目录号 | 产品详情 | 靶点 | |
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T8865 | Others | ||
ASN03576800 是 VP40 基质蛋白的抑制剂。 | |||
T17946 | Others | ||
Fmoc-Ala-Ala-Asn(Trt)-OH 是一种可切割的 ADC 接头,用于抗体-药物偶联物。 | |||
TP2305 | Others | ||
pGlu-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-Val 是一种肽。 | |||
T30161 | P450 | ||
EN3356 是一种可口服且具有选择性的类固醇 17-α- 羟化酶/C17,20 裂解酶(CYP17A1 或 CYP17)抑制剂,是一种非甾体类裂解酶选择性化合物,具有潜在的抗雄激素和抗肿瘤活性。 | |||
T38984 | |||
Z-Ala-Ala-Asn-AMC, also known as Cbz-Ala-Ala-Asn-AMC, serves as a substrate for legumain. The overexpression of legumain in 293 HEK-Leg cells results in efficient cleavage of Cbz-Ala-Ala-Asn-AMC. | |||
T40139 | |||
H-Asn-Arg-OH is used for the solid-phase peptide synthesis. | |||
T14331 | JAK Syk | ||
Gusacitinib (ASN-002) 是一种有效的 SYK 激酶和JAK 激酶的双抑制剂,IC50值为 5 到 46 nM 之间,具有抗癌活性。 | |||
TN3748 | Others Endogenous Metabolite | ||
D-Asparagine (H-D-Asn-OH) 是酵母菌株的氮源。 D-Asparagine 是 L-Asparagine 水解的竞争性抑制剂 (Ki = 0.24 mM)。 | |||
T38116 | |||
Fmoc-Ala-Glu-Asn-Lys-NH2 is a peptide inhibitor that selectively targets asparagine endopeptidase (AEP) and inhibits the cleavage of amyloid precursor protein (APP). AEP, a pH-controlled cysteine proteinase, plays a crucial role in the proteolytic processing of APP, and its activity is enhanced during the aging process [1]. | |||
TP2506 | |||
Ser-Asn-Thr-Arg 是一种四肽化合物,是通过转录激活因子样效应子截断形成的化合物。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-02707 | PAH Protein, Human, Recombinant (415 Asn/Asp, His) | Human | Baculovirus-Insect Cells | ||
PAH (phenylalanine hydroxylase), also known as PH, belongs to the biopterin-dependent aromatic amino acid hydroxylase family. It contains 1 ACT domain, N-terminal region of PAH is thought to contain allosteric binding sites for phenylalanine and to constitute an "inhibitory" domain that regulates the activity of a catalytic domain in the C-terminal portion of the molecule. In humans, PAH is expressed both in the liver and the kidney, and there is some indication that it may be differentially regulated in these tissues. PAH catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine. It is one of three members of the pterin-dependent amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin and a non-heme iron for catalysis. Defects in PAH are the cause of phenylketonuria (PKU). PKU is an autosomal recessive inborn error of phenylalanine metabolism, due to severe phenylalanine hydroxylase deficiency. It is characterized by blood concentrations of phenylalanine persistently above 1200 mumol.
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TMPY-00723 | Contactin 3 Protein, Human, Recombinant (708 Asp/Asn, His) | Human | HEK293 | ||
Contactins are a subgroup of molecules belonging to the immunoglobulin superfamily that are expressed exclusively in the nervous system. The subgroup consists of six members: Contactin-1, Contactin-2 (TAG-1), Contactin-3 (BIG-1), BIG-2, Contactin-5 (NB-2) and NB-3. Since their identification in the late 1980s, Contactin-1 and Contactin-2 have been studied extensively. Axonal expression and the neurite extension activity of Contactin-1 and Contactin-2 attracted researchers to study the function of these molecules in axon guidance during development. Contactin-1 and Contactin-2 have come to be known as the principal molecules in the function and maintenance of myelinated neurons. In contrast, the function of the other four members of this subgroup remained unknown until recently. Contactin-3, also known as CNTN3 (BIG-1 in rat and PANG in mouse), is a GPI-linked glycoprotein that is expressed on cerebellar Purkinje cells, amygdaloid and thalamic neurons and olfactory granule cells. In the brain, Contactin-3 is expressed in frontal lobe, occipital lobe, cerebellum and amygdala. Contactin-3 contains 4 fibronectin type-III domains and 6 Ig-like C2-type (immunoglobulin-like) domains. Human Contactin-3 shares 92% aa identity with mouse Contactin-3. The exact function of Contactin-3 is unclear. Contactin-3 may mediate cell-cell interaction and may promote neurite outgrowth.
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TMPY-00722 | Contactin 3 Protein, Human, Recombinant (708 Asp/Asn, hFc) | Human | HEK293 | ||
Contactins are a subgroup of molecules belonging to the immunoglobulin superfamily that are expressed exclusively in the nervous system. The subgroup consists of six members: Contactin-1, Contactin-2 (TAG-1), Contactin-3 (BIG-1), BIG-2, Contactin-5 (NB-2) and NB-3. Since their identification in the late 1980s, Contactin-1 and Contactin-2 have been studied extensively. Axonal expression and the neurite extension activity of Contactin-1 and Contactin-2 attracted researchers to study the function of these molecules in axon guidance during development. Contactin-1 and Contactin-2 have come to be known as the principal molecules in the function and maintenance of myelinated neurons. In contrast, the function of the other four members of this subgroup remained unknown until recently. Contactin-3, also known as CNTN3 (BIG-1 in rat and PANG in mouse), is a GPI-linked glycoprotein that is expressed on cerebellar Purkinje cells, amygdaloid and thalamic neurons and olfactory granule cells. In the brain, Contactin-3 is expressed in frontal lobe, occipital lobe, cerebellum and amygdala. Contactin-3 contains 4 fibronectin type-III domains and 6 Ig-like C2-type (immunoglobulin-like) domains. Human Contactin-3 shares 92% aa identity with mouse Contactin-3. The exact function of Contactin-3 is unclear. Contactin-3 may mediate cell-cell interaction and may promote neurite outgrowth.
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TMPH-01029 | CAPN1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-387' and 'His-409'.
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TMPH-02557 | CAPN1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-388' and 'His-410'.
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TMPH-01512 | HIF1AN Protein, Human, Recombinant (His) | Human | Yeast | ||
Hydroxylates HIF-1 alpha at 'Asn-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.
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TMPH-01646 | MMP-20 Protein, Human, Recombinant (His & Myc) | Human | Baculovirus | ||
Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.
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TMPH-01647 | MMP-20 Protein, Human, Recombinant (E. coli, His & Myc) | Human | E. coli | ||
Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.
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TMPH-01789 | NUP98 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes. Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body).; (Microbial infection) Binds HIV-1 capsid-nucleocapsid (HIV-1 CA-NC) complexes and may thereby promote the integration of the virus in the host nucleus (in vitro). Binding affinity to HIV-1 CA-NC complexes bearing the capsid change ASN-74-ASP is reduced (in vitro).
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TMPJ-00694 | BRD4 Protein, Human, Recombinant (His & Flag) | Human | E. coli | ||
Bromodomain-containing protein 4 (BRD4) is a member of the BET class chromatin reader proteins that bind acetylated histones and play a key role in transcriptional regulation and transmission of epigenetic memory. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. BRD bromodomains serve as recognition motifs for acetylated lysine residues on histones, while the NET domain may function by promoting phosphorylation of the C-terminal domain (CTD) of RNA Polymerase II. Some specific inhibitors of BRD4 that prevent binding to acetylated histones by binding Asn-140 and Asn-433 are promising therapeutic molecules for the treatment of leukemias. BRD4 is a potential therapeutic target in many diseases including breast cancer, AML, multiple myeloma, colon cancer and others.
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TMPJ-01298 | PRADC1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
PRADC1, also known as C2orf7 or PAP21, is short for Protease-associated domain-containing protein 1. It is a 188 aa. with a 21 aa. signal, and the 171 located Asn can be glycosylated. PRADC1 has two mutagenesis which are N121Q and N171Q. This protein is secreted and highly expressed in skeletal muscle, heart and liver. It is expressed at intermediate level in kidney.
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TMPJ-00200 | EpCAM/TROP1 Protein, Mouse, Recombinant (hFc) | Mouse | Human Cells | ||
Epithelial Cellular Adhesion Molecule (Ep-CAM), also known as EGP314, mEGP314, Protein 289A, Tumor-associated calcium signal transducer 1, CD326, belongs to the EPCAM family. Its’ monomer subunit structure interacts with phosphorylated CLDN7. Ep-CAM may act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. It plays a role in embryonic stem cells proliferation and differentiation. It also up-regulates the expression of FABP5, MYC and cyclins A and E. The post-translational modification glycosylation at Asn-198 is crucial for protein stability.
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TMPH-00617 | MazF Protein, E. coli, Recombinant (His) | E. coli | Yeast | ||
Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific endoribonuclease it inhibits protein synthesis by cleaving mRNA and inducing bacterial stasis. It is stable, single-strand specific with mRNA cleavage independent of the ribosome, although translation enhances cleavage for some mRNAs. Cleavage occurs at the 5'-end of ACA sequences, yielding a 2',3'-cyclic phosphate and a free 5'-OH, although cleavage can also occur on the 3'-end of the first A. Digests 16S rRNA in vivo 43 nts upstream of the C-terminus; this removes the anti-Shine-Dalgarno sequence forming a mixed population of wild-type and 'stress ribosomes'. Stress ribosomes do not translate leader-containing mRNA but are proficient in translation of leaderless mRNA, which alters the protein expression profile of the cell; MazF produces some leaderless mRNA. The toxic endoribonuclease activity is inhibited by its labile cognate antitoxin MazE. Toxicity results when the levels of MazE decrease in the cell, leading to mRNA degradation. This effect can be rescued by expression of MazE, but after 6 hours in rich medium overexpression of MazF leads to programmed cell death. MazF-mediated cell death occurs following a number of stress conditions in a relA-dependent fashion and only when cells are in log phase; sigma factor S (rpoS) protects stationary phase cells from MazF-killing. Cell growth and viability are not affected when MazF and MazE are coexpressed. Both MazE and MazE-MazF bind to the promoter region of the mazE-mazF operon to inhibit their own transcription. MazE has higher affinity for promoter DNA in the presence of MazF. Cross-talk can occur between different TA systems, ectopic expression of this toxin induces transcription of the relBEF TA system operon with specific cleavage of the mRNA produced.; Might also serve to protect cells against bacteriophage; in the presence of MazE-MazF fewer P1 phages are produced than in a disrupted strain. For strain K38 most wild-type cells are killed but not by phage lysis; it was suggested that MazE-MazF causes P1 phage exclusion from the bacterial population. This phenomenon is strain dependent.; The physiological role of this TA system is debated. Programmed cell death (PCD) occurs when cells are at high density and depends on the presence of MazE-MazF and a quorum sensing pentapeptide, the extracellular death factor (EDF) with sequence Asn-Asn-Trp-Asn-Asn (NNWNN), probably produced from the zwf gene product glucose-6-phosphate 1-dehydrogenase. Cell death governed by the MazE-MazF and DinJ-YafQ TA systems seems to play a role in biofilm formation, while MazE-MazF is also implicated in cell death in liquid media. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment. In conjunction with EDF prevents apoptotic-like death (ALD) in the presence of DNA damaging agents, probably by reducing recA mRNA levels in a non-endonuclease-mediated manner. Other studies (in strains BW25113 and MC4100, the latter makes EDF) demonstrate MazF does not cause PCD but instead bacteriostasis and possibly a dormant state as well as persister cell generation.
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TMPY-02050 | DDOST Protein, Human, Recombinant | Human | E. coli | ||
The enzyme oligosaccharyltransferase (dolichyl-diphosphooligosaccharide-protein glycosyltransferase) (DDOST), or 48-kDa subunit (OST48) is one of the catalytic subunits in this complex, exerts a typical type I membrane topology, containing a large luminal domain, a hydrophobic transmembrane domain and a short cytosolic peptide tail. DDOST/OST48 catalyzes the transfer of a high-mannose oligosaccharide (GlcNac2Man9Glc3) from a dolichol-linked oligosaccharide donor (dolichol-P-GlcNac2Man9Glc3) onto the asparagine acceptor site within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains across the membrane of the endoplasmic reticulum. The mammalian oligosaccharyltransferase (OST) is an oligomeric complex composed of three type I transmembrane proteins of the endoplasmic reticulum: ribophorin I (RI), ribophorin II (RII), and OST48. OST48 is not a glycoprotein and is not recognized by antibodies to either ribophorin. Like ribophorins I and II, OST48 was found to be an integral membrane protein, with the majority of the polypeptide located within the lumen of the endoplasmic reticulum (ER). OST48 does not show significant amino acid sequence homology to either ribophorin I or II. It had been found that only the luminal domain of RI contains ER retention information. The dilysine motif in OST48 functions as an ER localization motif because OST48 in which the two lysine residues are replaced by serine (OST48ss) is no longer retained in the ER and is found instead also at the plasma membrane.
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TMPY-06585 | C1s Protein, Human, Recombinant (His) | Human | HEK293 | ||
Complement is an integral component of the adaptive and innate immune systems and represents one of the major effector systems for the immune responses. The classical complement pathway is triggered by C1, a complex composed of the binding protein C1q and two proenzymes, C1r and C1s. Upon binding of IgG to the head of C1q, C1r undergoes autoactivation and in turn cleaves and activates C1s. C1r and C1s, the proteases responsible for activation and proteolytic activity of the C1 complex of complement, share similar overall structural organizations featuring five nonenzymic protein modules (two CUB modules surrounding a single EGF module, and a pair of CCP modules) followed by a serine protease domain. Besides highly specific proteolytic activities, both proteases exhibit interaction properties associated with their N-terminal regions. In contrast, C1r and C1s widely differ from each other by their glycosylation patterns: both proteins contain Asn-linked carbohydrates, but four glycosylation sites are present on C1r, and only two on C1s. As a highly specific serine protease, C1s executes the catalytic function of the C1 complex: the cleavage of C4 and C2, and thus instigates a sequence of activation steps of other components of the complement system, culminating in the formation of the membrane attack complex which induces cell lysis. Like other complement serine proteases C1s has restricted substrate specificity and it is engaged into specific interactions with other subcomponents of the complement system. The only other protein known to interact with C1s physiologically is SerpinC1, an inhibitor of serine protease, which inhibits C1s activity and thus plays a regulatory role in controlling the function of C1s enzyme.
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