目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T12432 | cGAS | ||
PF-06928215 是高亲和力 cGAS 抑制剂,IC50为 4.9 μΜ,亲和力 Kd 值为 0.2 μΜ。 | |||
T11673 | IRAK cGAS | ||
IRAK4-IN-4 (化合物 15) 是白介素-1 受体相关激酶抑制剂,IC50为 2.8 nM。它还抑制环 GMP-AM 合酶 ,IC50为 2.1 nM。 | |||
T9213 | cGAS | ||
G140 是选择性环状GMP-AMP 合酶抑制剂,具有抗炎活性,对 h-cGAS 和 m-cGAS 的IC50值分别为 14.0 和 442 nM。 | |||
T9119 | Others | ||
SU0268 是有效的 8-8-氧鸟嘌呤 DNA 糖基化酶1的选择性抑制剂,具有调控铜绿假单胞杆菌感染免疫反应的能力。 | |||
T11344 | DNA cGAS | ||
G150 是高选择性h-cGAS 抑制剂,IC50值为 10.2 nM,用于抑制 dsDNA 引发的干扰素表达。 | |||
T5486 | DNA cGAS | ||
RU.521 (RU3205217) 是选择性的环状 GMP-AMP 合成酶 (cGAS) 抑制剂,抑制 cGAS 介导的干扰素上调。它也抑制dsDNA 激活受体的活性,IC50为 700 nM。它可降低来自 Aicardi-Goutières 综合征小鼠模型的巨噬细胞中干扰素的组成型表达。 | |||
T78858 | |||
cGAS-IN-1(化合物C20)是一种黄酮类化合物,作为Cyclic GMP-AMP Synthase(cGAS)的抑制剂,其IC50分别为2.28 μM(针对人类cGAS)和1.44 μM(针对小鼠cGAS)。由于cGAS异常激活与众多免疫介导的炎症性疾病相关,cGAS-IN-1显示出了其抗炎潜力。 | |||
T61575 | DUB | ||
USP15-IN-1 是一种有效的 USP15 抑制剂(IC50 为 3.76 μM)。USP15-IN-1对非小细胞肺癌和白血病细胞具有高度的抗增殖活性 。USP15是 cGAS 的互作蛋白,并且 USP15可以促进 cGAS 识别DNA 激活下游信号通路。 | |||
T10065L | STING cGAS | ||
2',3'-cGAMP sodium (2'-3'-cyclic GMP-AMP sodium) 是一种cGAMP 合成酶(cGAS)影响细胞质DNA 产生的第二信使,是一种跨膜衔接蛋白,是细胞对致病性细胞质DNA 的先天免疫反应的关键组成部分。 | |||
T69663 | |||
G108 is a Novel h-cGAS specific inhibitor for repression of dsDNA-triggered interferon expression (IC50 of 27.5 nM and 5150 nM for h-cGAS and m-cGAS, respectively). |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPH-01166 | CGAS Protein, Human, Recombinant (His) | Human | E. coli | ||
CGAS Protein, Human, Recombinant (His) is expressed in E. coli.
|
|||||
TMPH-01055 | Caspase-1 Protein, Human, Recombinant (HA) | Human | E. coli | ||
Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides. Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a proinflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes. Cleaves a tetrapeptide after an Asp residue at position P1. Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD. In contrast to cleavage of interleukins IL1B and IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive. In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly.; Apoptosis inactive.; Apoptosis inactive.
|
|||||
TMPH-02315 | XRCC5 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA. Required for double-strand break repair and V(D)J recombination. Also has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and binds to the broken ends of the DNA and protects them from further resection. Binding to DNA may be mediated by XRCC6. The XRCC5-XRRC6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. The XRCC5-XRRC6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5-XRRC6 dimer together with APEX1 acts as a negative regulator of transcription. In association with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome. Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.
|
|||||
TMPH-02314 | XRCC5 Protein, Human, Recombinant (His & MBP) | Human | Baculovirus | ||
Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA. Required for double-strand break repair and V(D)J recombination. Also has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and binds to the broken ends of the DNA and protects them from further resection. Binding to DNA may be mediated by XRCC6. The XRCC5-XRRC6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. The XRCC5-XRRC6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5-XRRC6 dimer together with APEX1 acts as a negative regulator of transcription. In association with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome. Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.
|
|||||
TMPH-02521 | PYCARD Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing. Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA.
|