目录号 | 产品详情 | 靶点 | |
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T1602 | Mitophagy Gamma-secretase HIV Protease GABA Receptor HDAC Autophagy | ||
Valproic acid sodium salt (Sodium Valproate) 是一种HDAC 抑制剂,可抑制HDAC1的活性,诱导HDAC2的降解。它激活Notch1信号并抑制小细胞肺癌细胞的增殖。它可研究癫痫、偏头痛和双相情感障碍等。 | |||
T7064 | Mitophagy Gamma-secretase HIV Protease GABA Receptor Sodium Channel HDAC Autophagy | ||
Valproic Acid (2-Propylpentanoic Acid) 是一种 HDAC 抑制剂,可抑制 HDAC1 活性,诱导 HDAC2 降解,具有口服活性。Valproic Acid 可以用于癫痫和躁郁症的研究。 | |||
T6474 | HDAC | ||
Divalproex Sodium (Valproate semisodium) 结合并抑制 γ-氨基丁酸 (GABA) 转氨酶,其抗惊厥活性可通过增加 GABA 脑浓度和抑制分解 GABA 或阻止 GABA 再摄取到神经胶质和神经末梢的酶来发挥。它也是一种 HDAC 抑制剂。由丙戊酸钠和丙戊酸组成,具有抗惊厥和抗癫痫活性。 Divalproex 还可以通过抑制电压敏感的钠通道来抑制重复的神经元放电。 | |||
TP1540 | Gamma-secretase | ||
Jagged-1 (188-204) 是 JAG-1 蛋白的一个片段。其中 JAG-1 能够诱导单核细胞衍生的人树突状细胞成熟,是一种在培养的和原发性多发性骨髓瘤细胞中高度表达的 Notch 配体。 | |||
T3521 | Beta Amyloid Gamma-secretase | ||
γ-Secretase-IN-1 是一种高效的 γ-secretase 抑制剂,对T-47D 细胞显示部分抗增殖活性且抑制 β-amyloid(40),β-amyloid(42),和Notch γ-分泌酶裂解。 | |||
T14680 | Gamma-secretase | ||
BMS-906024 (Osugacestat) 是一种可口服且具有选择性的γ 分泌酶抑制剂,是一种小分子 Notch 抑制剂。BMS-906024 对多种人类癌症异种移植具有广谱抗肿瘤活性。BMS-906024 可阻止所有四种 Notch 受体的激活,对 Notch1、-2、-3 和 -4 受体的 IC50 分别为 1.6、0.7、3.4 和 2.9 nM。 | |||
T31987 | Wnt/beta-catenin Gamma-secretase | ||
Gossypolone 是一种棉酚主要代谢物。 Gossypolone 减少 Notch/Wnt 信号并诱导细胞凋亡。 | |||
T9015 | Gamma-secretase | ||
LY900009 是一种通过选择性抑制 γ-分泌酶蛋白来抑制 Notch 信号传导的小分子抑制剂。 | |||
T24159 | Smo | ||
IHR-1 是一种Smo 拮抗剂,不能透过细胞膜。 | |||
T21890 | Gamma-secretase | ||
JLK-6 是一种γ分泌酶抑制剂,选择性作用于 HEK293细胞的淀粉样β前体蛋白(APP)的γ-分泌酶裂解 APP,抑制 Aβ的生成,但对不 Notch 受体的裂解无影响。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-05054 | Notch 4 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
NOTCH4 (Notch Receptor 4) is a Protein Coding gene. Notch4 belongs to a family of transmembrane receptors that play an important role in vascular development and maintenance. The NOTCH4 gene is located at 6p21.3 and is involved in the development and patterning of the central nervous systems. It regulates signaling pathways associated with neuronal maturation, a process involved in the development and patterning of the central nervous system. The NOTCH4 gene has also been identified as a possible susceptibility gene for schizophrenia (SCZ). It is broadly expressed in fat, lung, and other tissues. The NOTCH4 gene, located within the MHC region, is involved in cellular differentiation and has varying effects dependent on tissue type.
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TMPY-05081 | Notch 1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
NOTCH1 is one of the four mammalian Notch receptors, which is involved in the Notch signaling pathway. Specifically, NOTCH1 promotes the proliferation of myogenic precursor cells, and the NICD domain of NOTCH1 can impair the regeneration of skeletal muscles.NOTCH1 is a prevalent signaling pathway in T cell acute lymphoblastic leukemia (T-ALL). The NOTCH signaling pathway is a conserved signaling cascade that regulates many aspects of development and homeostasis in multiple organ systems. The proto-oncogene NOTCH1 is frequently mutated in around 10% of patients with chronic lymphocytic leukemia (CLL). NOTCH1 mutations in oral squamous cell carcinoma (OSCC) frequently occur near the ligand-binding region. These mutations change the domain structure of this protein and affect the ligand-binding activity. When NOTCH1 is activated by ligand binding, the NOTCH1 intracellular domain (NICD) is cleaved from the cell membrane.
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TMPK-01396 | Notch 3 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Human Notch-3 is part of the Notch family of type I transmembrane glycoproteins involved in a number of early-event developmental processes. The extracellular domain of Notch receptors interact with the extracellular domain of transmembrane ligands Jagged, Delta, and Serrate expressed on the surface of a neighboring cell. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs.
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TMPK-01374 | Notch 3 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Human Notch-3 is part of the Notch family of type I transmembrane glycoproteins involved in a number of early-event developmental processes. The extracellular domain of Notch receptors interact with the extracellular domain of transmembrane ligands Jagged, Delta, and Serrate expressed on the surface of a neighboring cell. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs
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TMPY-04930 | Notch 2 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
NOTCH2 (Notch Receptor 2) is a Protein Coding gene. This gene encodes a member of the Notch family. Members of this Type 1 transmembrane protein family share structural characteristics and play a role in a variety of developmental processes by controlling cell fate decisions. Hajdu Cheney Syndrome (HCS) is a rare disease associated with mutations of NOTCH2 that lead to the translation of a truncated, presumably stable, NOTCH2 protein. NOTCH2 is down-regulated in colon cancer, and reduced expression is associated with a less differentiated, more aggressive phenotype, and reduced overall survival. NOTCH2 has also been shown to have pro-apoptotic and growth-suppressive effects in thyroid carcinoma, and carcinoid tumors. NOTCH2 acts as an oncogene that promotes bladder cancer growth and metastasis through EMT, cell-cycle progression, and maintenance of stemness.
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TMPK-01360 | Notch 3 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Human Notch-3 is part of the Notch family of type I transmembrane glycoproteins involved in a number of early-event developmental processes. The extracellular domain of Notch receptors interact with the extracellular domain of transmembrane ligands Jagged, Delta, and Serrate expressed on the surface of a neighboring cell. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs
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TMPK-01367 | Notch 3 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Human Notch-3 is part of the Notch family of type I transmembrane glycoproteins involved in a number of early-event developmental processes. The extracellular domain of Notch receptors interact with the extracellular domain of transmembrane ligands Jagged, Delta, and Serrate expressed on the surface of a neighboring cell. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs
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TMPK-00868 | Notch 4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
The Notch signaling pathway is important for cell-cell communication; it is involved in gene regulation mechanisms that control multiple cell differentiation processes during embryonic and adult life. Notch-4 expression correlates with Ki67. Notch-4 also plays a key role in breast cancer stem-like cells.
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TMPK-00465 | Notch 2 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Human Notch 2 is a 300 kDa type I transmembrane glycoprotein that is one of four human Notch homologues involved in developmental processes. Although Notch proteins are structurally and functionally similar, deletion of either Notch-1 or Notch 2 is lethal, showing that not all functions overlap.Notch 2 functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus.
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TMPK-00467 | Notch 1 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Human Notch-1 is a 300 kDa type I transmembrane glycoprotein that is one of four human Notch homologues involved in developmental processes.Notch-1 functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs.
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TMPY-00415 | Notch 1 Protein, Mouse, Recombinant (hFc) | Mouse | CHO | ||
NOTCH1 is one of the four mammalian Notch receptors, which is involved in the Notch signaling pathway. Specifically, NOTCH1 promotes the proliferation of myogenic precursor cells, and the NICD domain of NOTCH1 can impair the regeneration of skeletal muscles.NOTCH1 is a prevalent signaling pathway in T cell acute lymphoblastic leukemia (T-ALL). The NOTCH signaling pathway is a conserved signaling cascade that regulates many aspects of development and homeostasis in multiple organ systems. The proto-oncogene NOTCH1 is frequently mutated in around 10% of patients with chronic lymphocytic leukemia (CLL). NOTCH1 mutations in oral squamous cell carcinoma (OSCC) frequently occur near the ligand-binding region. These mutations change the domain structure of this protein and affect the ligand-binding activity. When NOTCH1 is activated by ligand binding, the NOTCH1 intracellular domain (NICD) is cleaved from the cell membrane.
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TMPY-02663 | Notch 1 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
NOTCH1 is one of the four mammalian Notch receptors, which is involved in the Notch signaling pathway. Specifically, NOTCH1 promotes the proliferation of myogenic precursor cells, and the NICD domain of NOTCH1 can impair the regeneration of skeletal muscles.NOTCH1 is a prevalent signaling pathway in T cell acute lymphoblastic leukemia (T-ALL). The NOTCH signaling pathway is a conserved signaling cascade that regulates many aspects of development and homeostasis in multiple organ systems. The proto-oncogene NOTCH1 is frequently mutated in around 10% of patients with chronic lymphocytic leukemia (CLL). NOTCH1 mutations in oral squamous cell carcinoma (OSCC) frequently occur near the ligand-binding region. These mutations change the domain structure of this protein and affect the ligand-binding activity. When NOTCH1 is activated by ligand binding, the NOTCH1 intracellular domain (NICD) is cleaved from the cell membrane.
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TMPJ-01452 | Notch 1 Protein, Mouse, Recombinant (aa 18-526, His) | Mouse | Human Cells | ||
Mouse Notch1 is a 300 kDa type I transmembrane glycoprotein and it functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Mouse Notch1 is synthesized as a 2531 amino acid (aa) precursor that contains an 18 aa signal sequence, a 1707 aa extracellular domain (ECD) with 36 EGFlike repeats and three Lin12/notch repeats, a 21 aa transmembrane segment and a 785 aa cytoplasmic domain that contains six ankyrin repeats, a glutamine-rich domain and a PEST sequence. Notch1 may play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation and may be involved in mesoderm development, somite formation and neurogenesis.
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TMPK-00466 | Notch 2 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Human Notch-2 is a 300 kDa type I transmembrane glycoprotein that is one of four human Notch homologues involved in developmental processes. Although Notch proteins are structurally and functionally similar, deletion of either Notch-1 or Notch-2 is lethal, showing that not all functions overlap.Notch-2 functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus.
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TMPK-00468 | Notch 1 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Human Notch-1 is a 300 kDa type I transmembrane glycoprotein that is one of four human Notch homologues involved in developmental processes.Notch-1 functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs.
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TMPY-05028 | NOTCH2NL Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
NOTCH2NLA (Notch 2 N-Terminal Like A) is a Protein Coding gene. NOTCH2NL, human-specific paralogs of the NOTCH2 receptor, stood out for their ability to promote cortical progenitor maintenance. It belongs to the NOTCH family. NOTCH2NL promote the clonal expansion of human cortical progenitors, ultimately leading to higher neuronal output. At the molecular level, NOTCH2NL function by activating the Notch pathway through inhibition of cis Delta/Notch interactions. NOTCH2NL ectopic expression delays differentiation of neuronal progenitors, while deletion accelerates differentiation into cortical neurons. The emergence of human-specific NOTCH2NL genes may have contributed to the rapid evolution of the larger human neocortex, accompanied by loss of genomic stability at the 1q21.1 locus and resulting recurrent neurodevelopmental disorders.
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TMPK-00360 | DLL4 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Delta-like protein 4 (DLL4) is a type I membrane protein belonging to the Delta/Serrate/Lag2 (DSL) family of Notch ligands. Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Essential for retinal progenitor proliferation. Required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types (By similarity). During spinal cord neurogenesis, inhibits V2a interneuron fate.
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TMPH-01783 | NOTCH2NLB Protein, Human, Recombinant (His & Myc) | Human | Baculovirus | ||
Human-specific protein that promotes neural progenitor proliferation and evolutionary expansion of the brain neocortex by regulating the Notch signaling pathway. Able to promote neural progenitor self-renewal, possibly by down-regulating neuronal differentiation genes, thereby delaying the differentiation of neuronal progenitors and leading to an overall final increase in neuronal production. Acts by enhancing the Notch signaling pathway via two different mechanisms that probably work in parallel to reach the same effect. Enhances Notch signaling pathway in a non-cell-autonomous manner via direct interaction with NOTCH2. Also promotes Notch signaling pathway in a cell-autonomous manner through inhibition of cis DLL1-NOTCH2 interactions, which promotes neuronal differentiation.
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TMPH-01784 | NOTCH2NLB Protein, Human, Recombinant (E. coli, His & Myc) | Human | E. coli | ||
Human-specific protein that promotes neural progenitor proliferation and evolutionary expansion of the brain neocortex by regulating the Notch signaling pathway. Able to promote neural progenitor self-renewal, possibly by down-regulating neuronal differentiation genes, thereby delaying the differentiation of neuronal progenitors and leading to an overall final increase in neuronal production. Acts by enhancing the Notch signaling pathway via two different mechanisms that probably work in parallel to reach the same effect. Enhances Notch signaling pathway in a non-cell-autonomous manner via direct interaction with NOTCH2. Also promotes Notch signaling pathway in a cell-autonomous manner through inhibition of cis DLL1-NOTCH2 interactions, which promotes neuronal differentiation.
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TMPY-01321 | DLL4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Delta-like protein 4 (DLL4, Delta4), a type I membrane-bound Notch ligand, is one of five known Notch ligands in mammals and interacts predominantly with Notch 1, which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth, forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore, the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions, such as cancer, DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis, but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies, blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density, yet causes marked growth inhibition due to functionally defective vasculature. Thus, DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy.
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TMPY-01379 | DLL1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Delta-like protein 1(DLL1), also known as Delta1, a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains, acts as a ligand for Notch receptors, and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor, and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway, whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells, DLL1 is constitutively cleaved by ADAM12, and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent, takes place in cis orientation, and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1, but not its N- or C-terminal proteolytic fragment, co-immunoprecipitates with ADAM12. By using a Notch reporter construct, we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore, ADAM9 and ADAM17 have the ability to process DLL1. In contrast, ADAM15 does not cleave DLL1, although the two proteins still co-immunoprecipitate with each other. During fetal development, DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries.
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TMPY-05833 | DLL1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Delta-like protein 1(DLL1), also known as Delta1, a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains, acts as a ligand for Notch receptors, and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor, and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway, whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells, DLL1 is constitutively cleaved by ADAM12, and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent, takes place in cis orientation, and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1, but not its N- or C-terminal proteolytic fragment, co-immunoprecipitates with ADAM12. By using a Notch reporter construct, we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore, ADAM9 and ADAM17 have the ability to process DLL1. In contrast, ADAM15 does not cleave DLL1, although the two proteins still co-immunoprecipitate with each other. During fetal development, DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries.
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TMPY-01915 | DLL1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Delta-like protein 1(DLL1), also known as Delta1, a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains, acts as a ligand for Notch receptors, and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor, and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway, whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells, DLL1 is constitutively cleaved by ADAM12, and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent, takes place in cis orientation, and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1, but not its N- or C-terminal proteolytic fragment, co-immunoprecipitates with ADAM12. By using a Notch reporter construct, we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore, ADAM9 and ADAM17 have the ability to process DLL1. In contrast, ADAM15 does not cleave DLL1, although the two proteins still co-immunoprecipitate with each other. During fetal development, DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries.
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TMPY-04803 | DLL4 Protein, Human, Recombinant | Human | HEK293 | ||
Delta-like protein 4 (DLL4, Delta4), a type I membrane-bound Notch ligand, is one of five known Notch ligands in mammals and interacts predominantly with Notch 1, which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth, forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore, the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions, such as cancer, DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis, but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies, blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density, yet causes marked growth inhibition due to functionally defective vasculature. Thus, DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy.
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TMPY-00776 | DLL4 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Delta-like protein 4 (DLL4, Delta4), a type I membrane-bound Notch ligand, is one of five known Notch ligands in mammals and interacts predominantly with Notch 1, which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth, forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore, the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions, such as cancer, DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis, but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies, blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density, yet causes marked growth inhibition due to functionally defective vasculature. Thus, DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy.
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TMPY-01337 | DLL4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Delta-like protein 4 (DLL4, Delta4), a type I membrane-bound Notch ligand, is one of five known Notch ligands in mammals and interacts predominantly with Notch 1, which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth, forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore, the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions, such as cancer, DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis, but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies, blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density, yet causes marked growth inhibition due to functionally defective vasculature. Thus, DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy.
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TMPY-01475 | Jagged 1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Protein Jagged 1, also known as JAG1, JAGL1, and CD339, is a single-pass type I membrane protein that contains 1 DSL domain and 15 EGF-like domains. JAG1/Jagged 1 is widely expressed in adult and fetal tissues. The expression of JAG1/Jagged 1 is up-regulated in cervical squamous cell carcinoma. JAG1/Jagged 1 is also expressed in bone marrow cell line HS-27a which supports the long-term maintenance of immature progenitor cells. JAG1/Jagged 1 is a ligand for multiple Notch receptors. It is involved in the mediation of Notch signaling. JAG1/Jagged 1 may be involved in cell-fate decisions during hematopoiesis. JAG1/Jagged 1 seems to be involved in the early and late stages of mammalian cardiovascular development. It inhibits myoblast differentiation and enhances fibroblast growth factor-induced angiogenesis. Defects in JAG1/Jagged 1 are the cause of Alagille syndrome type 1 (ALGS1). Alagille syndrome is an autosomal dominant multisystem disorder defined clinically by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations. Defects in JAG1/Jagged 1 are also a cause of tetralogy of Fallot (TOF). TOF is a congenital heart anomaly that consists of pulmonary stenosis, ventricular septal defect, dextroposition of the aorta (aorta is on the right side instead of the left), and hypertrophy of the right ventricle. This condition results in a blue baby at birth due to inadequate oxygenation.
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TMPY-02123 | DLL1 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Delta-like protein 1(DLL1), also known as Delta1, a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains, acts as a ligand for Notch receptors, and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor, and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway, whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells, DLL1 is constitutively cleaved by ADAM12, and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent, takes place in cis orientation, and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1, but not its N- or C-terminal proteolytic fragment, co-immunoprecipitates with ADAM12. By using a Notch reporter construct, we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore, ADAM9 and ADAM17 have the ability to process DLL1. In contrast, ADAM15 does not cleave DLL1, although the two proteins still co-immunoprecipitate with each other. During fetal development, DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries.
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TMPY-04098 | DLL1 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
Delta-like protein 1(DLL1), also known as Delta1, a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains, acts as a ligand for Notch receptors, and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor, and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway, whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells, DLL1 is constitutively cleaved by ADAM12, and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent, takes place in cis orientation, and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1, but not its N- or C-terminal proteolytic fragment, co-immunoprecipitates with ADAM12. By using a Notch reporter construct, we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore, ADAM9 and ADAM17 have the ability to process DLL1. In contrast, ADAM15 does not cleave DLL1, although the two proteins still co-immunoprecipitate with each other. During fetal development, DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries.
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TMPH-02854 | Jagged 1 Protein, Mouse, Recombinant (His & Myc & SUMO) | Mouse | E. coli | ||
Ligand for multiple Notch receptors and involved in the mediation of Notch signaling. May be involved in cell-fate decisions during hematopoiesis. Seems to be involved in early and late stages of mammalian cardiovascular development. Inhibits myoblast differentiation. May regulate fibroblast growth factor-induced angiogenesis.
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TMPY-06876 | DLL4 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Delta-like protein 4 (DLL4, Delta4), a type I membrane-bound Notch ligand, is one of five known Notch ligands in mammals and interacts predominantly with Notch 1, which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth, forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore, the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions, such as cancer, DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis, but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies, blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density, yet causes marked growth inhibition due to functionally defective vasculature. Thus, DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy.
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TMPY-05796 | DLL4 Protein, Mouse, Recombinant (mFc) | Mouse | HEK293 | ||
Delta-like protein 4 (DLL4, Delta4), a type I membrane-bound Notch ligand, is one of five known Notch ligands in mammals and interacts predominantly with Notch 1, which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth, forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore, the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions, such as cancer, DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis, but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies, blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density, yet causes marked growth inhibition due to functionally defective vasculature. Thus, DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy.
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TMPY-05093 | DLL4 Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
Delta-like protein 4 (DLL4, Delta4), a type I membrane-bound Notch ligand, is one of five known Notch ligands in mammals and interacts predominantly with Notch 1, which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth, forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore, the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions, such as cancer, DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis, but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies, blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density, yet causes marked growth inhibition due to functionally defective vasculature. Thus, DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy.
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TMPK-00945 | ASPH Protein, Human, Recombinant (His) | Human | E. coli | ||
Aspartate β-hydroxylase (ASPH) is silent in normal adult tissues only to re-emerge during oncogenesis where its function is required for generation and maintenance of malignant phenotypes. Exosomes enable prooncogenic secretome delivering and trafficking for long-distance cell-to-cell communication.Expression profiling of Notch signaling components positively correlates with ASPH expression in breast cancer patients, confirming that ASPH-Notch axis acts functionally in breast tumorigenesis.
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TMPK-01083 | ASPH Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Aspartate β-hydroxylase (ASPH) is silent in normal adult tissues only to re-emerge during oncogenesis where its function is required for generation and maintenance of malignant phenotypes. Exosomes enable prooncogenic secretome delivering and trafficking for long-distance cell-to-cell communication.Expression profiling of Notch signaling components positively correlates with ASPH expression in breast cancer patients, confirming that ASPH-Notch axis acts functionally in breast tumorigenesis.
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TMPH-01369 | PSENEN Protein, Human, Recombinant (His) | Human | in vitro E. coli expression system | ||
Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (Probable). PSENEN modulates both endoproteolysis of presenilin and gamma-secretase activity.
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TMPK-01208 | DLL3 Protein, Human, Recombinant (His & Flag) | Human | HEK293 | ||
Delta-like protein 3 (DLL3) is a transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. DLL3 inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
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TMPY-03276 | BLBP Protein, Human, Recombinant | Human | E. coli | ||
BLBP, also known as FABP7, is a brain fatty acid binding protein. Fatty acid binding proteins (FABPs) are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP7 binds DHA with the highest affinity among all of the FABPs. FABPs may play roles in fatty acid uptake, transport, and metabolism. BLBP is expressed, during development, in radial glia by the activation of notch receptors. It was shown that reelin induces FABP7 expression in neural progenitor cells via notch-1 activation. BLBP variation is linked to weak prepulse inhibition(PPI) in mice and deficit in PPI is an endophenotypic trait observed in schizophrenia patients and their relatives.
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TMPK-01207 | DLL3 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Delta-like protein 3 (DLL3) is a transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. DLL3 inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
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TMPK-00748 | DLL3 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Delta-like protein 3 (DLL3) is a transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. DLL3 inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
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TMPH-01654 | MAGEA1 Protein, Human, Recombinant (His) | Human | Yeast | ||
May be involved in transcriptional regulation through interaction with SNW1 and recruiting histone deactelyase HDAC1. May inhibit notch intracellular domain (NICD) transactivation. May play a role in embryonal development and tumor transformation or aspects of tumor progression. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes.
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TMPK-00542 | DLL3 Protein, Cynomolgus, Recombinant (aa 27-488, His) | Cynomolgus | HEK293 | ||
Delta-like protein 3 (DLL3) is a transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. DLL3 inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
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TMPK-01209 | DLL3 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Delta-like protein 3 (DLL3) is a transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. DLL3 inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
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TMPK-01210 | DLL3 Protein (Primary Amine Labeling), Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
Delta-like protein 3 (DLL3) is a transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. DLL3 inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
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TMPY-03308 | ADAM17 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
ADAM17 is a member of the ADAM protein family of disintegrins and metalloproteases. ADAM17 is ubiquitously expressed in the human colon, with increased activity in the colonic mucosa of patients with ulcerative colitis, a main form of inflammatory bowel disease. The expression of ADAM17 may be inhibited by ethanol. It is involved in the processing of tumor necrosis factor alpha (TNF-α) at the surface of the cell, and from within the intracellular membranes of the trans-Golgi network. ADAM17 also plays a role in the release of a diverse variety of membrane-anchored cytokines, cell adhesion molecules, receptors, ligands, and enzymes. ADAM17 may play a prominent role in the Notch signaling pathway, during the proteolytic release of the Notch intracellular domain (from the Notch1 receptor) that occurs following ligand binding.
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TMPK-01206 | DLL3 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Delta-like protein 3 (DLL3) is a transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. DLL3 inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
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TMPK-00543 | DLL3 Protein, Cynomolgus, Recombinant (aa 27-477, His) | Cynomolgus | HEK293 | ||
Delta-like protein 3 (DLL3) is a transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. DLL3 inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
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TMPK-00640 | DLL3 Protein, Rhesus macaque, Recombinant (His) | Rhesus macaque | HEK293 | ||
Delta-like protein 3 (DLL3) is a transmembrane protein that belongs to the Delta/Serrate/Lag-2 (DSL) family of Notch ligands. DLL3 inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
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TMPK-01030 | LRRN1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Lrrn1 is required for the formation of MHB--loss of function leads to a loss of the morphological constriction and loss of Fgf8. Cells overexpressing Lrrn1 violate the boundary and result in a loss of cell restriction between midbrain and hindbrain compartments. Lrrn1 also regulates the glycosyltransferase Lunatic Fringe, a modulator of Notch signalling, maintaining its expression in midbrain cells which is instrumental in MHB boundary formation.
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TMPH-02316 | YJEFN3 Protein, Human, Recombinant | Human | E. coli | ||
May accelerate cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis. May orchestrate hematopoietic stem and progenitor cell emergence from the hemogenic endothelium, a type of specialized endothelium manifesting hematopoietic potential. YJEFN3-mediated cholesterol efflux activates endothelial SREBF2, the master transcription factor for cholesterol biosynthesis, which in turn transactivates NOTCH and promotes hematopoietic stem and progenitor cell emergence. May play a role in spermiogenesis and oogenesis.
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