目录号 | 产品详情 | 靶点 | |
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TN2239 | ATPase Potassium Channel Sodium Channel Parasite Antifungal | ||
Strictosamide 具有抗炎、抗疟原虫和抗真菌活性。 | |||
T9530 | Others | ||
W36017 是利多卡因的一种杂质,其阻滞神经活性的pKa 为 7.4。 | |||
T7688 | FAAH | ||
4-Nonylphenylboronic acid 是 FAAH 的抑制剂。 | |||
T8538 | Others | ||
ML382 是选择性的 Mas 相关 G 蛋白偶联受体 X1MRGPRX1 (MrgX1)正向调节剂,其EC50=190 nM。 | |||
T7526 | TRP/TRPV Channel | ||
JNJ-17203212 是一种竞争性 TRPV1选择性拮抗剂。它被开发用于疼痛处理的研究。 | |||
T9683 | Sodium Channel | ||
VX-150 是一种口服有效的,高选择性的 NaV1.8抑制剂。VX-150 在各种疼痛适应症中有研究的价值。 | |||
T3S2312 | Apoptosis Others | ||
Poncirin (Isosakuranetin-7-neohesperidoside) 是从三叶草中分离出来的一种天然产物,具有抗炎活性。 它防止脂肪生成,增强间充质干细胞中的成骨细胞分化,增加骨矿物质密度,改善小梁微结构,可能反映 GIO 小鼠的骨形成增加和骨吸收减少。 | |||
T5460 | COX | ||
Mofezolac 是一种非甾体类抗炎药,可缓解疼痛并具有抗炎活性,抑制 COX-1和COX-2的IC50为 1.44 和 447 nM。 | |||
T5513 | P2X Receptor | ||
RO3 是一种能透过大脑的P2X3和P2X2/3拮抗剂,口服有活性。它对人同型多聚体 P2X3和异型多聚体 P2X2/3受体的 pIC50分别为 5.9 和 7.0。 | |||
T8410 | TRP/TRPV Channel | ||
ASP7663 是口服有效的TRPA1选择性激动剂。ASP7663具有抗便秘和抗腹痛的功效。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-05945 | Influenza A H1N2 (A/Swine/Spain/SF12091/2007) Neuraminidase/NA Protein (His) | H1N2 | HEK293 | ||
Neuraminidases are enzymes that cleave sialic acid groups from glycoproteins. Influenza neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Influenza neuraminidase is composed of four identical subunits arranged in a square. It is normally attached to the virus surface through a long protein stalk. The active sites are in a deep depression on the upper surface. They bind to polysaccharide chains and clip off the sugars at the end. The surface of neuraminidase is decorated with several polysaccharide chains that are similar to the polysaccharide chains that decorate our cell surface proteins. Neuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of the influenza virus. Hemagglutinin binds to the sialic acid-containing receptors on the surface of host cells during initial infection and at the end of an infectious cycle. Neuraminidase, on the other hand, cleaves the HA-sialic acid bondage from the newly formed virions and the host cell receptors during budding. Neuraminidase thus is described as a receptor-destroying enzyme that facilitates virus release and efficient spread of the progeny virus from cell to cell. Influenza antibody and influenza antibodies are very important research tools for influenza diagnosis, influenza vaccine development, and anti-influenza virus therapy development. The monoclonal or polyclonal antibody can be raised with protein based antigen or peptide-based antigen. Antibodies raised with protein-based antigen could have better specificity and/or binding affinity than antibodies raised with peptide based antigen, but the cost associated with the recombinant protein antigen is usually higher. Anti-influenza virus hemagglutinin (HA) monoclonal antibody or polyclonal antibody can be used for ELISA assay, western blotting detection, Immunohistochemistry (IHC), flow cytometry, neutralization assay, hemagglutinin inhibition assay, and early diagnosis of influenza viral infection. Sino Biological has developed state-of-the-art monoclonal antibody development technology platforms: mouse monoclonal antibody and rabbit monoclonal antibody. Our rabbit monoclonal antibody platform is one of a kind and offers some unique advantages over mouse monoclonal antibodies, such as high affinity, low cross-reactivity with rabbit polyclonal antibodies.
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TMPY-05682 | SARS-CoV-2 Plpro/papain-like protease Protein (aa 1564-1880, His) | SARS-CoV-2 | E. coli | ||
The coronaviral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpro), are attractive antiviral drug targets because they are essential for coronaviral replication. PLpro has the additional function of stripping ubiquitin and ISG15 from host-cell proteins to aid coronaviruses in their evasion of the host innate immune responses. Targeting PLpro with antiviral drugs may have an advantage in not only inhibiting viral replication but also inhibiting the dysregulation of signaling cascades in infected cells that may lead to cell death in surrounding, uninfected cells.
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TMPY-05892 | Influenza A H3N2 (A/swine/Spain/33601/2001) Hemagglutinin/HA Protein (His) | H3N2 | HEK293 | ||
The influenza viral Hemagglutinin (HA) protein is a homotrimer with a receptor binding pocket on the globular head of each monomer.HA has at least 18 different antigens. These subtypes are named H1 through H18.HA has two functions. Firstly, it allows the recognition of target vertebrate cells, accomplished through the binding to these cells' sialic acid-containing receptors. Secondly, once bound it facilitates the entry of the viral genome into the target cells by causing the fusion of the host endosomal membrane with the viral membrane. The influenza virus Hemagglutinin (HA) protein is translated in cells as a single protein, HA, or hemagglutinin precursor protein. For viral activation, hemagglutinin precursor protein (HA) must be cleaved by a trypsin-like serine endoprotease at a specific site, normally coded for by a single basic amino acid (usually arginine) between the HA1 and HA2 domains of the protein. After cleavage, the two disulfide-bonded protein domains produce the mature form of the protein subunits as a prerequisite for the conformational change necessary for fusion and hence viral infectivity.
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TMPY-04894 | SARS-CoV (strain WH20) Plpro/papain-like protease (His) | SARS | E. coli | ||
The coronaviral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpro), are attractive antiviral drug targets because they are essential for coronaviral replication. PLpro has the additional function of stripping ubiquitin and ISG15 from host-cell proteins to aid coronaviruses in their evasion of the host innate immune responses. Targeting PLpro with antiviral drugs may have an advantage in not only inhibiting viral replication but also inhibiting the dysregulation of signaling cascades in infected cells that may lead to cell death in surrounding, uninfected cells.
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TMPH-03151 | Gingipain R1 Protein, Porphyromonas gingivalis, Recombinant (His) | Porphyromonas gingivalis | Yeast | ||
Thiol protease. Acts synergistically with RgpB to catalyze the maturation of fimbrial subunits, such as FimA. Its proteolytic activity is a major factor in both periodontal tissue destruction and in evasion of host defense mechanisms (Probable).
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TMPH-03648 | Cruzipain Protein, Trypanosoma cruzi, Recombinant (His & Myc) | Trypanosoma cruzi | E. coli | ||
Cruzipain Protein, Trypanosoma cruzi, Recombinant (His & Myc) is expressed in E. coli.
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TMPH-03153 | Gingipain R2 Protein, Porphyromonas gingivalis, Recombinant (His) | Porphyromonas gingivalis | E. coli | ||
Thiol protease. Acts synergistically with RgpA to catalyze the maturation of fimbrial subunits, such as FimA. Its proteolytic activity is a major factor in both periodontal tissue destruction and in evasion of host defense mechanisms.
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TMPH-03598 | Streptopain Protein, S. pyogenes serotype M28, Recombinant (His & SUMO) | Streptococcus pyogenes | E. coli | ||
Important streptococcal virulence factor which cleaves human fibronectin and degrades vitronectin. Also cleaves human IL1B precursor to form biologically active IL1B. Can induce apoptosis in human monocytes and epithelial cells in vitro, and reduces phagocytic activity in monocytic cells. Thus, may play a role in bacterial colonization, invasion, and inhibition of wound healing.
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TMPH-03152 | Gingipain R1 Protein, Porphyromonas gingivalis, Recombinant (B2M & His) | Porphyromonas gingivalis | E. coli | ||
Thiol protease. Acts synergistically with RgpB to catalyze the maturation of fimbrial subunits, such as FimA. Its proteolytic activity is a major factor in both periodontal tissue destruction and in evasion of host defense mechanisms (Probable).
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TMPH-03156 | Lys-gingipain Protein, Porphyromonas gingivalis, Recombinant (His & SUMO) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
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TMPH-00347 | Papain Protein, Carica papaya, Recombinant (His) | Carica papaya | E. coli | ||
Papain Protein, Carica papaya, Recombinant (His) is expressed in E. coli with N-terminal 6xHis tag. The predicted molecular weight is 27.4 kDa. Accession number: P00784
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TMPK-01384 | SARS PLpro/papain-like protease Protein (His) | SARS | E. coli | ||
The coronaviral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpro), are attractive antiviral drug targets because they are essential for coronaviral replication. Although the primary function of PLpro and 3CLpro are to process the viral polyprotein in a coordinated manner, PLpro has the additional function of stripping ubiquitin and ISG15 from host-cell proteins to aid coronaviruses in their evasion of the host innate immune responses.
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TMPJ-01431 | SARS-CoV-2 Papain-Like Protease Protein | SARS-CoV-2 | E. coli | ||
Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). These proteases are important targets for development of antiviral drugs that would inhibit viral replication and reduce mortality associated with outbreaks of SARS-CoV. PLpro is a cysteine protease located within the non-structural protein 3 (NS3) section of the viral polypeptide. PLPro activity is required to process the viral polyprotein into functional, mature subunits; specifically, PLPro cleaves a site at the amino-terminus of the viral replicase region. In addition to its role in viral protein maturation, PLPro possesses a deubiquitinating and deISGylating activity. In vivo, this protease antagonizes innate immunity by inhibiting IRF3-induced production of type I interferons.
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TMPK-01352 | SARS-CoV-2 PLpro/papain-like protease Protein (His & Avi) | SARS | E. coli | ||
The coronaviral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpro), are attractive antiviral drug targets because they are essential for coronaviral replication. Although the primary function of PLpro and 3CLpro are to process the viral polyprotein in a coordinated manner, PLpro has the additional function of stripping ubiquitin and ISG15 from host-cell proteins to aid coronaviruses in their evasion of the host innate immune responses.
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TMPH-02414 | Lys-gingipain W83 Protein, Porphyromonas gingivalis, Recombinant (His) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria. Has hemolytic activity; this is mediated by the adhesin domains and does not require the catalytic domain.
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TMPH-03576 | Staphopain A Protein, S. aureus, Recombinant (His & Myc) | Staphylococcus aureus | E. coli | ||
Cysteine protease that plays an important role in the inhibition of host innate immune response. Cleaves host elastins found in connective tissues, pulmonary surfactant protein A in the lungs, and the chemokine receptor CXCR2 on leukocytes. Proteolytic cleavage of surfactant protein A impairs bacterial phagocytocis by neutrophils while CXCR2 degradation blocks neutrophil activation and chemotaxis. Additionally, promotes vascular leakage by activating the plasma kallikerin/kinin system, resulting in hypotension.
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TMPH-03155 | Lys-gingipain HG66 Protein, Porphyromonas gingivalis, Recombinant (His & Myc) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
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TMPH-03154 | Lys-gingipain 381 Protein, Porphyromonas gingivalis, Recombinant (His) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
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TMPH-03577 | Staphopain B Protein, S. aureus, Recombinant (GST) | Staphylococcus aureus | E. coli | ||
Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S. aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin.
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TMPH-03599 | Streptopain Protein, S. pyogenes, Recombinant (His & SUMO) | Streptococcus pyogenes | E. coli | ||
Important streptococcal virulence factor which cleaves human fibronectin and degrades vitronectin. Also cleaves human IL1B precursor to form biologically active IL1B. Can induce apoptosis in human monocytes and epithelial cells in vitro, and reduces phagocytic activity in monocytic cells. Thus, may play a role in bacterial colonization, invasion, and inhibition of wound healing.
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TMPK-00735 | CXCL13/BCA-1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Recent studies have implicated chemokines in microglial activation and pathogenesis of neuropathic pain. C-X-C motif chemokine 13 (CXCL13) is a B lymphocyte chemoattractant that activates CXCR5. Using the spinal nerve ligation (SNL) model of neuropathic pain, CXCL13 was persistently upregulated in spinal cord neurons after SNL, resulting in spinal astrocyte activation via CXCR5 in mice.
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TMPY-03050 | CXCL5 Protein, Human, Recombinant | Human | E. coli | ||
CXCL5 is a small cytokine belonging to the CXC chemokine family. CXC chemokines are particularly significant for leukocyte infiltration in inflammatory diseases. CXCL5 is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. It also can be detected in eosinophils, and can be inhibited with the type II interferon. CXCL5 plays a role in reducing sensitivity to sunburn pain in some subjects, and is a potential target which can be utilized to understand more about pain in other inflammatory conditions like arthritis and cystitis. It stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2.
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TMPY-01084 | TrkA Protein, Human, Recombinant (His) | Human | HEK293 | ||
TRKA is a member of the neurotrophic tyrosine kinase receptor (NTKR) family. It is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by the pluripotent neural stem and neural crest progenitors. The presence of NTRK1 leads to cell differentiation and may play a role in specifying sensory neuron subtypes. Mutations in the TRKA gene have been associated with congenital insensitivity to pain, anhidrosis, self-mutilating behavior, mental retardation, and cancer. It was originally identified as an oncogene as it is commonly mutated in cancers, particularly colon and thyroid carcinomas. TRKA is required for high-affinity binding tonerve growth factor (NGF), neurotrophin-3 and neurotrophin-4/5 but not brain-derived neurotrophic factor (BDNF). Known substrates for the Trk receptors are SHC1, PI 3-kinase, and PLC-gamma-1. NTRK1 has a crucial role in the development and function of the nociceptive reception system as well as the establishment of thermal regulation via sweating. It also activates ERK1 by either SHC1- or PLC-gamma-1-dependent signaling pathway. Defects in NTRK1 are a cause of congenital insensitivity to pain with anhidrosis and thyroid papillary carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-06985 | NGF Protein, Human, Recombinant (HEK293) | Human | HEK293 | ||
Nerve growth factor (NGF) is important for the development and maintenance of the sympathetic and sensory nervous systems. NGF protein was identified as a large complex consisting of three non-covalently linked subunits, α, β, and γ, among which, the β subunit, called β-NGF (beta-NGF), was demonstrated to exhibits the growth-stimulating activity of NGF protein. NGFB/beta-NGF gene is a member of the NGF-beta family and encodes a secreted protein that homodimerizes and is incorporated into a larger complex. NGF protein acts via at least two receptors on the surface of cells (TrkA and p75 receptors) to regulate neuronal survival, promote neurite outgrowth, and up-regulate certain neuronal functions such as mediation of pain and inflammation. Also, previous studies indicated that NGF may also have an important role in the regulation of the immune system.
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TMPY-01010 | NGF Protein, Human, Recombinant | Human | CHO | ||
Nerve growth factor (NGF) is important for the development and maintenance of the sympathetic and sensory nervous systems. NGF protein was identified as a large complex consisting of three non-covalently linked subunits, α, β, and γ, among which, the β subunit, called β-NGF (beta-NGF), was demonstrated to exhibits the growth-stimulating activity of NGF protein. NGFB/beta-NGF gene is a member of the NGF-beta family and encodes a secreted protein that homodimerizes and is incorporated into a larger complex. NGF protein acts via at least two receptors on the surface of cells (TrkA and p75 receptors) to regulate neuronal survival, promote neurite outgrowth, and up-regulate certain neuronal functions such as mediation of pain and inflammation. Also, previous studies indicated that NGF may also have an important role in the regulation of the immune system.
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TMPY-01727 | GLA/alpha-Galactosidase A Protein, Human, Recombinant (His) | Human | HEK293 | ||
Alpha-galactosidase A, also known as Alpha-D-galactoside galactohydrolase, Alpha-D-galactosidase A, Melibiase and GLA, is a member of the glycosyl hydrolase 27 family. GLA is used as a long-term enzyme replacement therapy in patients with a confirmed diagnosis of Fabry disease. Defects in GLA are the cause of Fabry disease (FD) which is a rare X-linked sphingolipidosis disease where glycolipid accumulates in many tissues. The disease consists of an inborn error of glycosphingolipid catabolism. FD patients show systemic accumulation of globotriaoslyceramide (Gb3) and related glycosphingolipids in the plasma and cellular lysosomes throughout the body. Clinical recognition in males results from characteristic skin lesions (angiokeratomas) over the lower trunk. Patients may show ocular deposits, febrile episodes, and burning pain in the extremities. Death results from renal failure, cardiac or cerebral complications of hypertension or other vascular disease. Deficiency of GLA leads to the accumulation of glycosphingolipids in the vasculature leading to multiorgan pathology. In addition to well-described microvascular disease, deficiency of GLA is also characterized by premature macrovascular events such as stroke and possibly myocardial infarction.
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TMPK-00541 | SEZ6 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface.
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TMPK-00997 | SEZ6 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface.
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TMPK-00998 | SEZ6 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface.
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TMPK-01065 | SEZ6 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface.
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TMPK-00018 | CXCL13/BCA-1 Protein, Human, Recombinant (His & Sumo) | Human | E. coli | ||
Recent studies have implicated chemokines in microglial activation and pathogenesis of neuropathic pain. C-X-C motif chemokine 13 (CXCL13) is a B lymphocyte chemoattractant that activates CXCR5. Using the spinal nerve ligation (SNL) model of neuropathic pain, CXCL13 was persistently upregulated in spinal cord neurons after SNL, resulting in spinal astrocyte activation via CXCR5 in mice.
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TMPH-01764 | Neuropeptide B Protein, Human, Recombinant (GST) | Human | E. coli | ||
May be involved in the regulation of feeding, neuroendocrine system, memory, learning and in the afferent pain pathway.
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TMPK-00017 | CXCL13/BCA-1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Recent studies have implicated chemokines in microglial activation and pathogenesis of neuropathic pain. C-X-C motif chemokine 13 (CXCL13) is a B lymphocyte chemoattractant that activates CXCR5. Using the spinal nerve ligation (SNL) model of neuropathic pain, CXCL13 was persistently upregulated in spinal cord neurons after SNL, resulting in spinal astrocyte activation via CXCR5 in mice.
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TMPK-00996 | SEZ6 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface.
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TMPK-00734 | CXCL13/BCA-1 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Recent studies have implicated chemokines in microglial activation and pathogenesis of neuropathic pain. C-X-C motif chemokine 13 (CXCL13) is a B lymphocyte chemoattractant that activates CXCR5. Using the spinal nerve ligation (SNL) model of neuropathic pain, CXCL13 was persistently upregulated in spinal cord neurons after SNL, resulting in spinal astrocyte activation via CXCR5 in mice.
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TMPY-04790 | CXCL5 Protein, Mouse, Recombinant (His) | Mouse | Yeast | ||
CXCL5 is a small cytokine belonging to the CXC chemokine family. CXC chemokines are particularly significant for leukocyte infiltration in inflammatory diseases. CXCL5 is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. It also can be detected in eosinophils, and can be inhibited with the type II interferon. CXCL5 plays a role in reducing sensitivity to sunburn pain in some subjects, and is a potential target which can be utilized to understand more about pain in other inflammatory conditions like arthritis and cystitis. It stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2.
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TMPH-01765 | Neuropeptide B Protein, Human, Recombinant | Human | E. coli | ||
May be involved in the regulation of feeding, neuroendocrine system, memory, learning and in the afferent pain pathway.
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TMPH-02118 | SCN1A Protein, Human, Recombinant (His) | Human | E. coli | ||
Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Plays a key role in brain, probably by regulating the moment when neurotransmitters are released in neurons. Involved in sensory perception of mechanical pain: activation in somatosensory neurons induces pain without neurogenic inflammation and produces hypersensitivity to mechanical, but not thermal stimuli.
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TMPH-00055 | Alpha-toxin Amm8 Protein, Androctonus mauritanicus, Recombinant (His & Myc) | Androctonus mauritanicus | Baculovirus | ||
Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. The toxin principally slows the inactivation process of TTX-sensitive sodium channels. It discriminates neuronal versus muscular sodium channel, as it is more potent on rat brain Nav1.2/SCN2A (EC(50)=29 nM) than on rat skeletal muscle Nav1.4/SCN4A (EC(50)=416 nM). It also shows a weak activity on Nav1.7/SCN9A (EC(50)=1.76 uM). In vivo, the toxin produces pain hypersensibility to mechanical and thermal stimuli.(PubMed:23685008). It also exhibits potent analgesic activity (when injected intraperitoneally), increasing hot plate and tail flick withdrawal latencies in a dose-dependent fashion. This paradoxical analgesic action, is significantly suppressed by opioid receptor antagonists, suggesting a pain-induced analgesia mechanism that involves an endogenous opioid system. This led to hypothesis that pain relief induced by peripheral administration of Amm VIII may result from sensitization of primary afferent neurons and subsequent activation of an opioid-dependent noxious inhibitory control.
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TMPJ-00737 | PDYN Protein, Human, Recombinant (His) | Human | Human Cells | ||
Proenkephalin-B(PDYN), belongs to the opioid neuropeptide precursor family. The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. Leu-enkephalins, which is a type of Proenkephalin-B, compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A has a typical opiod activity, it is 700 times more potent than Leu-enkephalin.
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TMPY-06967 | TrkA Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
TRKA is a member of the neurotrophic tyrosine kinase receptor (NTKR) family. It is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by the pluripotent neural stem and neural crest progenitors. The presence of NTRK1 leads to cell differentiation and may play a role in specifying sensory neuron subtypes. Mutations in the TRKA gene have been associated with congenital insensitivity to pain, anhidrosis, self-mutilating behavior, mental retardation, and cancer. It was originally identified as an oncogene as it is commonly mutated in cancers, particularly colon and thyroid carcinomas. TRKA is required for high-affinity binding tonerve growth factor (NGF), neurotrophin-3 and neurotrophin-4/5 but not brain-derived neurotrophic factor (BDNF). Known substrates for the Trk receptors are SHC1, PI 3-kinase, and PLC-gamma-1. NTRK1 has a crucial role in the development and function of the nociceptive reception system as well as the establishment of thermal regulation via sweating. It also activates ERK1 by either SHC1- or PLC-gamma-1-dependent signaling pathway. Defects in NTRK1 are a cause of congenital insensitivity to pain with anhidrosis and thyroid papillary carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-03035 | M-myrmeciitoxin-Mp2b Protein, Myrmecia pilosula, Recombinant (GST & His) | Myrmecia pilosula | Baculovirus | ||
Heterodimer protein that may serve both defensive (pain-inducing) and predatory (insecticidal) roles. Has membrane-disrupting activity and shows induction of non-specific calcium influx into cells,. Shows broad-spectrum activity against a diverse range of bacteria, and cell lines, as well as hemolytic activity (EC(50)=2.18 uM). In vivo, shows moderate insecticidal activity against D.melanogaster and potent anthelmintic activity against the veterinary nematode H.contortus. In addition, intraplantar injection into mice induces nocifensive behavior and mechanical allodynia.
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TMPH-00859 | HTR1B Protein, Human, Recombinant (His) | Human | in vitro E. coli expression system | ||
G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances, such as lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Regulates the release of 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby affects neural activity, nociceptive processing, pain perception, mood and behavior. Besides, plays a role in vasoconstriction of cerebral arteries.
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TMPJ-00475 | Kallikrein 1/KLK1 Protein, Human, Recombinant (aa 19-262, His) | Human | Human Cells | ||
Kallikrein-1 (KLK1) is a member of human tissue Kallikrein family. Human KLK1 precursor contains a singal peptide (residues 1 to 18), a short pro peptide (residues 19 to 24) and a mature chain (residues 25 to 262). The function of KLK1 is to cleave Kininogen in order to release the vasoactive Kinin peptide (Lysyl-Bradykinin or Bradykinin). The Kinin peptide controls blood pressure reduction, vasodilation, smooth muscle relaxation and contraction, pain induction and inflammation. KLK1 also plays a role in angiogensis and tumorigenesis.
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TMPH-00054 | AaH II Protein, Androctonus australis, Recombinant (His & SUMO) | Androctonus australis | E. coli | ||
Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. The toxin principally slows the inactivation process of TTX-sensitive sodium channels. It is active on rat brain Nav1.2/SCN2A sodium channel (EC(50)=2.6 nM) and on rat skeletal muscle Nav1.4/SCN4A sodium channel (EC(50)=2.2 nM), as well as on human neuronal Nav1.7/SCN9A (EC(50)=6.8 nM). This toxin is active against mammals. In vivo, intraplantar injection into mice induces spontaneous pain responses.
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TMPY-01760 | TrkA Protein, Human, Recombinant (aa 194-413, His) | Human | HEK293 | ||
TRKA is a member of the neurotrophic tyrosine kinase receptor (NTKR) family. It is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by the pluripotent neural stem and neural crest progenitors. The presence of NTRK1 leads to cell differentiation and may play a role in specifying sensory neuron subtypes. Mutations in the TRKA gene have been associated with congenital insensitivity to pain, anhidrosis, self-mutilating behavior, mental retardation, and cancer. It was originally identified as an oncogene as it is commonly mutated in cancers, particularly colon and thyroid carcinomas. TRKA is required for high-affinity binding tonerve growth factor (NGF), neurotrophin-3 and neurotrophin-4/5 but not brain-derived neurotrophic factor (BDNF). Known substrates for the Trk receptors are SHC1, PI 3-kinase, and PLC-gamma-1. NTRK1 has a crucial role in the development and function of the nociceptive reception system as well as the establishment of thermal regulation via sweating. It also activates ERK1 by either SHC1- or PLC-gamma-1-dependent signaling pathway. Defects in NTRK1 are a cause of congenital insensitivity to pain with anhidrosis and thyroid papillary carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04663 | TrkA Protein, Rabbit, Recombinant (His) | Rabbit | HEK293 | ||
TRKA is a member of the neurotrophic tyrosine kinase receptor (NTKR) family. It is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by the pluripotent neural stem and neural crest progenitors. The presence of NTRK1 leads to cell differentiation and may play a role in specifying sensory neuron subtypes. Mutations in the TRKA gene have been associated with congenital insensitivity to pain, anhidrosis, self-mutilating behavior, mental retardation, and cancer. It was originally identified as an oncogene as it is commonly mutated in cancers, particularly colon and thyroid carcinomas. TRKA is required for high-affinity binding tonerve growth factor (NGF), neurotrophin-3 and neurotrophin-4/5 but not brain-derived neurotrophic factor (BDNF). Known substrates for the Trk receptors are SHC1, PI 3-kinase, and PLC-gamma-1. NTRK1 has a crucial role in the development and function of the nociceptive reception system as well as the establishment of thermal regulation via sweating. It also activates ERK1 by either SHC1- or PLC-gamma-1-dependent signaling pathway. Defects in NTRK1 are a cause of congenital insensitivity to pain with anhidrosis and thyroid papillary carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03536 | TrkA Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
TRKA is a member of the neurotrophic tyrosine kinase receptor (NTKR) family. It is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by the pluripotent neural stem and neural crest progenitors. The presence of NTRK1 leads to cell differentiation and may play a role in specifying sensory neuron subtypes. Mutations in the TRKA gene have been associated with congenital insensitivity to pain, anhidrosis, self-mutilating behavior, mental retardation, and cancer. It was originally identified as an oncogene as it is commonly mutated in cancers, particularly colon and thyroid carcinomas. TRKA is required for high-affinity binding tonerve growth factor (NGF), neurotrophin-3 and neurotrophin-4/5 but not brain-derived neurotrophic factor (BDNF). Known substrates for the Trk receptors are SHC1, PI 3-kinase, and PLC-gamma-1. NTRK1 has a crucial role in the development and function of the nociceptive reception system as well as the establishment of thermal regulation via sweating. It also activates ERK1 by either SHC1- or PLC-gamma-1-dependent signaling pathway. Defects in NTRK1 are a cause of congenital insensitivity to pain with anhidrosis and thyroid papillary carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04285 | TrkA Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
TRKA is a member of the neurotrophic tyrosine kinase receptor (NTKR) family. It is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by the pluripotent neural stem and neural crest progenitors. The presence of NTRK1 leads to cell differentiation and may play a role in specifying sensory neuron subtypes. Mutations in the TRKA gene have been associated with congenital insensitivity to pain, anhidrosis, self-mutilating behavior, mental retardation, and cancer. It was originally identified as an oncogene as it is commonly mutated in cancers, particularly colon and thyroid carcinomas. TRKA is required for high-affinity binding tonerve growth factor (NGF), neurotrophin-3 and neurotrophin-4/5 but not brain-derived neurotrophic factor (BDNF). Known substrates for the Trk receptors are SHC1, PI 3-kinase, and PLC-gamma-1. NTRK1 has a crucial role in the development and function of the nociceptive reception system as well as the establishment of thermal regulation via sweating. It also activates ERK1 by either SHC1- or PLC-gamma-1-dependent signaling pathway. Defects in NTRK1 are a cause of congenital insensitivity to pain with anhidrosis and thyroid papillary carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01083 | TrkA Protein, Human, Recombinant (His & hFc) | Human | HEK293 | ||
TRKA is a member of the neurotrophic tyrosine kinase receptor (NTKR) family. It is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by the pluripotent neural stem and neural crest progenitors. The presence of NTRK1 leads to cell differentiation and may play a role in specifying sensory neuron subtypes. Mutations in the TRKA gene have been associated with congenital insensitivity to pain, anhidrosis, self-mutilating behavior, mental retardation, and cancer. It was originally identified as an oncogene as it is commonly mutated in cancers, particularly colon and thyroid carcinomas. TRKA is required for high-affinity binding tonerve growth factor (NGF), neurotrophin-3 and neurotrophin-4/5 but not brain-derived neurotrophic factor (BDNF). Known substrates for the Trk receptors are SHC1, PI 3-kinase, and PLC-gamma-1. NTRK1 has a crucial role in the development and function of the nociceptive reception system as well as the establishment of thermal regulation via sweating. It also activates ERK1 by either SHC1- or PLC-gamma-1-dependent signaling pathway. Defects in NTRK1 are a cause of congenital insensitivity to pain with anhidrosis and thyroid papillary carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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