicated that IL-1, produced by macrophages, facilitates IL-2 production by T lymphocytes (T cells).Interleukin-2 / IL-2 is produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Interleukin-2 / IL-2 is normally produced by the body during an immune response. When environmental substances (molecules or microbes) gain access to the body, these substances (termed antigens) are recognized as foreign by antigen receptors that are expressed on the surface of lymphocytes. Antigen binding to the T cell receptor (TCR) stimulates the secretion of Interleukin-2 / IL-2 and the expression of IL-2 receptors IL-2R. The IL-2 / IL-2R interaction then stimulates the growth, differentiation, and survival of antigen-selected cytotoxic T cells via the activation of the expression of specific genes. Interleukin-2 / IL-2 can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells. The World Reference Standard for Interleukin-2 / IL-2 is produced by the National Institute of Biological Standards and Control in the UK. A recombinant form of Interleukin-2 / IL-2 for clinical use is manufactured by Chiron Corporation with the brand name Proleukin. It has been approved by the Food and Drug Administration (FDA) for the treatment of cancers (malignant melanoma, renal cell cancer), and is in clinical trials for the treatment of chronic viral infections, and as a booster (adjuvant) for vaccines. The use of Interleukin-2 / IL-2 in HIV therapy is ineffective.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02788 | IL-2 Protein, Mouse, Recombinant | Mouse | E. coli | ||
Interleukin-2, also known as a T-cell growth factor, TCGF, Aldesleukin, and IL2, is a secreted protein that belongs to the IL-2 family. Interleukin-2 / IL-2 was the first interleukin molecule to be discovered. Interleukin-2 / IL-2 molecule was first purified to homogeneity by immunoaffinity chromatography by Kendall Smith and his team at Dartmouth Medical School. Interleukin-2 / IL-2 was also the first cytokine shown to mediate its effects via a specific IL-2 receptor, and it was also the first interleukin to be cloned and expressed from a complementary DNA (cDNA) library. Interleukin-2 / IL-2 was designated number 2 because Smith's data at the time indicated that IL-1, produced by macrophages, facilitates IL-2 production by T lymphocytes (T cells).Interleukin-2 / IL-2 is produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Interleukin-2 / IL-2 is normally produced by the body during an immune response. When environmental substances (molecules or microbes) gain access to the body, these substances (termed antigens) are recognized as foreign by antigen receptors that are expressed on the surface of lymphocytes. Antigen binding to the T cell receptor (TCR) stimulates the secretion of Interleukin-2 / IL-2 and the expression of IL-2 receptors IL-2R. The IL-2 / IL-2R interaction then stimulates the growth, differentiation, and survival of antigen-selected cytotoxic T cells via the activation of the expression of specific genes. Interleukin-2 / IL-2 can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells. The World Reference Standard for Interleukin-2 / IL-2 is produced by the National Institute of Biological Standards and Control in the UK. A recombinant form of Interleukin-2 / IL-2 for clinical use is manufactured by Chiron Corporation with the brand name Proleukin. It has been approved by the Food and Drug Administration (FDA) for the treatment of cancers (malignant melanoma, renal cell cancer), and is in clinical trials for the treatment of chronic viral infections, and as a booster (adjuvant) for vaccines. The use of Interleukin-2 / IL-2 in HIV therapy is ineffective.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPK-00660 | AMIGO2 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Bromodomain and extraterminal domain inhibitors (BETi) represent promising therapeutic agents for metastatic melanoma, yet their mechanism of action remains unclear. Here we interrogated the transcriptional effects of BETi and identified AMIGO2, a transmembrane molecule, as a BET target gene essential for melanoma cell survival. AMIGO2 is upregulated in melanoma cells and tissues compared to human melanocytes and nevi, and AMIGO2 silencing in melanoma cells induces G1/S arrest followed by apoptosis.
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TMPK-01454 | HLA-A*02:01&B2M&PRAME (SLLQHLIGL) Tetramer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
PRAME (PReferentially expressed Antigen in MElanoma) is a melanoma-associated antigen expressed in cutaneous and ocular melanomas and some other malignant neoplasms, while its expression in normal tissue and benign tumors is limited.
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TMPK-01072 | AMIGO2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Bromodomain and extraterminal domain inhibitors (BETi) represent promising therapeutic agents for metastatic melanoma, yet their mechanism of action remains unclear. Here we interrogated the transcriptional effects of BETi and identified AMIGO2, a transmembrane molecule, as a BET target gene essential for melanoma cell survival. AMIGO2 is upregulated in melanoma cells and tissues compared to human melanocytes and nevi, and AMIGO2 silencing in melanoma cells induces G1/S arrest followed by apoptosis.
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TMPK-01469 | HLA-A*02:01&B2M&MART-1 (ELAGIGILTV) Monomer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
Melanoma antigen recognized by T cell-1 (Mart-1), one of the melanosome-specific proteins, also recognized by cytotoxicity T lymphocytes as a marker. Mart-1 is considered to play a critical role in the immunotherapy for melanoma.
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TMPK-01447 | HLA-A*02:01&B2M&PRAME (SLLQHLIGL) Monomer Protein, Human, MHC (His & Avi), Biotinylated | Human | HEK293 | ||
PRAME (PReferentially expressed Antigen in MElanoma) is a melanoma-associated antigen expressed in cutaneous and ocular melanomas and some other malignant neoplasms, while its expression in normal tissue and benign tumors is limited.
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TMPK-01441 | HLA-A*02:01&B2M&PRAME (ALYVDSLFFL) Monomer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
PRAME (PReferentially expressed Antigen in MElanoma) is a melanoma-associated antigen expressed in cutaneous and ocular melanomas and some other malignant neoplasms, while its expression in normal tissue and benign tumors is limited.
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TMPK-01455 | HLA-A*02:01&B2M&PRAME (SLLQHLIGL) Monomer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
PRAME (PReferentially expressed Antigen in MElanoma) is a melanoma-associated antigen expressed in cutaneous and ocular melanomas and some other malignant neoplasms, while its expression in normal tissue and benign tumors is limited.
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TMPK-01406 | HLA-A*02:01&B2M&PRAME (SLLQHLIGL) Tetramer Protein, Human, MHC (His & Avi), PE-Labeled | Human | HEK293 | ||
PRAME (PReferentially expressed Antigen in MElanoma) is a melanoma-associated antigen expressed in cutaneous and ocular melanomas and some other malignant neoplasms, while its expression in normal tissue and benign tumors is limited.
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TMPJ-01145 | ABCB5 Protein, Human, Recombinant (Trx) | Human | E. coli | ||
ATP-binding cassette sub-family B member 5(ABCB5) is a plasma membrane-spanning protein. ABCB5 is principally expressed in physiological skin and human malignant melanoma. ABCB5 has been suggested to regulate skin progenitor cell fusion and mediate chemotherapeutic drug resistance in stem-like tumor cell subpopulations in human malignant melanoma. It is commonly over-expressed on circulating melanoma tumour cells. Furthermore, the ABCB5+ melanoma- initiating cells were demonstrated to express FLT1 (VEGFR1) receptor tyrosine kinase which was functionally required for efficient xenograft tumor formation, as demonstrated by shRNA knockdown experiments.
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TMPK-01468 | HLA-A*02:01&B2M&MART-1 (ELAGIGILTV) Tetramer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
Melanoma antigen recognized by T cell-1 (Mart-1), one of the melanosome-specific proteins, also recognized by cytotoxicity T lymphocytes as a marker. Mart-1 is considered to play a critical role in the immunotherapy for melanoma.
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TMPY-03675 | TSPAN8 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
Tetraspanin 8 (TSPAN8) as an important modulator of melanoma invasiveness, and several of its transcriptional regulators, which affect TSPAN8 expression during melanoma progression toward an invasive stage. p53 as a negative regulator of Tspan8 expression. p53 as a regulator of melanoma invasion and the concept that reactivating p53 could provide a strategy for modulating not only proliferative but also invasive capacity in melanoma treatment. Tetraspanin 8 (TSPAN8) is a tumor-associated antigen implicated in tumor progression and metastasis. TSPAN8 may play an important role in mCRC cell invasion. TSPAN8 was overexpressed in human gastric cancer tissues and gastric cancer cell lines compared with the normal. TSPAN8 overexpression promoted cell proliferation and invasion, while TSPAN8 suppression inhibited cell proliferation and invasion. TSPAN8 could activate the ERK MAPK pathway in gastric cancer cells, and MEK-ERK inhibition reversed the effects of TSPAN8 overexpression on cell proliferation and invasion.
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