目录号 | 产品详情 | 靶点 | |
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T76329 | |||
[Asn18] Endothelin-1, human 为一种多肽,属于内皮素家族中的主要亚型,关键于血管功能调节。 | |||
T83541 | |||
(Gln22,Asn23)-Amyloid β-Protein (1-40) 为特定多肽,主要应用于研究脑淀粉样血管病的相关突变。 | |||
T83507 | |||
[Asn23] β-Amyloid (1-40), Iowa mutation 是一种与重度大脑淀粉样蛋白血管病 (CAA) 相关的生物活性肽。该突变涉及 APP 694 位点的错义突变,Asp 23 位置的天冬酰胺被天冬酰氨酸取代。这种变异的 β-Amyloid 肽倾向于更快聚集,并形成有害的原纤维。 | |||
T64688 | |||
(H-Tyr-Ile-Asn-Leu-Cys-Thr-Arg-Nva-Arg-Tyr-NH2)2 trifluoroacetate 是一种有用的有机化合物,可用于生命科学领域的相关研究,其产品编号为 T64688。 | |||
T83506 | |||
[Asn23]-beta-Amyloid (1-42), iowa mutation 是具有生物活性的肽,与阿尔茨海默病中的一种严重神经病理状况——大脑淀粉样蛋白血管病 (CAA) 密切相关。这种变异是由于在 APP 694 位点发生了错义突变,其中 Asp 23 被 Asn 取代,导致的。该变异形式的β-淀粉样肽倾向于更快聚集,形成具有毒性的原纤维。 | |||
T76586 | |||
(Asn10,Leu11,D-Trp12)-pTH-Related Protein (7-34) amide (human, mouse, rat) 是一种有效的 PTH-1R 拮抗剂。 | |||
T12929 | Others | ||
SKF-34288 hydrochloride (3-Mercaptopicolinic acid hydrochloride) 是一种磷酸烯醇丙酮酸羧激酶抑制剂。它抑制 Asn 代谢并导致氨基酸和酰胺的增加。它通过糖异生途径中 PEPCK 的特异性抑制来抑制葡萄糖合成,是降血糖药。 | |||
T21798L | GTPase | ||
Dynamin inhibitory peptide Acetate 是一种具有序列 Gln-Val-Pro-Ser-Arg-Pro-Asn-Arg-Ala-Pro 的肽,可抑制 GTPase dynamin。 | |||
TP1386L1 | Others | ||
Mastoparan acetate(72093-21-1 free base) 是一种来自黄蜂毒液的肽毒素。它的化学结构为 Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-Ala-Lys-Lys-Ile-Leu-NH2。 | |||
T21662L | Others | ||
Cadherin Peptide, avian Acetate 是一种肽,序列为 Leu-Arg-Ala-His-Ala-Val-Asp-Val-Asn-Gly-NH2。钙粘蛋白是一类 1 型跨膜蛋白。 |
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-00722 | Contactin 3 Protein, Human, Recombinant (708 Asp/Asn, hFc) | Human | HEK293 Cells | ||
Contactin 3 Protein, Human, Recombinant (708 Asp/Asn, hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 134.5 kDa and the accession number is Q9P232.
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TMPY-00723 | Contactin 3 Protein, Human, Recombinant (708 Asp/Asn, His) | Human | HEK293 Cells | ||
Contactin 3 Protein, Human, Recombinant (708 Asp/Asn, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 109.2 kDa and the accession number is Q9P232.
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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'. CAPN1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 85.9 kDa and the accession number is P07384.
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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 | P. pastoris (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-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-01646 | MMP-20 Protein, Human, Recombinant (His & Myc) | Human | Baculovirus Insect Cells | ||
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-00130 | Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B Protein, Aspergillus phoenicis, Recombinant (His & Myc) | Aspergillus phoenicis | E. coli | ||
Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2). Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B Protein, Aspergillus phoenicis, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 61.3 kDa and the accession number is Q12563.
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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 | HEK293 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 | HEK293 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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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 Cells | ||
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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