目录号 | 产品详情 | 靶点 | |
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T77575 | P-gp | ||
P-gb-IN-1 是一种有效的 P-糖蛋白 (P-gp) 抑制剂,通过抑制 P-gp 外流展现出逆转活性。P-gb-IN-1 通过与残基 Asn 721 和 Met 986 形成氢键相互作用从而显示出对 P-gp 的抑制作用。P-gb-IN-1 在 MCF-7/ADR 细胞中显示出低毒性。 | |||
TP2178 | Others | ||
β-Interleukin II is a peptide with the sequence NH2-ILE-LEU-ASN-GLY-ILE-ASN-ASN-TYR-LYS-ASN-PRO-LYS-LEU-COOH. | |||
TP2230 | Others | ||
Fusion glycoprotein (92-106) [Human respiratory syncytial virus] is a peptide with the sequence H2N-Glu-Leu-Gln-Leu-Leu-Met-Gln-Ser-Thr-Pro-Pro-Thr-Asn-Asn-Arg-OH, MW= 1741.96. | |||
TP2177 | Others | ||
Amyloid precursor c-terminal peptide has the amino acid sequence Gly-Tyr-Glu-Asn-Pro-Thr-Tyr-Lys-Phe-Phe-Glu-Gln-Met-Gln-Asn. APP is best known as the precursor molecule whose proteolysis generates beta-amyloid (Aβ), a 37 to 49 amino acid peptide whose am | |||
TP2214 | Others | ||
Adrenomedullin (AM) (1-12), human, is a peptide with the sequence Tyr-Arg-Gln-Ser-Met-Asn-Asn-Phe-Gln-Gly-Leu-Arg. Adrenomedullin (AM) (1-12), human, was initially identified as a vasodilator, and as such, it has the ability to relax vascular tone. Other | |||
TP2255 | Others | ||
Heparin cofactor II precursor fragment [Homo sapiens] is a peptide with the sequence H2N-Tyr-Glu-Ile-Thr-Thr-Ile-His-Asn-Leu-Phe-Arg-OH, MW=1406.58. | |||
TP1386 | |||
Mastoparan is a peptide toxin from wasp venom. It has the chemical structure Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-Ala-Lys-Lys-Ile-Leu-NH2. | |||
TP2269 | Others | ||
This Mitogen-activated protein kinase (MAP kinase) fragment has a peptide sequence of Lys-Tyr-Ile-His-Ser-Ala-Asn-Val-Leu. The MAP kinases are serine/threonine-specific protein kinases belonging to the CMGC (CDK/MAPK/GSK3/CLK) kinase group. | |||
TP2281 | Others | ||
p53 tumor suppressor fragment (232-240) is a peptide with the sequence H2N-Lys-Tyr-Met-Cys-Asn-Ser-Ser-Cys-Met-OH, MW= 1066.3. p53 is a tumor suppressor protein that in humans is encoded by the TP53 gene. p53 is crucial in multicellular organisms, where i | |||
TP2195 | Others | ||
Nitric Oxide Synthase (599-613) Blocking Peptide, Bovine Endothelial Cell (Ac-Pro-Tyr-Asn-Ser-Ser-Pro-Arg-Pro-Glu-Gln-His-Lys-Ser-Tyr-Lys-Cys) is a peptide that inhibits the function of NOSs as a result it blocks the production of NO. Because of the invol |
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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