目录号 | 产品详情 | 靶点 | |
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T20539 | AChE Parasite | ||
Pirimiphos-methyl (AI3-27699) 是一种速效有机磷杀虫剂和杀螨剂,对目标生物的乙酰胆碱酯酶有抑制作用。甲基嘧啶磷常用于农粮贮藏过程中甲虫、鼻甲虫、飞蛾和蝽蛄的防治。 | |||
T5220 | Others Endogenous Metabolite | ||
D-(-)-Lactic acid sodium (Sodium D-lactate) 是一种有机酸。它是一种手性分子,由 L-乳酸和 D-乳酸两种光学异构体组成,其中 L-异构体在生物体中最常见。D-(-)-Lactic acid sodium 也是一种微生物代谢产物。 | |||
T4749 | Reactive Oxygen Species Endogenous Metabolite Antifungal | ||
Squalene (AddaVax) 是胆固醇合成的中间产物,具有降血脂、保肝、心脏保护、抗氧化和抗毒活性等多种药理特性。它还具有抗真菌活性,可用于毛癣菌治疗的相关研究。 | |||
T1438 | Estrogen/progestogen Receptor Antifungal | ||
Butoconazole nitrate (RS 35887) 是一种咪唑类抗真菌药物,可治疗由白色念珠菌引起的阴道感染。它可通过抑制类固醇合成起到抗菌作用。 | |||
T3138 | Reactive Oxygen Species PPAR | ||
Astaxanthin (trans-Astaxanthin) 是可从雨生红球藻等多种海洋生物中提取得到的红色类胡萝卜素,是过氧化物酶体增殖物活化受体γ 的调节剂,具有抗增殖、神经保护作用和抗炎活性。它是一种抗氧化剂,有用于癌症和心血管疾病的研究潜力,作为颜色添加剂用于动物食品中。 | |||
T4713 | Others Endogenous Metabolite | ||
Phosphorylcholine chloride calcium salt tetrahydrate (Phosphocholine chloride calcium salt tet) 是内源性代谢产物的一种。 | |||
T65979 | Nucleoside Antimetabolite/Analog | ||
Adenosine 5'-monophosphate disodium salt (Adenosine Phosphate Disodium) 是一种参与 ATP 代谢的嘌呤核苷酸,用于研究 ATP 对细胞和生物体的影响。Adenosine 5'-monophosphate disodium salt 已被证明具有多种生化和生理作用,它可以促进细胞代谢、基因表达和蛋白质合成。 | |||
T9492 | Others | ||
3-METHOXY-DL-TYROSINE 是一种在人体和许多其他生物体中发现的天然氨基酸,是一种非必需氨基酸。它是神经递质多巴胺的前体,参与大脑中多巴胺水平的调节,在多种疾病中有潜在治疗应用,包括帕金森病、抑郁症和肥胖症。 | |||
T1631 | Antibacterial Antibiotic | ||
Sulbactam (CP45899) 是一种竞争性、不可逆的 β-内酰胺酶抑制剂,抑制耐多药不动杆菌-鲍曼不动杆菌复合物。它具有抗菌活性。 | |||
T19281L | Others | ||
Dihydroxyacetone phosphate hemimagnesium salt hydrate 也称为磷酸二羟基丙酮或 3-羟基-2-氧代丙基磷酸。 Dihydroxyacetone phosphate hemimagnesium salt hydrate 存在于从细菌到人类的所有生物中。在人类体内, Dihydroxyacetone phosphate hemimagnesium salt hydrate参与许多酶促反应。 Dihydroxyacetone phosphate hemimagnesium salt hydrate 已被研究用于治疗淋巴瘤、大细胞淋巴瘤、弥漫性淋巴瘤。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-00392 | PAM Protein, Human, Recombinant (His) | Human | HEK293 | ||
Peptidylglycine alpha-amidating monooxygenase (PAM) is highly expressed in neurons and endocrine cells, where it catalyzes one of the final steps in the biosynthesis of bioactive peptides. PAM is also expressed in unicellular organisms such as Chlamydomonas reinhardtii, which do not store peptides in secretory granules. As for other granule membrane proteins, PAM is retrieved from the cell surface and returned to the trans-Golgi network. This pathway involves regulated entry of PAM into multivesicular body intralumenal vesicles (ILVs). Peptidylglycine alpha-amidating monooxygenase (PAM) is an essential enzyme that catalyzes the COOH-terminal amidation of many neuroendocrine peptides.
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TMPY-00382 | Thioredoxin/TRX Protein, Mouse, Recombinant | Mouse | E. coli | ||
Thioredoxin, also known as ATL-derived factor, Surface-associated sulphydryl protein, SASP and TXN, is a nucleus, cytoplasm and secreted protein that belongs to the thioredoxin family. Thioredoxins are proteins that act as antioxidants by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange. Thioredoxins are found in nearly all known organisms and are essential for life in mammals. Thioredoxin / TXN participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Thioredoxin / TXN plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Thioredoxin / TXN nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Thioredoxin / TXN induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
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TMPY-01371 | IL-17RA Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-03565 | Mannan Binding Lectin/MBL2 Protein, Human, Recombinant | Human | CHO | ||
MBL (mannose-binding lectin) is primarily a liver-derived collagen-like serum protein, which binds sugar structures on micro-organisms and dying host cells and is one of the four known mediators that initiate activation of the complement system via the lectin pathway. MBL and the ficolins (Ficolin-1, Ficolin-2, and Ficolin-3) are soluble collagen-like proteins that are involved in innate immune defense. They bind sugar structures or acetylated compounds present on microorganisms and dying host cells and they initiate activation of the lectin complement pathway in varying degrees. MBL2 encodes the mannose-binding lectin, which is a key player in the innate immune system and has recently been found to play a role in the development of type 1 diabetes and gestational diabetes mellitus. Common variant alleles situated both in the promoter and structural regions of the MBL2 gene influence the stability and the serum concentration of the protein. Several polymorphisms in the promoter and structural regions of MBL2 adversely affect the plasma concentration and the oligomeric state of MBL. The possession of mutant alleles has been linked to disease outcomes for a variety of bacterial and viral infections. Mutant MBL2 haplotypes have been linked to disease progression and response to therapy in HCV infection.
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TMPH-00345 | Catalase Protein, Capsicum annuum, Recombinant (His) | Capsicum annuum | E. coli | ||
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
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TMPH-00080 | Catalase-2 Protein, Arabidopsis thaliana, Recombinant (His & SUMO) | Arabidopsis thaliana | E. coli | ||
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
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TMPH-00384 | Vitellogenin-1 Protein, Chicken, Recombinant (His) | Chicken | E. coli | ||
Precursor of the egg-yolk proteins that are sources of nutrients during early development of oviparous organisms.; Phosvitin is believed to be of importance in sequestering calcium, iron and other cations for the developing embryo.
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TMPK-00236 | CEACAM8 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Eosinophils and their products are likely important in the pathophysiology of allergic diseases, such as bronchial asthma, and in host immunity to parasitic organisms. CD66b (CEACAM8, CGM6, NCA-95) is a single chain, GPI-anchored, highly glycosylated protein belonging to the carcinoembryonic Ag supergene family. CD66b is an activation marker for human granulocytes.
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TMPJ-00823 | UBB Protein, Human, Recombinant | Human | E. coli | ||
Polyubiquitin-B(UBB) is one of Ubiquitins. Ubiquitin is one of the most conserved proteins known in eukaryotic organisms. Ubiquitin is required for ATP-dependent, non-lysosomal intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation.
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TMPJ-00882 | Desmin Protein, Human, Recombinant (His) | Human | E. coli | ||
Desmin is a cytoplasmic protein and belongs to the intermediate filament family. interacts with DST and MTM1. Desmin is only expressed in vertebrates, however homologous proteins are found in many organisms. Desmin is the main intermediate filament in mature skeletal, cardiac and smooth-muscle cells. DES founctions as homopolymers to form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. .Defects in DES are cause of the myopathy myofibrillar type 1, cardiomyopathy dilated type 1I, and neurogenic scapuloperoneal syndrome Kaeser type.
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TMPY-02209 | CUTC Protein, Human, Recombinant (His) | Human | E. coli | ||
Copper homeostasis protein cutC homolog, also known as CGI-32 and CUTC, is a cytoplasm and nucleus protein which belongs to theCutC family. CUTC may play a role in copper homeostasis. It can bind one Cu1+per subunit. Copper is an essential trace element to life and particularly plays a pivotal role in the physiology of aerobic organisms. Copper is a micronutrient that is required for proper metabolic functioning of most prokaryotic and eukaryotic organisms. To sustain an adequate supply of copper, a cell requires molecular mechanisms that control the metal content to avoid copper toxicity. This toxicity comes primarily from the reactivity of copper, which can lead to the generation of free radicals. In bacteria, two independent systems are responsible for maintaining the balance of copper within the cells ( Cop and Cut family proteins ). The Cut protein family is associated with copper homeostasis and involved in uptake, storage, delivery, and efflux of copper. CutC is a member of the Cut family and is suggested to be involved in efflux trafficking of cuprous ion. CutC is able to respond transcriptionally to copper and to participate in the control of copper homeostasis in E. faecalis.
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TMPJ-00764 | Catalase/CAT Protein, Human, Recombinant | Human | E. coli | ||
Catalase (CAT) is a member of the catalase family. It exists as a homotetramer that occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Catalase is localized in the peroxisome. Catalase promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells, and normal and transformed fibroblast cells. Defects in CAT are the cause of acatalasemia which is characterized by absence of catalase activity in red cells and is associated with ulcerating oral lesions.
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TMPY-03990 | Profilin 4 Protein, Human, Recombinant (His) | Human | E. coli | ||
PFN4, also known as profilin 4, is a member of the profilin family. Profilin can be detected in all eukaryotic organisms. It plays an important role in the spatially and temporally controlled growth of actin microfilaments. Profilin is one of the most abundant actin monomer binders, but proteins such as CAP and (in mammals) thymosin β4 have some functional overlaps with profilin. In contrast, ADF/cofilin has some properties that antagonize profilin action. PFN4 also functions in the dynamic turnover and restructuring of the actin cytoskeleton.
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TMPJ-00048 | CYPA Protein, Mouse, Recombinant | Mouse | E. coli | ||
Peptidyl-prolyl cis-trans isomerase A is a cytoplasm protein which belongs to the cyclophilin-type PPIase family and PPIase A subfamily. Cyclophilins(CyPs) are a family of proteins found in organisms ranging from prokaryotes to humans. These molecules exhibit peptidyl-prolyl isomerase activity, suggesting that they influence the conformation of proteins in cells. Cyclophilin A accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Cyclophilin A can interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions.
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TMPK-00073 | TDGF1/Cripto Protein, Human, Recombinant (His) | Human | HEK293 | ||
TDGF1 (CRIPTO) is a member of the epidermal growth factor-Cripto-1/FRL-1/Cryptic (EGF/CFC) gene family and an obligate co-receptor involved in NODAL signaling, a developmental program implicated in midline, forebrain, and left-right axis development in model organisms. Cripto-1 is enriched in a subpopulation of embryonal, melanoma, prostate, and pancreatic cancer cells that possess stem-like characteristics. Therefore, Cripto-1 may play a role during developmental EMT, and it may also be involved in the reprogramming of differentiated tumor cells into cancer stem cells through the induction of an EMT program.
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TMPY-03619 | p67phox Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
NCF2 (Neutrophil Cytosolic Factor 2, also known as NCF-2 and p67phox) is a Protein Coding gene. 4 alternatively spliced human isoforms have been reported. This gene encodes neutrophil cytosolic factor 2, the 67-kilodalton cytosolic subunit of the multi-protein NADPH oxidase complex found in neutrophils. This oxidase produces a burst of superoxide which is delivered to the lumen of the neutrophil phagosome. NCF2 belongs to the NCF2/NOXA1 family. NCF2, NCF1, and a membrane-bound cytochrome b558 are required for activation of the latent NADPH oxidase. Mutations in the NCF2 gene, as well as in other NADPH oxidase subunits, can result in chronic granulomatous disease, a disease that causes recurrent infections by catalase-positive organisms.
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TMPY-00149 | PAM Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Peptidylglycine alpha-amidating monooxygenase (PAM) is highly expressed in neurons and endocrine cells, where it catalyzes one of the final steps in the biosynthesis of bioactive peptides. PAM is also expressed in unicellular organisms such as Chlamydomonas reinhardtii, which do not store peptides in secretory granules. As for other granule membrane proteins, PAM is retrieved from the cell surface and returned to the trans-Golgi network. This pathway involves regulated entry of PAM into multivesicular body intralumenal vesicles (ILVs). Peptidylglycine alpha-amidating monooxygenase (PAM) is an essential enzyme that catalyzes the COOH-terminal amidation of many neuroendocrine peptides.
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TMPY-04336 | Orange fluorescent protein Protein, Discosoma sp, Recombinant (His) | Discosoma sp | E. coli | ||
OFPSparkTM is a red (orange) fluorescent protein (excitation/emission maxima are 549 and 566 nm, respectively) derived from DsRed. Possessing high photostability and pH stability, OFPSparkTM is more than twice brighter than mOrange2. Fast OFPSparkTM maturation makes it detectable in mammalian cells as early as within 8 hrs after transfection. OFPSparkTM can be expressed and detected in a wide range of organisms. Mammalian cells transiently transfected with OFPSparkTM expression vectors produce bright fluorescence in 8 hrs after transfection. No cytotoxic effects or visible protein aggregation are observed. For its monomer structure, OFPSparkTM performs well in some fusions and protein labeling applications.
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TMPJ-01321 | MAP1LC3B Protein, Human, Recombinant | Human | E. coli | ||
Microtubule-associated proteins 1A/1B light chain 3B (MAP1LC3B) is a member of the highly conserved ATG8 protein family. ATG8 proteins are present in all known eukaryotic organisms. MAP1LC3B is one of the four genes in the MAP1LC3 subfamily (others include MAP1LC3A, MAP1LC3C, and MAP1LC3B2). It is moat abundantly expressed in heart, brain, skeletal muscle and testis. LMAP1LC3B is a subunit of neuronal microtubule and functions in formation of autophagosomal vacuoles (autophagosomes). It associated MAP1A and MAP1B proteins, which are involved in microtubule assembly and important for neurogenesis. MAP1LC3B also plays a role in autophagy, a process that involves the bulk degradation of cytoplasmic component.
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TMPY-03390 | LSM1 Protein, Human, Recombinant (His) | Human | E. coli | ||
LSM1 is an Sm-like protein. Sm-like proteins can be detected in a variety of organisms based on sequence homology with the Sm protein family. Sm-like proteins include the Sm sequence motif, which consists of two regions separated by a linker of variable length that folds as a loop. The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing. LSM1 has a role in replication-dependent histone mRNA degradation and binds specifically to the 3''-terminal U-tract of U6 snRNA. LSM1 also facilitates RNA protein interactions and structural modifications which are required during ribosomal subunit assembly.
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TMPJ-01147 | Cld Protein, Dechloromonas aromatica, Recombinant (His) | Dechloromonas aromatica | E. coli | ||
Chlorite dismutase (Cld) found in prokaryotic organisms, also known as Chlorite O2-lyase, is a b-type heme containing enzyme that catalyzes the reduction of chlorite into chloride plus dioxygen. The subunit of chlorite dismutase consists of a heme free N-terminal and a heme b containing C-terminal ferredoxin-like fold with high structural homology to the dye-decolorizing peroxidases (DyPs). The physiological role of Cld in prokaryote has been shown that some microorganisms can use perchlorate or chlorate as terminal electron acceptors for anaerobic respiration thereby producing chlorite that must be detoxified. This enzyme has gained attention because it can be used in the development of bioremediation processes, biosensors, and controlled dioxygen production.
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TMPY-04770 | RIOK1 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
RIOK1, also known as RIO kinase 1, is a member of the RIO family of atypical serine protein kinases first characterized in yeast. RIOK1 and RIOK2 proteins are present in organisms from Archaea to humans. RIOK1 functions as a new interactor of protein arginine methyltransferase 5 (PRMT5), competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity. RioK1 and pICln bind to PRMT5 in a mutually exclusive fashion. This results in a PRMT5-WD45/MEP5 core structure that either associates with pICln or RioK1 RIOK1 in distinct complexes. RIOK1 functions in analogy to pICln as an adapter protein by recruiting the RNA-binding protein nucleolin to the PRMT5 complex for its symmetrical methylation.
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TMPY-02306 | MAB21L2 Protein, Human, Recombinant (His & ZZ) | Human | E. coli | ||
MAB21L2 (Mab-21 Like 2) is a Protein Coding gene. It encodes a protein similar to C. elegans mab-21 cell fate-determining factor. The protein encoded by this gene is primarily nuclear, although some cytoplasmic localization has been observed. MAB21L2 belongs to the mab-21 family. It is required for several aspects of embryonic development including normal development of the eye. It is thought that this gene may also be involved in neural development. The identification of MAB21L2 as a novel factor involved in human coloboma and highlight the power of genome editing manipulation in model organisms for analysis of the effects of whole-exome variation in humans. Diseases associated with MAB21L2 include Microphthalmia/Coloboma And Skeletal Dysplasia Syndrome and Microphthalmia.
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TMPY-03660 | p67phox Protein, Human, Recombinant | Human | Baculovirus-Insect Cells | ||
NCF2 (Neutrophil Cytosolic Factor 2, also known as NCF-2 and p67phox) is a Protein Coding gene. 4 alternatively spliced human isoforms have been reported. This gene encodes neutrophil cytosolic factor 2, the 67-kilodalton cytosolic subunit of the multi-protein NADPH oxidase complex found in neutrophils. This oxidase produces a burst of superoxide which is delivered to the lumen of the neutrophil phagosome. NCF2 belongs to the NCF2/NOXA1 family. NCF2, NCF1, and a membrane-bound cytochrome b558 are required for activation of the latent NADPH oxidase. Mutations in the NCF2 gene, as well as in other NADPH oxidase subunits, can result in chronic granulomatous disease, a disease that causes recurrent infections by catalase-positive organisms.
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TMPY-03473 | MBL1 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
Mannose-binding lectin (MBL), also named mannose or mannan-binding protein (MBP), is a C-type lectin that participates in the innate immune system as an activator of the complement system and as opsonin after binding to certain carbohydrate structures on microorganisms and pathogens. Its function appears to be pattern recognition in the first line of defense in the pre-immune host. MBL recognizes carbohydrate patterns found on the surface of a large number of pathogenic micro-organisms including bacteria, viruses, protozoa, and fungi. The binding of MBL to a micro-organism results in activation of the lectin pathway of the complement system. Two forms of MBL, MBL-A, and MBL-C were characterized in rodents, rabbits, bovine, and rhesus monkeys, whereas only one form was identified in humans, chimpanzees, and chickens. The two forms are encoded by two distinct genes named MBL1 and MBL2, which have been identified in many species including the pig. The MBL1 and MBL2 genes encode mannan-binding lectins (MBL) A and C, respectively, that are collagenous lectins (collectins) produced mainly by the liver. The MBL1 gene encodes MBL-A, which has bacteria-binding properties in pigs and rodents but is mutated to a pseudogene in humans and chimpanzees. Deficiency of MBL is probably the most common human immunodeficiency and is associated with an increased risk of mucosally acquired infections including meningococcal disease. MBL could modify disease susceptibility by modulating macrophage interactions with mucosal organisms at the site of initial acquisition.
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TMPY-00993 | MBL1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Mannose-binding lectin (MBL), also named mannose or mannan-binding protein (MBP), is a C-type lectin that participates in the innate immune system as an activator of the complement system and as opsonin after binding to certain carbohydrate structures on microorganisms and pathogens. Its function appears to be pattern recognition in the first line of defense in the pre-immune host. MBL recognizes carbohydrate patterns found on the surface of a large number of pathogenic micro-organisms including bacteria, viruses, protozoa, and fungi. The binding of MBL to a micro-organism results in activation of the lectin pathway of the complement system. Two forms of MBL, MBL-A, and MBL-C were characterized in rodents, rabbits, bovine, and rhesus monkeys, whereas only one form was identified in humans, chimpanzees, and chickens. The two forms are encoded by two distinct genes named MBL1 and MBL2, which have been identified in many species including the pig. The MBL1 and MBL2 genes encode mannan-binding lectins (MBL) A and C, respectively, that are collagenous lectins (collectins) produced mainly by the liver. The MBL1 gene encodes MBL-A, which has bacteria-binding properties in pigs and rodents but is mutated to a pseudogene in humans and chimpanzees. Deficiency of MBL is probably the most common human immunodeficiency and is associated with an increased risk of mucosally acquired infections including meningococcal disease. MBL could modify disease susceptibility by modulating macrophage interactions with mucosal organisms at the site of initial acquisition.
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TMPY-04476 | MVK Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
Mevalonate kinase belongs to the GHMP kinase family, Mevalonate kinase subfamily. It can be found in a wide variety of organisms from bacteria to mammals. Mevalonate kinase may be a regulatory site in the cholesterol biosynthetic pathway. Defects in mevalonate kinase can cause mevalonic aciduria (MEVA). It is an accumulation of mevalonic acid which causes a variety of symptoms such as psychomotor retardation, dysmorphic features, cataracts, hepatosplenomegaly, lymphadenopathy, anemia, hypotonia, myopathy, and ataxia. Defects in mevalonate kinase can also cause hyperimmunoglobulinemia D and periodic fever syndrome (HIDS). HIDS is an autosomal recessive disease characterized by recurrent episodes of unexplained high fever associated with skin rash, diarrhea, adenopathy (swollen, tender lymph nodes), arthralgias, and/or arthritis.
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TMPJ-00761 | FTH Protein, Human, Recombinant (His) | Human | E. coli | ||
Ferritin heavy polypeptide 1(FTH1), is a ubiquitous intracellular protein which stores iron in a soluble, non-toxic, readily available form. FTH1 has ferroxidase activity and is important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Ferritin is composed of 24 subunits of the light and heavy ferritin chains. It plays a role in delivery of iron to cells and mediates iron uptake in capsule cells of the developing kidney. Variation of ferritin subunit composition may affect iron absorption and release in different tissues. Deficiency of ferritin proteins may cause several neurodegenerative diseases. Almost all living organisms can produce this protein, including algae, bacteria, higher plants, and animals.
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TMPY-03457 | ERH Protein, Human, Recombinant (His) | Human | E. coli | ||
ERH(enhancer of rudimentary homolog) belongs to the E(R) family. It is expressed in all tissues examined. The monomeric structure of ERH comprises a single domain consisting of three α-helices and four β-strands, which is a novel fold. In the crystal structure, ERH assumes a dimeric structure, through interactions between the β-sheet regions. The formation of an ERH dimer is consistent with the results of analytical ultracentrifugation. ERH may have a role in the cell cycle. The Drosophila protein ERH is a small protein of 14 amino acids. It has been found to be an enhancer of the rudimentary gene, involved in pyrimidine biosynthesis. From an evolutionary point of view, ERH is highly conserved and has been found to exist in probably all multicellular eukaryotic organisms. ERH interacts with POLDIP3.
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TMPY-02582 | Ferritin light chain Protein, Human, Recombinant (His) | Human | E. coli | ||
Ferritin, light polypeptide (FTL) is the light subunit of the ferritin protein. Ferritin is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Storage of iron in the tissues occurs in the form of ferritin and hemosiderin. The latter originates from ferritin that has undergone intracellular digestion of its protein shell, leaving the iron core. Ferritin and hemosiderin are components of a continuum. Ferritin has been identified in all types of living organisms: animals, plants, molds, and bacteria. Whithin the protein shell of ferritin, iron is first oxidized to the ferric state for storage as ferric oxyhdroxide. Thus, ferritin removes excess iron from the cell sap where it could otherwise participate in peroxidation mechanisms.
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TMPJ-00015 | GABARAP Protein, Human, Recombinant (His & hFc) | Human | E. coli | ||
Gamma-Aminobutyric Acid Receptor-Associated Protein (GABARAP) is a ligand-gated chloride channel protein that mediates inhibitory neurotransmission and belongs to the MAP1 LC3 family. GABARAP is highly positively charged in its N-terminus and shares sequence similarity with light chain-3 of microtubule-associated proteins 1A and 1B. GABARAP clusters neurotransmitter receptors by mediating interaction with the cytoskeleton. Autophagy is the process by which cells recycle cytoplasm and dispose of excess or defective organelles. This process is suggested to be involved development, differentiation, growth regulation and tissue remodeling in multicellular organisms. An important inhibitory neurotransmitter, GABA, acts on GABA receptors that are ubiquitously expressed in the CNS. GABARAP has been shown to play a important role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton.
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TMPY-03505 | COMMD9 Protein, Human, Recombinant (His) | Human | E. coli | ||
COMMD9 is a COMM domain-containing or COMMD protein. COMMD family is comprised of ten members which are widely conserved throughout evolution and share certain functional properties. They represent a recently discovered set of evolutionarily conserved factors characterized by the presence of a defining carboxy-terminal motif. COMMD protein functions in the control of the transcription factor NFkappaB. NFkappaB plays a critical role in a number of homeostatic processes in multicellular organisms, including the regulation of immunity and cell survival. COMMD proteins inhibit NFkappaB mediated gene expression, and recent mechanistic studies have revealed that COMMD1 controls the ubiquitination of NFkappaB subunits, an event linked to transcriptional termination. COMMD1 binds to a multimeric ubiquitin ligase containing Elongins B/C, Cul2 and SOCS1 (ECS( SOCS1)). In this complex, COMMD1 facilitates the binding of NFkappaB subunits to the ligase, thereby promoting their ubiquitination and degradation. Additional insights gained from these studies indicate that COMMD proteins likely play a broader role in cellular homeostasis through their participation in the ubiquitination pathway.
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TMPY-05119 | IL-17RA Protein, Human, Recombinant (His & hFc), Biotinylated | Human | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-02996 | IL-17RA Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-04400 | TLK2 Protein, Human, Recombinant (aa 397-772, His & GST) | Human | Baculovirus-Insect Cells | ||
Serine / threonine-protein kinase tousled-like 2, also known as PKU-alpha, Tousled-like kinase 2 and TLK2, is a nucleus protein which belongs to the protein kinase superfamily and Ser/Thr protein kinase family. The tousled-like kinases are an evolutionarily conserved family of proteins implicated in DNA repair, DNA replication and mitosis in metazoans and plants. Their absence from the yeasts and other eukaryotic 'microbes' suggests a specific role for them in the development of multicellular organisms. Tousled-like kinase 2 / TLK2 is widely expressed. It is present in fetal placenta, liver, kidney, pancreas, heart and skeletal muscle. It is also found in adult cell lines. Tousled-like kinase 2 / TLK2 contains one protein kinase domain. Tousled-like kinase 2 / TLK2 is rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly.
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TMPY-03557 | IL-17RA Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-02908 | BPI Protein, Human, Recombinant (His) | Human | HEK293 | ||
Bactericidal/permeability-increasing protein is a member of the BPI/LBP/Plunc superfamily and BPI/LBP family. It is a cationic protein which can be detected in the azurophilic granule and on the surface of polymorphonuclear leukocytes. Bactericidal/permeability-increasing protein also is a lipopolysaccharide binding protein. It is associated with human neutrophil granules and has bactericidal activity on gram-negative organisms. Bactericidal/permeability-increasing protein contains two domains that adopt the same structural fold, even though they have little sequence similarity. It binds to and neutralises lipopolysaccharides from the outer membrane of Gram-negative bacteria. The cytotoxic action of bactericidal/permeability-increasing protein is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.
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TMPY-00140 | ABP1/AOC1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Amine oxidase copper-containing 1 (AOC1; formerly known as amiloride-binding protein 1) is a secreted glycoprotein that catalyzes the degradation of putrescine and histamine. Polyamines and their diamine precursor putrescine are ubiquitous to all organisms and fulfill pivotal functions in cell growth and proliferation. That the Wilms tumor protein, WT1, which is necessary for normal kidney development, activates transcription of the AOC1 gene. Expression of a firefly luciferase reporter under control of the proximal AOC1 promoter was significantly enhanced by co-transfection of a WT1 expression construct. Binding of WT1 protein to a cis-regulatory element in the AOC1 promoter was confirmed by electrophoretic mobility shift assay and chromatin immunoprecipitation. WT1-dependent control of polyamine breakdown, which is mediated by changes in AOC1 expression, has a role in kidney organogenesis.
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TMPJ-00016 | GABARAP Protein, Human, Recombinant (GST) | Human | E. coli | ||
Gamma-Aminobutyric Acid Receptor-Associated Protein (GABARAP) is a ligand-gated chloride channel protein that mediates inhibitory neurotransmission and belongs to the MAP1 LC3 family. GABARAP is highly positively charged in its N-terminus and shares sequence similarity with light chain-3 of microtubule-associated proteins 1A and 1B. GABARAP clusters neurotransmitter receptors by mediating interaction with the cytoskeleton. Autophagy is the process by which cells recycle cytoplasm and dispose of excess or defective organelles. This process is suggested to be involved development, differentiation, growth regulation and tissue remodeling in multicellular organisms. An important inhibitory neurotransmitter, GABA, acts on GABA receptors that are ubiquitously expressed in the CNS. GABARAP has been shown to play a important role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton.
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TMPY-03344 | LSM3 Protein, Human, Recombinant (His) | Human | E. coli | ||
LSM3 (LSM3 Homolog, U6 Small Nuclear RNA And MRNA Degradation Associated) is a Protein Coding gene. LSM3 is a member of the snRNP Sm proteins family. It plays role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as a component of the pre-catalytic spliceosome (spliceosome B complex). Sm-like proteins can be detected in a variety of organisms. They all have the Sm sequence motif, which consists of 2 regions separated by a linker of variable length that folds as a loop. The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing. Diseases associated with LSM3 include Spondylolysis.
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TMPY-01368 | Cystatin F/CST7 Protein, Human, Recombinant (His) | Human | HEK293 | ||
The cystatin superfamily members are important natural cysteine protease inhibitors present in a wide variety of organisms and are divided into three classes. Cystatin F, also known as leukocystatin and CMAP (Cystatin-like Metastasis-Associated Protein), is a type 2 cystatin and its expression is limited to hematopoietic cells, with the highest expression levels being observed in monocytes, dendritic cells, and certain types of T-cells. Furthermore, cystatin F mRNA becomes up-regulated during dendritic cell maturation, and thus suggests a specific role of cystatin F in immune regulation. Cystatin F is produced as a dimer, an inactive cathepsin inhibitor which is activated by chemical reduction. In addition, Cystatin F and its homologues have been observed expressing in various human cancer cell lines established from malignant tumors, and thus indicates a new diagnosis and prevention approach of certain human carcinomas metastasis.
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TMPY-00770 | Cystatin F/CST7 Protein, Human, Recombinant | Human | HEK293 | ||
The cystatin superfamily members are important natural cysteine protease inhibitors present in a wide variety of organisms and are divided into three classes. Cystatin F, also known as leukocystatin and CMAP (Cystatin-like Metastasis-Associated Protein), is a type 2 cystatin and its expression is limited to hematopoietic cells, with the highest expression levels being observed in monocytes, dendritic cells, and certain types of T-cells. Furthermore, cystatin F mRNA becomes up-regulated during dendritic cell maturation, and thus suggests a specific role of cystatin F in immune regulation. Cystatin F is produced as a dimer, an inactive cathepsin inhibitor which is activated by chemical reduction. In addition, Cystatin F and its homologues have been observed expressing in various human cancer cell lines established from malignant tumors, and thus indicates a new diagnosis and prevention approach of certain human carcinomas metastasis.
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TMPY-02727 | METAP2 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
METAP2 (Methionine aminopeptidase 2), also known as MAP2 is a protein that belongs to the peptidase M24A family. MAP2 binds 2 cobalt or manganese ions and contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. It is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. The catalytic activity of human MAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. This protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amino-terminal methionine residue from nascent protein. MAP2 protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. It also plays a critical role in the regulation of protein synthesis.
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TMPJ-00728 | Beta-galactosidase Protein, E. coli, Recombinant | E.coli | E. coli | ||
β-galactosidase is an exoglycosidase which hydrolyzes the β-glycosidic bond formed between a galactose and its organic moiety. It may also cleave fucosides and arabinosides but with much lower efficiency. β-galactosides include carbohydrates containing galactose where the glycosidic bond lies above the galactose molecule. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. It is an essential enzyme in the human body. Deficiencies in the protein can result in galactosialidosis or Morquio B syndrome. In E. coli, the gene of β-galactosidase, the lacZ gene, is present as part of the inducible system lac operon which is activated in the presence of lactose when glucose level is low. β-galactosidase is important for organisms as it is a key provider in the production of energy and a source of carbons through the break down of lactose to galactose and glucose.
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TMPY-00769 | Cystatin F/CST7 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
The cystatin superfamily members are important natural cysteine protease inhibitors present in a wide variety of organisms and are divided into three classes. Cystatin F, also known as leukocystatin and CMAP (Cystatin-like Metastasis-Associated Protein), is a type 2 cystatin and its expression is limited to hematopoietic cells, with the highest expression levels being observed in monocytes, dendritic cells, and certain types of T-cells. Furthermore, cystatin F mRNA becomes up-regulated during dendritic cell maturation, and thus suggests a specific role of cystatin F in immune regulation. Cystatin F is produced as a dimer, an inactive cathepsin inhibitor which is activated by chemical reduction. In addition, Cystatin F and its homologues have been observed expressing in various human cancer cell lines established from malignant tumors, and thus indicates a new diagnosis and prevention approach of certain human carcinomas metastasis.
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TMPY-02856 | Cystatin F/CST7 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
The cystatin superfamily members are important natural cysteine protease inhibitors present in a wide variety of organisms and are divided into three classes. Cystatin F, also known as leukocystatin and CMAP (Cystatin-like Metastasis-Associated Protein), is a type 2 cystatin and its expression is limited to hematopoietic cells, with the highest expression levels being observed in monocytes, dendritic cells, and certain types of T-cells. Furthermore, cystatin F mRNA becomes up-regulated during dendritic cell maturation, and thus suggests a specific role of cystatin F in immune regulation. Cystatin F is produced as a dimer, an inactive cathepsin inhibitor which is activated by chemical reduction. In addition, Cystatin F and its homologues have been observed expressing in various human cancer cell lines established from malignant tumors, and thus indicates a new diagnosis and prevention approach of certain human carcinomas metastasis.
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TMPY-03509 | TCTP/TPT1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Tumor protein, also known as TPT1, is a highly conserved protein among many eukaryotic organisms. Tumor protein is involved in a variety of cellular activities, including microtubule stabilization, calcium-binding activities, and apoptosis. The Mammalian translationally controlled tumour protein (TPT1) (or P23) is a protein that has been found to be preferentially synthesised in cells during the early growth phase of some types of tumour, but which is also expressed in normal cells. It was first identified as a histamine-releasing factor, acting in IgE +-dependent allergic reactions. In addition, TPT1 has been shown to bind to tubulin in the cytoskeleton, has a high affinity for calcium, is the binding target for the antimalarial compound artemisinin, and is induced in vitamin D-dependent apoptosis. TPT1 production is thought to be controlled at the translational as well as the transcriptional level.
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TMPY-00018 | METAP2 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
METAP2 (Methionine aminopeptidase 2), also known as MAP2 is a protein that belongs to the peptidase M24A family. MAP2 binds 2 cobalt or manganese ions and contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. It is found in all organisms and is especially important because of its critical role in tissue repair and protein degradation. The catalytic activity of human MAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. This protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amino-terminal methionine residue from nascent protein. MAP2 protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. It also plays a critical role in the regulation of protein synthesis.
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TMPY-02177 | Cyclophilin A Protein, Human, Recombinant (His) | Human | E. coli | ||
Peptidyl-prolyl cis-trans isomerase A, also known as PPIase A, Rotamase A, Cyclophilin A, Cyclosporin A-binding protein, PPIA and CYPA, is a cytoplasm protein that belongs to the cyclophilin-type PPIase family and PPIase A subfamily. Cyclophilins (CyPs) are a family of proteins found in organisms ranging from prokaryotes to humans. These molecules exhibit peptidyl-prolyl isomerase activity, suggesting that they influence the conformation of proteins in cells. PPIA / Cyclophilin A accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIA / Cyclophilin A is secreted by vascular smooth muscle cells in response to inflammatory stimuli, and could thus contribute to atherosclerosis. It is not essential for mammalian cell viability. PPIA / Cyclophilin A can interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions.
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TMPY-01593 | Cyclophilin A Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Peptidyl-prolyl cis-trans isomerase A, also known as PPIase A, Rotamase A, Cyclophilin A, Cyclosporin A-binding protein, PPIA and CYPA, is a cytoplasm protein that belongs to the cyclophilin-type PPIase family and PPIase A subfamily. Cyclophilins (CyPs) are a family of proteins found in organisms ranging from prokaryotes to humans. These molecules exhibit peptidyl-prolyl isomerase activity, suggesting that they influence the conformation of proteins in cells. PPIA / Cyclophilin A accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIA / Cyclophilin A is secreted by vascular smooth muscle cells in response to inflammatory stimuli, and could thus contribute to atherosclerosis. It is not essential for mammalian cell viability. PPIA / Cyclophilin A can interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions.
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