目录号 | 产品详情 | 靶点 | |
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T3876 | PAI-1 ERK Potassium Channel JNK | ||
Loureirin B 是从剑叶龙血树中分离到的一种黄酮,是 PAI-1抑制剂,IC50值为 26.10 μM。它抑制 KATP,以及 ERK 和 JNK 的磷酸化,具有抗糖尿病的功效。 | |||
TN1721 | ERK p38 MAPK Calcium Channel NF-κB ROS | ||
Gypenoside L 是存在于绞股蓝中的一种皂苷,可增加 SA-β-半乳糖苷酶活性,促进衰老相关分泌细胞因子的产生。它还可以激活p38和ERK MAPK 通路和NF-κB 通路以诱导衰老,具有抗肿瘤和抗炎活性。 | |||
T1842 | ERK | ||
XMD17-109 (ERK5-IN-1) 是一种特异性的ERK-5抑制剂,在 HEK293 细胞系中的EC50为 4.2 μM。 | |||
T2029 | ERK CDK | ||
Bohemine 是一种合成的选择性CDK 抑制剂,是嘌呤类似物,具有抗癌活性。它对Cdk2/cyclin E、Cdk2/cyclin A 和Cdk9/cyclin T1的IC50分别为 4.6 μM、83 μM 和 2.7 μM。 | |||
T7506 | Piezo Channel | ||
Yoda 1 是Piezo1激动剂,能够激活纯化的 Piezo1 通道。 | |||
T4496 | ERK Trk receptor Akt | ||
LM22B-10 是TrkB/TrkC 神经营养因子受体激活剂,诱导体内外TrkB、TrkC、AKT 和ERK 的活化。 | |||
T5727 | ERK NF-κB COX PGE Synthase | ||
Cafestol 是咖啡特有的一种二萜,可靶向 AP-1 抑制ERK,有化学预防、抗肿瘤、保肝、抗氧化和抗炎作用。它通过抑制NF-kB 活化途径强烈的抑制 PGE2的产生,还抑制 LGE 激活的 RAW264.7 细胞中的PGE2产生和环氧合酶(COX-2)的 mRNA 表达。 | |||
T6S0619 | ERK Akt | ||
Pachymic acid (3-O-Acetyltumulosic acid) 是来自茯苓的一种三萜,可抑制Akt 和ERK 信号传导途径。 | |||
TMS2181 | ERK MEK Endogenous Metabolite | ||
trans-Zeatin ((E)-Zeatin) 是植物细胞分裂素,可抑制紫外线诱导的MEK/ERK 的活化,在细胞生长、分化和分裂中起着重要的作用。 | |||
T14042 | Melatonin Receptor MT Receptor | ||
4-P-PDOT (4-phenyl-2- propionamidotetralin) 是一种选择性和亲和性的褪黑激素受体拮抗剂,可显著抵消褪黑激素介导的抗氧化作用。它对MT2的选择性是 MT1 的 300 倍以上。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-04539 | ERK2 Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
ERK2 Protein, Human, Recombinant (GST) is expressed in Baculovirus insect cells with GST tag. The predicted molecular weight is 67 kDa and the accession number is P28482-1.
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TMPY-04571 | ERK2 Protein, Mouse, Recombinant (His & GST) | Mouse | Baculovirus Insect Cells | ||
ERK2 Protein, Mouse, Recombinant (His & GST) is expressed in Baculovirus insect cells with His and GST tag. The predicted molecular weight is 69.1 kDa and the accession number is P63085.
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TMPY-04430 | p38 gamma/MAPK12 Protein, Human, Recombinant | Human | Baculovirus Insect Cells | ||
p38 gamma/MAPK12 Protein, Human, Recombinant is expressed in Baculovirus insect cells. The predicted molecular weight is 42.1 kDa and the accession number is P53778.
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TMPY-04429 | p38 gamma/MAPK12 Protein, Human, Recombinant (His & GST) | Human | Baculovirus Insect Cells | ||
p38 gamma/MAPK12 Protein, Human, Recombinant (His & GST) is expressed in Baculovirus insect cells with His and GST tag. The predicted molecular weight is 69.8 kDa and the accession number is P53778.
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TMPY-00784 | EphB2 Protein, Human, Recombinant (His & hFc) | Human | HEK293 Cells | ||
EphB2 Protein, Human, Recombinant (His & hFc) is expressed in HEK293 mammalian cells with His and hFc tag. The predicted molecular weight is 86 kDa and the accession number is P29323-2.
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TMPY-04216 | EphB2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
EphB2 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 59.3 kDa and the accession number is P54763-3.
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TMPY-03621 | EphB2 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 Cells | ||
EphB2 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 84.6 kDa and the accession number is P54763-3.
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TMPY-04386 | EphB2 Protein, Human, Recombinant (aa 570-987, His & GST) | Human | Baculovirus Insect Cells | ||
EphB2 Protein, Human, Recombinant (aa 570-987, His & GST) is expressed in Baculovirus insect cells with His and GST tag. The predicted molecular weight is 75.2 kDa and the accession number is P29323-3.
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TMPY-01067 | EphB2 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
EphB2 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 59.7 kDa and the accession number is P29323-2.
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TMPK-00563 | EPHB2 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 Cells | ||
EphB2, a receptor tyrosine kinase for ephrin ligands, is overexpressed in various cancers and plays an important role in tumor progression. EPHB2 promotes endothelial-mesenchymal transition (EMT) and elicits associated pathologic characteristics of glioblastoma multiforme (GBM) such as invasion and migration. EPHB2 is epigenetically overexpressed in hypoxia, a condition highly prevalent in malignancy. Furthermore, HIF-2α is required for EPHB2 stabilization by hypoxia.
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TMPY-04544 | MEK2 Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
Dual specificity mitogen-activated protein kinase kinase 2, also known as MAP kinase kinase 2, MAPKK2, ERK activator kinase 2, MAPK / ERK kinase 2, MEK2 and MAP2K2, is a member of the protein kinase superfamily, STE Ser/Thr protein kinase family and MAP kinase kinase subfamily. MAP2K2 / MEK2 contains one protein kinase domain. MEK1 and MEK2 (also known as MAP2K1 and MAP2K2, respectively) are evolutionarily conserved, dual-specificity kinases that mediate Erk1 and Erk2 activation during adhesion and growth factor signaling. MAP2K1 / MEK1 is a crucial modulator of Mek and Erk signaling and have potential implications for the role of MEK1 and MEK2 in tumorigenesis. MAP2K2 / MEK2 catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. It also activates the ERK1 and ERK2 MAP kinases. Defects in MAP2K2 are a cause of Cardiofaciocutaneous Syndrome (CFC Syndrome) which is characterized by a distinctive facial appearance, heart defects, and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects, and hypertrophic cardiomyopathy.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04572 | MKK4 Protein, Mouse, Recombinant (His & GST) | Mouse | Baculovirus Insect Cells | ||
Dual specificity mitogen-activated protein kinase kinase 4, also known as MAP kinase kinase 4, MAPKK4, JNK-activating kinase 1, MAPK/ERK kinase 4, SAPK/ERK kinase 1, c-Jun N-terminal kinase kinase 1, JNKK, and MAP2K4, is a protein that belongs to the protein kinase superfamily, STE Ser/Thr protein kinase family and MAP kinase kinase subfamily. MAP2K4 / JNKK1 is a protein kinase that is a direct activator of MAP kinases in response to various environmental stresses or mitogenic stimuli. MAP2K4 / JNKK1 has been shown to activate MAPK8 / JNK1, MAPK9 / JNK2, and MAPK14 / p38, but not MAPK1 / ERK2 or MAPK3 / ERK1. MAP2K4 / JNKK1 is phosphorylated, and thus activated by MAP3K1 / MEKK. The stress-activated protein kinase (SAPK) pathways represent phosphorylation cascades that convey pro-apoptotic signals. The mitogen-activated protein kinase kinase (MAPKK) homolog MAP2K4 ( MKK4, SEK, JNKK1 ) is a centrally-placed mediator of the SAPK pathways.
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TMPY-04425 | PRAK/MAPKAPK5 Protein, Human, Recombinant (His & GST) | Human | Baculovirus Insect Cells | ||
MAPKAPK5 contains 1 protein kinase domain and belongs to the protein kinase superfamily, CAMK Ser/Thr protein kinase family. MAPKAPK5 has significant sequence homology to mitogen-activated protein kinase (MAPK)-activated protein kinase (MAPKAPK). It is widely distributed. MAPKAPK5 can be phosphorylated by an extracellular-regulated kinase (ERK), and p38 kinase but not by c-jun N-terminal kinase (JNK)in vitro. Recombinant GST-MAPKAPK5 protein can phosphorylate a peptide derived from the regulatory light chain of myosin II. Phosphorylation of MAPKAPK5 by ERK and p38 kinase increased its activity by 9 and 15 fold respectively. Taken together, these data suggest that MAPKAPK5 is a novel in vitro substrate for ERK and p38 kinase. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. MAPKAPK5 also mediates stress-induced small heat shock protein 27 phosphorylation.
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TMPJ-00376 | IL-17RD Protein, Human, Recombinant (hFc) | Human | HEK293 Cells | ||
Interleukin-17 receptor D (IL-17 RD), also known as SEF (similar expression to FGFs), is a type I transmembrane protein that is found in both the cytoplasm and plasma membrane. IL-17RD functions as a feedback inhibitor of fibroblast growth factor mediated Ras-MAPK signaling and ERK activation. It may inhibit FGF-induced FGFR1 tyrosine phosphorylation, regulate the nuclear ERK signaling pathway by spatially blocking nuclear translocation of activated ERK By similarity, and mediate JNK activation and may be involved in apoptosis. IL-17RD interacts with the IL-17R downstream molecule TRAF6. It has been proposed that the IL-17RD intracellular domain interacts with IL-17R and TRAF6 to deliver the downstream signal.
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TMPH-01692 | MAPK3 Protein, Human, Recombinant (His) | Human | E. coli | ||
Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade.
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TMPK-00136 | ULBP-2 Protein, Human, Recombinant (His & Avi) | Human | HEK293 Cells | ||
ULBPs activate multiple signaling pathways in primary NK cells, resulting in the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D induces calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway, mediating natural killer cell cytotoxicity.
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TMPK-00820 | AREG Protein, Human, Recombinant (hFc) | Human | HEK293 Cells | ||
Amphiregulin (AREG) is a member of the epidermal growth factor (EGF) family and is expressed in a plethora of cancers. Tumour growth and metastasis were decreased by AREG silencing in an orthotopic model of pancreatic cancer. AREG may play a critical role in cell migration, invasion, and EMT by activating the EGFR/ERK/NF‑κB signalling pathway in pancreatic cancer cells.
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TMPK-00723 | RANK/TNFRSF11A Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 Cells | ||
TNFRSF11A, also known as receptor activator of NF-κB (RANK), activates several signaling pathways, such as NF-κB, JNK, ERK, p38α, and Akt/PKB. RANK/TNFRSF11A is a novel and frequent target for de novo methylation in gliomas, which affects apoptotic activity and focus formation thereby contributing to the molecular pathogenesis of gliomas. RANK/TNFRSF11A Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 47.0 kDa and the accession number is O35305.
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TMPH-03368 | SG3/Secretogranin 3 Protein, Rat, Recombinant (His & Myc) | Rat | E. coli | ||
Member of the granin protein family that regulates the biogenesis of secretory granules. Acts as a sorting receptor for intragranular proteins including chromogranin A/CHGA. May also play a role in angiogenesis. Promotes endothelial proliferation, migration and tube formation through MEK/ERK signaling pathway. SG3/Secretogranin 3 Protein, Rat, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 58.2 kDa and the accession number is P47868.
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TMPH-03265 | CMKLR2 Protein, Rat, Recombinant (His) | Rat | E. coli | ||
Receptor for chemoattractant adipokine chemerin/RARRES2 suggesting a role for this receptor in the regulation of inflammation and energy homesotasis. Signals mainly via beta-arrestin pathway. Binding of RARRES2 activates weakly G proteins, calcium mobilization and MAPK1/MAPK3 (ERK1/2) phosphorylation too. Acts also as a receptor for TAFA1, mediates its effects on neuronal stem-cell proliferation and differentiation via the activation of ROCK/ERK and ROCK/STAT3 signaling pathway.
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TMPH-01609 | LGI1 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by precluding channel closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that positively regulates synaptic transmission mediated by AMPA-type glutamate receptors. Plays a role in suppressing the production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK pathway. May play a role in the control of neuroblastoma cell survival.
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TMPY-04378 | MAPKAPK3 Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
The MAPKAP kinases are a group of MAP kinase substrates that are themselves kinases. In response to activation, the MAP kinases phosphorylate downstream components on a consensus Pro-X-Ser/Thr-Pro motif. Several kinases that contain this motif have been identified and serve as substrates for the ERK and p38 MAP kinases. Mitogen-activated protein (MAP) kinase-activated protein kinase 3, also known as MAPKAPK-3 and 3pK, is a member of the Ser/Thr protein kinase family. It is widely expressed in human tissues, with a higher expression level observed in the heart and skeletal muscle. No expression in the brain. MAPKAPK-3 is unique since it was shown to be activated by three members of the MAPK family, namely extracellular-signal-regulated kinase (ERK), p38, and Jun-N-terminal kinase (JNK). It is highly activated both by mitogens and by stress-inducing agents or proinflammatory cytokines and translocates to the cytoplasm from the nucleus. MAPKAPK-3 is exclusively activated via the classical MAPK cascade, while stress-induced activation of MAPKAPK-3 is mainly mediated by p38, however, the mechanism defining the specificity remains unknown.
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TMPY-04374 | MST4 Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
MST4, also known as mammalian STE2-like protein kinase 4, is a novel member of the germinal center kinase subfamily of human Ste2-like kinases and is closely related to MST3. The 416 amino acid full-length MST4 contains a C-terminal regulatory domain and an N-terminal kinase domain, both of which are required for full activation of the kinase. MST4 is highly expressed in the placenta, thymus, and peripheral blood leukocytes. MST4 specifically activates ERK but not JNK or p38 MAPK in transiently transfected cells or stable cell lines, and thus is biologically active in the activation of the MEK/ERK pathway mediating cell growth and transformation. Further, MST4 kinase activity is stimulated significantly by epidermal growth factor receptor (EGFR) ligands, which are known to promote the growth of certain cancer cells. Accordingly, MST4 has a potential role in signal transduction pathways involved in cancer progression. Three alternatively spliced isoforms of MST4 have been isolated, and isoform 3 lacks an exon encoding kinase domain and may function as a dominant-negative regulator of the MST4 kinase.
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TMPK-00925 | Noggin/NOG Protein, Mouse, Recombinant | Mouse | HEK293 Cells | ||
Noggin is an antagonist of bone morphogenetic proteins (BMP), being indispensable for certain developmental events.Noggin expression positively correlated with EGFR expression in both GC cell line models and The Cancer Genome Atlas human GC cohort. Targeting EGFR and its downstream pathways diminished cell proliferation which was promoted by Noggin. Noggin promotes the proliferation of GC cells by upregulating EGFR and enhancing a vicious circle formed by β‑catenin, EGFR, ERK and Akt. Noggin/NOG Protein, Mouse, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 23.07 kDa and the accession number is P97466.
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TMPK-00351 | RANK/TNFRSF11A Protein, Human, Recombinant (aa 30-212, hFc) | Human | HEK293 Cells | ||
TNFRSF11A, also known as receptor activator of NF-κB (RANK), activates several signaling pathways, such as NF-κB, JNK, ERK, p38α, and Akt/PKB. RANK/TNFRSF11A is a novel and frequent target for de novo methylation in gliomas, which affects apoptotic activity and focus formation thereby contributing to the molecular pathogenesis of gliomas. RANK/TNFRSF11A Protein, Human, Recombinant (aa 30-212, hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 46.85 kDa and the accession number is Q9Y6Q6-1.
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TMPK-00926 | Noggin/NOG Protein, Mouse, Recombinant (His & Flag) | Mouse | HEK293 Cells | ||
Noggin is an antagonist of bone morphogenetic proteins (BMP), being indispensable for certain developmental events.Noggin expression positively correlated with EGFR expression in both GC cell line models and The Cancer Genome Atlas human GC cohort. Targeting EGFR and its downstream pathways diminished cell proliferation which was promoted by Noggin. Noggin promotes the proliferation of GC cells by upregulating EGFR and enhancing a vicious circle formed by β‑catenin, EGFR, ERK and Akt. Noggin/NOG Protein, Mouse, Recombinant (His & Flag) is expressed in HEK293 mammalian cells with N-His-Flag tag. The predicted molecular weight is 25.16 kDa and the accession number is P97466.
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TMPJ-01125 | PEA15 Protein, Human, Recombinant | Human | E. coli | ||
Astrocyticphosphoprotein PEA-15 (PEA15) is a death effector domain (DED)-containing protein. PEA15 is mainly expressed in the central nervous system, principally in astrocytes. Increased PEA15 levels affect tumorigenesis and cancer progression. PEA15 is overexpressed in breast cancers and gliomas as well as in type 2 diabetes. PEA15 blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. PEA15 also inhibits RPS6KA3 activities by holding it in the cytoplasm. In addition, PEA15 inhibits both TNFRSF6 and TNFRSF1A mediated CASP8 activity and apoptosis. At present, PEA15 expression is also a significant prognostic marker in ovarian cancer.
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TMPY-04466 | STK40 Protein, Human, Recombinant (His & GST) | Human | Baculovirus Insect Cells | ||
STK40 is localized to both the cytoplasm and the nucleus. It is ubiquitously expressed. Mechanistically, Stk40 interacts with Rcn2, which also activates Erk1/2 to induce ExEn specification in mouse ESCs. Stk40 is able to activate the Erk/MAPK pathway and induce extraembryonic-endoderm (ExEn) differentiation in mouse ESCs. Interestingly, cells overexpressing Stk40 exclusively contribute to the ExEn layer of chimeric embryos when injected into host blastocysts. In contrast, deletion of Stk40 in ESCs markedly reduces ExEn differentiation in vitro. STK40 has a central serine/threonine protein kinase domain and is homologous to TRB-3, a protein that regulates activation of MAP kinases and inhibits NFκB-mediated gene transcription. Similarly, overexpression of STK40 inhibits NFκB activation triggered by TNF and also inhibits p53-mediated transcription. There are four named isoforms of STK40 that are produced as a result of alternative splicing.
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TMPY-04410 | MAP4K5 Protein, Human, Recombinant (His & GST) | Human | Baculovirus Insect Cells | ||
Mitogen-activated protein kinase kinase kinase kinase 5, also known as Kinase homologous to SPS1/STE2, MAPK/ERK kinase kinase kinase 5, MEK kinase kinase 5, and MAP4K5, is a cytoplasm protein that belongs to the protein kinase superfamily, STE Ser/Thr protein kinase family and STE2 subfamily. MAP4K5 is ubiquitously expressed in all tissues examined, with high levels in the ovary, testis, and prostate. It contains one CNH domain and one protein kinase domain. MAP4K5 is highly similar to yeast SPS1/STE2 kinase. Yeast SPS1/STE2 functions near the beginning of the MAP kinase signal cascades that are essential for yeast pheromone response. MAP4K5 has been shown to interact with CRKL and TRAF2. This kinase was shown to activate Jun kinase in mammalian cells. MAP4K5 is an early component of MAP kinase signal cascades. It may play a role in the response to environmental stress. MAP4K5 appears to act upstream of the JUN N-terminal pathway.
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TMPJ-00796 | Serpin E2 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Serpin E2 is a secreted protein that belongs to the serpin family. Serpin E2 is a serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Serpin E2 expression is weak or absent in all normal pancreas and chronic pancreatitis tissue. In contrast, it was strongly over-expressed in the majority of pancreatic carcinoma as well as gastric and colorectal cancer samples. Serpin E2 promotes neurite extension by inhibiting thrombin. It also can bind heparin. It has been shown that Serpin E2 is a novel target of ERK signaling involved in human colorectal tumorigenesis. It plays an important role in controlling male fertility because its knockout male mice show a marked impairment in fertility from the onset of sexual maturity and its abnormal expression is found in the semen of men with seminal dysfunction.
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TMPY-02595 | DUSP14 Protein, Human, Recombinant (His & MBP) | Human | E. coli | ||
Dual specific phosphatase 14 / MAP-kinase phophatase-6 (DUSP14 / MKP6) is a member of Dual-specificity phosphatases that is a subclass of protein tyrosine phosphatases (PTP) families that can dephosphorylate bothe phosphotyrosine and phosphoserine / phosphothreonine residues in substrates. Unlike many other DUSPs, DUSP14 only contains a catalytic domain within the C-terminal region. In signal transduction, DUSP14 has been considered as negative regulator of the mitogen-activated protein kinase (MAPK) / extracellular signal-regulated kinase 1 / 2 (ERK 1 / 2) pathway. DUSP14 phosphatase activity has been confirmed to be inhibited by PTP inhibitor Ⅳ. PTP inhibitor binds to the catalytic site of DUSP14. PTP inhibitor Ⅳ effectively and specifically inhibited DUSP14-mediated dephosphorylation of JNK, a member of the mitogen-activated protein kinase (MAPK) family through dephosphorylation of both the Ser / Thr and Tyr residues of MAPKs.
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TMPJ-00155 | Mucin-1/MUC1 Protein, Human, Recombinant (hFc&Avi), Biotinylated | Human | HEK293 Cells | ||
Mucin-1, is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach and pancreas. MUC-1 exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. MUC-1 can act both as an adhesion and an anti-adhesion protein. This protein may provide a protective layer on epithelial cells against bacterial and enzyme attack. MUC-1 participated in modulates signaling in ERK, SRC and NF-kappa-B pathways. In activated T-cells, MUC-1 influences directly or indirectly the Ras/MAPK pathway. MUC-1 promotes tumor progression and regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response.
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TMPY-04389 | MAP3K8 Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
Mitogen-activated protein kinase kinase kinase 8, also known as Cancer Osaka thyroid oncogene, Proto-oncogene c-Cot, Serine/threonine-protein kinase cot, Tumor progression locus 2 and MAP3K8, is a cytoplasm protein that belongs to the protein kinase superfamily, STE Ser/Thr protein kinase family and MAP kinase kinase kinase subfamily. MAP3K8 is expressed in several normal tissues and human tumor-derived cell lines. Isoform 1 of MAP3K8 is activated specifically during the S and G2/M phases of the cell cycle. MAP3K8 is required for TLR4 activation of the MEK/ERK pathway. It can activate NF-kappa-B 1 by stimulating proteasome-mediated proteolysis of NF-kappa-B 1/p15. MAP3K8 plays a role in the cell cycle. The longer form has some transforming activity, although it is much weaker than the activated cot oncoprotein. MAP3K8 oncogene linked to human endometrial carcinoma suggesting that it may be another molecule involved in human endometrial cancer. MAP3K8 may also be an important mediator of intracellular mechanotransduction in human bone marrow-derived mesenchymal stem cells (MSCs).
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TMPJ-00674 | RANK/TNFRSF11A Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
Receptor activator of NF-κB(RANK,TNFRSF11A) belongs to one member of tumor necrosis factor receptor family.It is a receptor for TNFSF11/RANKL/TRANCE/OPGL. This gene encodes a type 1 membrane protein with a 30 amino acids (aa) signal peptide, 184 aa extracellular region , a 20 aa transmembrane domain and a 391 aa cytoplasmic region. Human and murine RANK share 81% aa identity in their extracellular domains. RANK is ubiquitous highly expressed in trabecular bone, thymus, small intestine, lung, brain and kidney, but weakly expressed in spleen and bone marrow. After binding its ligand RANKL, RANK can activate signaling pathways such as NF-κB, JNK, ERK, p38, and Akt/PKB, through TRAF protein phosphorylation. RANK/TNFRSF11A signaling is largely considered to be growth promoting and apoptosis reducing such as the effects observed in osteoclasts. RANK/TNFRSF11A was also found to be involved in the regulation of interactions between T-cells and dendritic cells.
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TMPY-04412 | Germinal Center Kinase/MAP4K2 Protein, Human, Recombinant (His & GST) | Human | Baculovirus Insect Cells | ||
Mitogen-activated protein kinase kinase kinase kinase 2, also known as B lymphocyte serine/threonine-protein kinase, Germinal center kinase, MAPK/ERK kinase kinase kinase 2, MEK kinase kinase 2, Rab8-interacting protein, and MAP4K2, is cytoplasm and peripheral membrane protein that belongs to the protein kinase superfamily, STE Ser/Thr protein kinase family and STE2 subfamily. MAP4K2 contains one CNH domain and one protein kinase domain. Although this kinase is found in many tissues, its expression in lymphoid follicles is restricted to the cells of the germinal center, where it may participate in B-cell differentiation. MAP4K2 can be activated by TNF-alpha and has been shown to specifically activate MAP kinases. It is also found to interact with TNF receptor-associated factor 2 (TRAF2), which is involved in the activation of MAP3K1 / MEKK1. MAP4K2 enhances MAP3K1 oligomerization, which may relieve amino-terminal mediated MAP3K1 autoinhibition and lead to activation following autophosphorylation. It may also play a role in the regulation of vesicle targeting or fusion.
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TMPY-02519 | BLVRB Protein, Human, Recombinant (His) | Human | E. coli | ||
Biliverdin reductase (hBVR) is a serine/threonine kinase that catalyzes reduction of the heme oxygenase (HO) activity product, biliverdin, to bilirubin. BVR consists of an N-terminal dinucleotide-binding domain (Rossmann-fold) and a C-terminal domain that contains a six-stranded β-sheet that is flanked on one face by several α-helices. The C-terminal and N-terminal domains interact extensively, forming the active site cleft at their interface. Biliverdin reductase (BVR) catalyzes the last step in heme degradation by reducing the γ-methene bridge of the open tetrapyrrole, biliverdin IXα, to bilirubin with the concomitant oxidation of a β-nicotinamide adenine dinucleotide (NADH) or β-nicotinamide adenine dinucleotide phosphate (NADPH) cofactor. It is now recognized that human BVR (hBVR) is a dual-specificity kinase (Ser / Thr and Tyr) upstream activator of the insulin/insulin growth factor-1 (IGF-1) and mitogen-activated protein kinase (MAPK) signaling pathways. Human BVR (hBVR) is essential for MAPK-extracellular signal-regulated kinase (ERK)1/2 (MEK)-eukaryotic-like protein kinase (Elk) signaling and has been identified as the cytoplasm-nuclear heme transporter of ERK1/2 and hematin, the key components of stress-responsive gene expression.
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TMPY-04084 | ANGPTL1 Protein, Canine, Recombinant (hFc) | Canine | HEK293 Cells | ||
Angiopoietin-like protein 1 (ANGPTL1) has been reported to suppress migration and invasion in lung and breast cancer, acting as a novel tumor suppressor candidate. Downregulation of tumor suppressor signaling plays an important role in the pathogenesis of hepatocellular carcinoma (HCC).The downregulation of the angiopoietin-like protein ANGPTL1 is associated with vascular invasion, tumor thrombus, metastasis, and poor prognosis in HCC. Ectopic expression of ANGPTL1 in HCC cells effectively decreased their in vitro and in vivotumorigenicity, cell motility, and angiogenesis. shRNA-mediated depletion of ANGPTL1 exerted opposing effects. ANGPTL1 promoted apoptosis via inhibition of the STAT3/Bcl-2-mediated antiapoptotic pathway and decreased cell migration and invasion via downregulation of transcription factors SNAIL and SLUG. Furthermore, ANGPTL1 inhibited angiogenesis by attenuating ERK and AKT signaling and interacted with integrin α1β1 receptor to suppress the downstream FAK/Src-JAK-STAT3 signaling pathway. Taken together, these results suggest ANGPTL1 as a prognostic biomarker and novel therapeutic agent in HCC. ANGPTL1 expression was down-regulated in CRC tissues and inversely correlated with poor survival. ANGPTL1 repressed migration and invasion of CRC cells, and microRNA-138 was involved in this process. Angiopoietin-like protein 1 (ANGPTL1) has been shown to act as a tumor suppressor by inhibiting angiogenesis, cancer invasion, and metastasis.
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TMPY-04467 | NME1 Protein, Human, Recombinant (His) | Human | E. coli | ||
NME1, also known as Nucleoside Diphosphate Kinase A (NDK-A), or NM23-H1, belongs to the NDK family. NM23-H1 is known to have a metastasis suppressive activity in many tumor cells. Recent studies have shown that the interacting proteins with NM23-H1 which mediate cell proliferation, may act as modulators of the metastasis suppressor activity. The interacting proteins with NM23-H1 can be classified into 3 groups. The first group of proteins can be classified as upstream kinases of NM23-H1 such as CKI and Aurora-A/STK15. The second group of proteins acts as downstream effectors for the regulation of specific gene transcriptions, GTP-binding protein functions, and signal transduction in the Erk signal cascade. The third group of proteins can be classified as bi-directionally influencing binding partners of NM23-H1. As a result, the interactions with NM23-H1 and binding partners have implications in the biochemical characterization involved in metastasis and tumorigenesis. NDKA is increased in human postmortem cerebrospinal fluid (CSF), a model of global brain insult, suggesting that measurement in CSF and, more importantly, in plasma may be useful as a biomarker of stroke. Additionally, NM23-H1 significantly reduces metastasis without effects on primary tumor size and was the first discovered metastasis suppressor gene.
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TMPY-04455 | PKC iota Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
Protein kinase C iota type, also known as Atypical protein kinase C-lambda/iota, aPKC-lambda/iota and PRKCI, is a cytoplasm, membrane and nucleus protein which belongs to the protein kinase superfamily, AGC Ser/Thr protein kinase family and PKC subfamily. PRKCI contains one AGC-kinase C-terminal domain, one OPR domain, one phorbol-ester/DAG-type zinc finger and one protein kinase domain. PRKCI is predominantly expressed in lung and brain, but also expressed at lower levels in many tissues including pancreatic islets. It is highly expressed in non-small cell lung cancers. PRKCI is a calcium-independent, phospholipid-dependent, serine- and threonine-specific kinase. It may play a role in the secretory response to nutrients. PRKCI is involved in cell polarization processes and the formation of epithelial tight junctions. It is implicated in the activation of several signaling pathways including Ras, c-Src and NF-kappa-B pathways. PRKCI functions in both pro- and anti-apoptotic pathways. It functions in the RAC1/ERK signaling required for transformed growth. PRKCI plays a role in microtubule dynamics through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). PRKCI might be a target for novel lipid activators that are elevated during nutrient-stimulated insulin secretion.
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TMPY-02191 | BLNK Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
B-cell linker protein, also known as B-cell adapter containing a SH2 domain protein, B-cell adapter containing a Src homology 2 domain protein, Cytoplasmic adapter protein, Src homology 2 domain-containing leukocyte protein of 65 kDa, SLP-65 and BLNK, is a cytoplasm and cell membrane protein which contains oneSH2 domain. BLNK is expressed in B-cell lineage and fibroblast cell lines. Highest levels of expression is in the spleen, with lower levels in the liver, kidney, pancreas, small intestines and colon. BLNK functions as a central linker protein that bridges kinases associated with the B-cell receptor (BCR) with a multitude of signaling pathways, regulating biological outcomes of B-cell function and development. BLNK plays a role in the activation of ERK / EPHB2, MAP kinase p38 and JNK. BLNK modulates AP1 activation. It is important for the activation of NF-kappa-B and NFAT. BLNK plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca2+mobilization and is required for trafficking of the BCR to late endosomes. BLNK may be required for the RAC1-JNK pathway. It plays a critical role in orchestrating the pro-B cell to pre-B cell transition. BLNK also plays an important role in BCR-induced B-cell apoptosis.Defects in BLNK are the cause of agammaglobulinemia type 4 (AGM4) which is a primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B cells due to an early block of B-cell development.
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TMPJ-00060 | IL-25/IL17E Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Interleukin 25 (IL-25) belongs to the Interleukin 17 (IL-17) family of proteins, which is comprised of six members (IL-17, IL-17B through IL-17F). These proteins are secreted and are structurally related by sharing a conserved cysteine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus. With the exception of IL-17B, which exists as a non-covalently linked dimer, all IL-17 family members are disulfide-linked dimers. IL-17 family proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions. Human interleukin-17E (IL17E), also referred to as Interleukin-25 (IL25), is a distinct member of the IL17 cytokine family comprised of at least six members sharing a conserved cysteine-knot structure but divergent at the N-terminus. IL25 is a glycoprotein secreted as dimers by innate effector eosinophils and basophils, and present at very low levels in various peripheral tissues. IL25, together with IL17B, are ligands for the cytokine receptor IL17BR, and the cross-linking induces NF-κB activation and production of the proinflammatory chemokine IL-8, as well as ERK, JNK, and p38 activation. Overexpression of IL25 gene in transgenic mice suggested that this cytokine can regulate hematopoietic and immune functions, and additionally is identified as a proinflammatory cytokine favoring Th2-type immune responses possibly by enhancing the maintenance and functions of adaptive Th2 memory cells.
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TMPY-04391 | Lyn Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
Tyrosine-protein kinase Lyn is a member of the Src family of protein tyrosine kinases, which is mainly expressed in hematopoietic cells, in neural tissues liver, and adipose tissue. Tyrosine-protein kinase Lyn has many functions. Lyn kinase may downregulate the expression of stem cell growth factor receptor (KIT). Lyn kinase Acts as an effector of EpoR (erythropoietin receptor) in controlling KIT expression and may play a central role in erythroid differentiation during the switch between proliferation and maturation. Lyn kinase also acts as a positive regulator of cell movement while negatively regulating adhesion to stromal cells by inhibiting the ICAM-1-binding activity of beta-2 integrins. Lyn kinase relays suppressing signals from the chemokine receptor CXCR4 to beta-2 integrin LFA-1 in hematopoietic precursors. This kinase is involved in the induction of stress-activated protein kinase (SAPK), but not ERK or p38 MAPK, in response to genotoxic agents. In a word, Lyn kinase functions primarily as a negative regulator, but can also function as an activator, depending on the context. Tyrosine-protein kinase Lyn is Required for the initiation of the B-cell response, but also its down-regulation and termination. It also plays an important role in the regulation of B-cell differentiation, proliferation, survival, and apoptosis, and is important for immune self-tolerance. It has been reported that Lyn kinase plays a role in the inflammatory response to bacterial lipopolysaccharide. Lyn kinase Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils, and eosinophils.
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