目录号 | 产品详情 | 靶点 | |
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T83969 | Hydroxylase | ||
Casein 是一种具有多种作用的牛奶蛋白,参与新型药物递送系统,通过其胃内凝血特性以不同的方式影响餐后氨基酸递送。 | |||
T64376 | NADPH | ||
Casein kinase 1δ-IN-9是一种醌还原酶2(Quinone reductase 2)抑制剂,IC50为0.6μM。 | |||
T77500 | Casein Kinase | ||
Casein kinase 1δ-IN-6 是一种有效且具有选择性的蛋白激酶 CK-1δ 抑制剂,其 IC50 为 23 nM。Casein kinase 1δ-IN-6 在体外和体内实验中均显示出神经保护和抗炎活性。Casein kinase 1δ-IN-6 可用于研究神经退行性疾病。 | |||
T64350 | Casein Kinase | ||
Casein kinase 1δ-IN-3 (Casein kinase 1δ-IN-3) (Compound 23a) 是一种酪蛋白激酶 1δ (CK1d) 抑制剂,pIC50 为 6.5376。 | |||
T9175 | Apoptosis Casein Kinase | ||
Casein Kinase inhibitor A51 是一种具有口服活性的酪蛋白激酶 1α (CK1α) 抑制剂,具有抗癌活性,可诱导白血病细胞凋亡 (apoptosis),可用于研究颈部癌、急性髓系白血病、乳腺癌和前列腺癌。 | |||
T10687 | Casein Kinase | ||
Casein Kinase II Inhibitor IV 是一种小分子诱导剂,可诱导表皮角质形成细胞分化。 | |||
T77648 | Others | ||
Casein kinase 1δ-IN-14(WAY-637081) 可用于研究动脉粥样硬化相关心血管疾病。 | |||
T60295 | Casein Kinase | ||
Casein kinase 1δ-IN-1 (WAY-643895) 是一种酪蛋白激酶 1δ (CK1δ) 的抑制剂,对CK1δ有抑制作用。Casein kinase 1δ-IN-1 可用于如阿尔茨海默病类的神经退行性疾病的研究。 | |||
T39482 | |||
Casein Kinase inhibitor A86 is a highly effective and orally bioavailable inhibitor of casein kinase 1α (CK1α). Additionally, it displays inhibitory actions towards CDK7 (TFIIH) and CDK9 (P-TEFb). Furthermore, Casein Kinase inhibitor A86 demonstrates the ability to induce apoptosis in leukemia cells, portraying substantial anti-leukemic effects. | |||
T2449 | Apoptosis Casein Kinase ALK Autophagy | ||
D4476 (Casein Kinase I Inhibitor) 是一种选择性和细胞渗透性的CK1抑制剂,在体外实验的IC50值为0.3 μM。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-04750 | CSNK2A2 Protein, Human, Recombinant | Human | Baculovirus-Insect Cells | ||
Casein kinase II subunit alpha', also known as CSNK2A2 and CK2A2, is a member of the protein kinase superfamily, Ser/Thr protein kinase family and CK2 subfamily. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha and alpha' chains contain the catalytic site. CSNK2A2 is a tetramer composed of an alpha chain, an alpha' and two beta chains. It is also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation. Protein kinase casein kinase II (Ck2) is a cyclic-AMP and calcium-independent serine-threonine kinase that is composed of two catalytic subunits (alpha and alpha') and two regulatory beta-subunits. Ck2 is not a casein kinase in vivo, but over 1 substrates are known. The highly conserved amino acid sequences of its subunits and their broad expression suggest that Ck2 may have a fundamental role in cell function. Ck2 has been implicated in DNA replication, regulation of basal and inducible transcription, translation and control of metabolism. The Ck2alpha and Ck2alpha' isoforms (products of the genes Csnk2a1 and Csnk2a2, respectively) are highly homologous, the reason for their redundancy and evolutionary conservation is unknown. CSNK2A2 may be a candidate gene for these inherited syndromes.
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TMPJ-00500 | Kappa-Casein Protein, Human, Recombinant (His) | Human | Human Cells | ||
Kappa-Casein (CSN3) is a secreted protein that belongs to the Kappa-Casein family. CSN3 exists in heteromultimers that are composed of alpha-s 1casein and kappa casein linked by disulfide bonds. CSN3 is involved in a number of important physiological processes. In the gut, CSN3 protein is split into an insoluble peptide (para kappa-casein) and a soluble hydrophilic glycopeptide (caseinomacropeptide). Caseinomacropeptide is responsible for increased efficiency of digestion, prevention of neonate hypersensitivity to ingested proteins, and inhibition of gastric pathogens. Kappa-casein also stabilizes micelle formation, preventing casein precipitation in milk.
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TMPH-00227 | Beta-casein Protein, Bovine, Recombinant (His & Myc) | Bovine | E. coli | ||
Important role in determination of the surface properties of the casein micelles.; Casoparan acts as a macrophage activator, increasing the phagocytic activity of macrophages and peroxide release from macrophages. It also acts as a bradykinin-potentiating peptide.; Casohypotensin acts as a bradykinin-potentiating peptide. Induces hypotension in rats. Acts as a strong competitive inhibitor of endo-oligopeptidase A.; Antioxidant peptide has antioxidant activity.
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TMPY-04422 | Casein Kinase 1 gamma 2 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Casein kinase I gamma 2 isoform (CSNK1G2), a member of the large casein kinase I (CKI) subfamily, protein kinase superfamily. It may affect the development of brain, and associate with vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. The CKI family includes several other isoforms (alpha, beta, gamma, and delta). Dishevelled (Dsh), another positive component of the Wnt pathway, becomes phosphorylated in response to Wnt signals. All the CKI isoforms, with the exception of gamma, increase the phosphorylation of Dsh in vivo. Casein kinase 1 gamma (CK1gamma, or CSNK1G) is associated with the cell membrane and binds to LRP. CK1gamma was found to be needed for Wnt signaling through Wnt receptor LRP. CSNK1G2 inhibits Smad3-mediated TGF-beta responses including induction of target genes and cell growth arrest, and this inhibition is dependent on CSNK1G2 kinase activity. The overexpression of CSNK1G2 in human cancers, may act as an oncoprotein during tumorigenesis. In addition, as an MTA1s-binding protein, CSNK1G2 could further potentiate the estrogen receptor (ER) corepressive function of MTA1s.
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TMPY-04375 | Casein Kinase 1 alpha Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
Casein kinase I isoform alpha, also known as CKI-alpha, CK1 and CSNK1A1, is a cytoplasm protein which belongs to theprotein kinase superfamily, CK1 Ser/Thr protein kinase family and casein kinase I subfamily. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. High expression of CSNK2A1, or concomitantly high expression of CSNK2A1, are independent prognostic factors of poor survival in NSCLC patients. CSNK2A1 are useful prognosis markers in non-small cell lung cancer (NSCLC) patients after complete resection, independent of lymph node metastasis status. CSNK1A1 can phosphorylate a large number of proteins. It participates in Wnt signaling. It phosphorylates CTNNB1 at 'Ser-45'. CSNK1A1 may play a role in segregating chromosomes during mitosis.
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TMPY-04402 | CSNK1G1 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
Casein kinase I isoform gamma-1, also known as CSNK1G1, is a member of the protein kinase superfamily, CK1 Ser/Thr protein kinase family and casein kinase I subfamily. Thecasein kinase I family of protein kinases are serine / threonine-selective enzymes that function as regulators ofsignal transductionpathways in most eukaryotic cell types. Casein has been used as a substrate since the earliest days of research on protein phosphorylation. Casein kinase activity associated with the endoplasmic reticulum of mammary glands was first characterized in 1974 and its activity was shown to not depend on cyclic AMP. The CKI family of monomeric serine–threonine protein kinases is found in eukaryotic organisms from yeast to human. Mammals have seven family members: alpha, beta 1, gamma 1, gamma 2, gamma 3, delta, and epsilon. The family members have the highest homology in their kinase domains (53%–98% identical) and differ from most other protein kinases by the presence of the sequence S-I-N instead of A-P-E in kinase domain VIII. The CKI family members appear to have similar substrate specificity and substrate selection is thought to be regulated via subcellular localization and docking sites in specific substrates.
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TMPY-04758 | CK2 alpha/CSNK2A1 Protein, Mouse, Recombinant | Mouse | Baculovirus-Insect Cells | ||
Casein kinase II subunit alpha, also known as CK II alpha, CSNK2A1 and CK2A1, is a member of the protein kinase superfamily, Ser / Thr protein kinase family and CK2 subfamily. Casein kinase II (CSNK2A1) is a serine / threonine protein kinase that phosphorylates acidic proteins such as casein. This kinase is composed of an alpha, an alpha-prime, and two beta subunits. The alpha subunits contain the catalytic activity while the beta subunits undergo autophosphorylation. Casein kinase II (CSNK2A1) is a constitutively active, ubiquitously expressed serine / threonine protein kinase that is thought to have a regulatory function in cell proliferation, cell differentiation and apoptosis. CSNK2A1 functions as a tetrameric complex consisting of two regulatory beta-subunits and two catalytic units (alpha and alpha') in a homomeric or heteromeric conformation. Whilst the alpha- and alpha'-subunits are catalytically identical, proteins that regulate CSNK2A1, such as cdc2 and Hsp90, preferentially bind to the alpha and not the alpha'-subunit. CSNK2A1 can phosphorylate a number of key intracellular signaling proteins implicated in tumor suppression (p53 and PTEN) and tumorigenesis (myc, jun, NF-kappaB). CSNK2A1 is also thought to influence Wnt signaling via beta-catenin phosphorylation and the PI 3-K signaling pathway via the phosphorylation of Akt.
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TMPY-04441 | CK2 alpha/CSNK2A1 Protein, Mouse, Recombinant (His & GST) | Mouse | Baculovirus-Insect Cells | ||
Casein kinase II subunit alpha, also known as CK II alpha, CSNK2A1 and CK2A1, is a member of the protein kinase superfamily, Ser / Thr protein kinase family and CK2 subfamily. Casein kinase II (CSNK2A1) is a serine / threonine protein kinase that phosphorylates acidic proteins such as casein. This kinase is composed of an alpha, an alpha-prime, and two beta subunits. The alpha subunits contain the catalytic activity while the beta subunits undergo autophosphorylation. Casein kinase II (CSNK2A1) is a constitutively active, ubiquitously expressed serine / threonine protein kinase that is thought to have a regulatory function in cell proliferation, cell differentiation and apoptosis. CSNK2A1 functions as a tetrameric complex consisting of two regulatory beta-subunits and two catalytic units (alpha and alpha') in a homomeric or heteromeric conformation. Whilst the alpha- and alpha'-subunits are catalytically identical, proteins that regulate CSNK2A1, such as cdc2 and Hsp90, preferentially bind to the alpha and not the alpha'-subunit. CSNK2A1 can phosphorylate a number of key intracellular signaling proteins implicated in tumor suppression (p53 and PTEN) and tumorigenesis (myc, jun, NF-kappaB). CSNK2A1 is also thought to influence Wnt signaling via beta-catenin phosphorylation and the PI 3-K signaling pathway via the phosphorylation of Akt.
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TMPY-04372 | CK2 alpha/CSNK2A1 Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
Casein kinase II subunit alpha, also known as CK II alpha, CSNK2A1 and CK2A1, is a member of the protein kinase superfamily, Ser / Thr protein kinase family and CK2 subfamily. Casein kinase II (CSNK2A1) is a serine / threonine protein kinase that phosphorylates acidic proteins such as casein. This kinase is composed of an alpha, an alpha-prime, and two beta subunits. The alpha subunits contain the catalytic activity while the beta subunits undergo autophosphorylation. Casein kinase II (CSNK2A1) is a constitutively active, ubiquitously expressed serine / threonine protein kinase that is thought to have a regulatory function in cell proliferation, cell differentiation and apoptosis. CSNK2A1 functions as a tetrameric complex consisting of two regulatory beta-subunits and two catalytic units (alpha and alpha') in a homomeric or heteromeric conformation. Whilst the alpha- and alpha'-subunits are catalytically identical, proteins that regulate CSNK2A1, such as cdc2 and Hsp90, preferentially bind to the alpha and not the alpha'-subunit. CSNK2A1 can phosphorylate a number of key intracellular signaling proteins implicated in tumor suppression (p53 and PTEN) and tumorigenesis (myc, jun, NF-kappaB). CSNK2A1 is also thought to influence Wnt signaling via beta-catenin phosphorylation and the PI 3-K signaling pathway via the phosphorylation of Akt.
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TMPY-04393 | CSNK2A2 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
Casein kinase II subunit alpha', also known as CSNK2A2 and CK2A2, is a member of the protein kinase superfamily, Ser/Thr protein kinase family and CK2 subfamily. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha and alpha' chains contain the catalytic site. CSNK2A2 is a tetramer composed of an alpha chain, an alpha' and two beta chains. It is also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation. Protein kinase casein kinase II (Ck2) is a cyclic-AMP and calcium-independent serine-threonine kinase that is composed of two catalytic subunits (alpha and alpha') and two regulatory beta-subunits. Ck2 is not a casein kinase in vivo, but over 1 substrates are known. The highly conserved amino acid sequences of its subunits and their broad expression suggest that Ck2 may have a fundamental role in cell function. Ck2 has been implicated in DNA replication, regulation of basal and inducible transcription, translation and control of metabolism. The Ck2alpha and Ck2alpha' isoforms (products of the genes Csnk2a1 and Csnk2a2, respectively) are highly homologous, the reason for their redundancy and evolutionary conservation is unknown. CSNK2A2 may be a candidate gene for these inherited syndromes.
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TMPH-01054 | CSNK1E Protein, Human, Recombinant (His) | Human | E. coli | ||
Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates DVL1 and DVL2. Central component of the circadian clock. In balance with PP1, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. Inhibits cytokine-induced granuloytic differentiation.
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TMPJ-01387 | PACSIN2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Protein Kinase C and Casein Kinase Substrate in Neurons Protein 2 (PACSIN2) is a member of the PACSIN family. PACSIN2 is localized to the plasma membrane via its coiled-coil domain. PACSIN2 is widely expressed and contains one FCH domain and one SH3 domain. PACSIN2 forms homo- and hetero-aggregates with other PACSINs. PACSIN2 may play a role in vesicle formation and transport. In addition, PACSIN2 is involved in linking the actin cytoskeleton with vesicle formation by regulating tubulin polymerization.
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TMPJ-01307 | PACSIN1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Protein Kinase C and Casein Kinase Substrate in Neurons Protein 1 (PACSIN1) belongs to the PACSIN family. PACSIN1 contains one FCH domain and one SH3 domain. PACSIN1 is highly expressed in the brain and at lower leves in the heart, pancreas, and liver. PACSIN1 may play a role in vesicle formation and transport. PACSIN1 has been shown to interact with DNM1, PACSIN3, Huntingtin, and PACSIN2. In addition, PACSIN1 is phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC).
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TMPH-00223 | Alpha-S2-casein Protein, Bovine, Recombinant (His & KSI) | Bovine | E. coli | ||
Important role in the capacity of milk to transport calcium phosphate.; Casocidin-I inhibits the growth of E.coli and S.carnosus.
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TMPY-02078 | HtrA2/Omi Protein, Human, Recombinant (His) | Human | E. coli | ||
Serine protease HTRA2, also known as high-temperature requirement protein A2, Omi stress-regulated endoprotease, Serine protease 25, Serine proteinase OMI and HTRA2, is a single-pass membrane protein that belongs to the peptidase S1B family. HTRA2 contains one PDZ (DHR) domain. HTRA2 is a serine protease that shows proteolytic activity against a non-specific substrate beta-casein. It promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity or by a BIRC inhibition-independent, caspase-independent, and serine protease activity-dependent mechanism. HTRA2 cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 of HTRA2 seems to be proteolytically inactive. Defects in HTRA2 are the cause of Parkinson disease type 13 (PARK13) which is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity, and postural instability, as well as by a clinically significant response to treatment with levodopa.
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TMPH-02402 | Zinc metalloproteinase Protein, Legionella pneumophila, Recombinant (His) | Legionella pneumophila | E. coli | ||
Cleaves collagen, gelatin, casein, alpha-1-antitrypsin, and bovine insulin. May play a role in the pathogenesis of legionnaires disease.
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TMPH-01644 | MMP-7 Protein, Human, Recombinant (GST) | Human | E. coli | ||
Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.
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TMPH-03583 | Extracellular elastase Protein, S. epidermidis, Recombinant (His & Myc) | Staphylococcus epidermidis | E. coli | ||
Protease that has a low substrate specificity. Glucagon is preferentially cleaved between aromatic (Phe) and hydrophobic (Val) amino acids. Hydrolyzes casein and elastin.
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TMPH-03156 | Lys-gingipain Protein, Porphyromonas gingivalis, Recombinant (His & SUMO) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
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TMPH-02414 | Lys-gingipain W83 Protein, Porphyromonas gingivalis, Recombinant (His) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria. Has hemolytic activity; this is mediated by the adhesin domains and does not require the catalytic domain.
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TMPH-02342 | Collagenase Protein, Hypoderma lineatum, Recombinant (His & Myc) | Hypoderma lineatum | E. coli | ||
This enzyme is a serine protease capable of degrading the native triple helix of collagen. Also cleaves the B chain of insulin at the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl phosphate, 2-naphthyl butyrate, 2-naphthyl caprylate, 2-naphthyl myristate, L-leucine 2-2-naphthylamide, L-valine 2-naphthylamide, L-cysteine 2-naphthylamide or L-glutarylphenylalanine 2-naphthylamide.
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TMPH-02899 | VRK1 Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Serine/threonine kinase involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation. Acts by mediating phosphorylation of downstream target protein. Phosphorylates 'Thr-18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2. Phosphorylates casein and histone H3. Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its binding to LEM domain-containing proteins and causes its relocalization from the nucleus to the cytoplasm. Phosphorylates ATF2 which activates its transcriptional activity.
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TMPH-03155 | Lys-gingipain HG66 Protein, Porphyromonas gingivalis, Recombinant (His & Myc) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
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TMPH-03154 | Lys-gingipain 381 Protein, Porphyromonas gingivalis, Recombinant (His) | Porphyromonas gingivalis | E. coli | ||
Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
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TMPJ-01068 | FKBP25/FKBP3 Protein, Human, Recombinant (His) | Human | E. coli | ||
FKBP25 contains 1 PPIase FKBP-type domain, belongs to the FKBP-type PPIase family. FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. FKBP3 is a cis-trans prolyl isomerase enzyme that binds the immunosuppressants FK506 and rapamycin, as well as histone deacetylases, the transcription factor YY1, casein kinase II, and nucleolin. It has a higher affinity for rapamycin than for FK506 and thus may be an important target molecule for immunosuppression by rapamycin.
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TMPH-02174 | PYCR1 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
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TMPH-00217 | SVMP Protein, Bothrops leucurus, Recombinant (His & Myc) | Bothrops leucurus | E. coli | ||
Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen, as well as fibrin, fibronectin and casein. Beta and gamma chains are also hydrolyzed, but more slowly. Thrombolytic activity is also observed. Induces detachment of endothelial cells followed by death, and inhibits endothelial cell adhesion to fibronectin. Induces edema in mouse paw. Inhibits ADP-induced platelet aggregation on human platelet-rich plasma with an IC(50) of 2.8 uM.
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TMPY-03889 | STC2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
STC2 is a secreted, homodimeric glycoprotein expressed in a wide variety of tissues. STC2 has an anti-hypocalcemic action on calcium and phosphate homeostasis. It may have autocrine or paracrine functions. Its C-terminus contains a cluster of histidine residues that may interact with metal ions. STC2 has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. It may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis.
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TMPY-03279 | STC2 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
STC2 is a secreted, homodimeric glycoprotein expressed in a wide variety of tissues. STC2 has an anti-hypocalcemic action on calcium and phosphate homeostasis. It may have autocrine or paracrine functions. Its C-terminus contains a cluster of histidine residues that may interact with metal ions. STC2 has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. It may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis.
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TMPJ-01261 | PPP1R14A Protein, Human, Recombinant (His) | Human | E. coli | ||
Protein Phosphatase 1 Regulatory Subunit 14A (PPP1R14A) belongs to the PP1 inhibitor family. PPP1R14A is mapped to chromosome 19q13.13-q13.2. PPP1R14A binds directly to protein kinase C and casein kinase I. Meantime, PPP1R14A is a phosphorylation-dependent inhibitor of smooth muscle myosin phosphatase. PPP1R14A is the inhibitor of PPP1CA. When phosphorylated, PPP1R14A has over 1000-fold higher inhibitory activity, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction. In addition, inhibition of PPP1R14A also enhances contraction of smooth muscle in the absence of increment of intracellular Ca2+ concentration.
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TMPH-02647 | FAM20C Protein, Mouse, Recombinant (His & Myc) | Mouse | Baculovirus | ||
Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs and plays a key role in biomineralization of bones and teeth. Constitutes the main protein kinase for extracellular proteins, generating the majority of the extracellular phosphoproteome. Mainly phosphorylates proteins within the Ser-x-Glu/pSer motif, but also displays a broader substrate specificity. Phosphorylates casein as well as a number of proteins involved in biomineralization such as AMELX, AMTN, ENAM and SPP1. In addition to its role in biomineralization, also plays a role in lipid homeostasis, wound healing and cell migration and adhesion.
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TMPY-04100 | MMP-26 Protein, Human, Recombinant | Human | E. coli | ||
MMP26 (Matrix Metallopeptidase 26) is a Protein Coding gene. MMP26 is a member of matrix metalloproteinases (MMPs) and has been reported to be highly expressed in many cancers. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain. It may hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin, and alpha-1 proteinase inhibitor, and is also able to activate progelatinase B. MMP26 is a target gene of miR-125b, and the expression profile of MMP26 showed an inverse relationship with miR-125b in vivo and in vitro. The overexpression of MMP26 in SW1353 cells increased cell invasiveness, while inhibition of MMP26 decreased cell invasiveness.
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TMPJ-01190 | SPESP1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Sperm Equatorial Segment Protein 1 (SPESP1) is a member of the SPESP1 family. SPESP1 is highly expressed in the testis, where it is localized to the acrosome of postmeiotic stages of spermiogenesis; it is expressed at lower levels in the placenta and fetal lung. SPESP1 is involved in the multicellular organisimal development. Disruption of SPESP1 leads to abnormal distribution of sperm proteins resulting in a detached membrane from the equatorial segment and less fertile sperm. SPESP1 may interact with IZUMO1 and MN9 antigen and it contains an N-glycosylation site as well as several cAMP-dependent kinase, protein kinase C, and casein kinase II consensus phosphorylation sites.
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TMPJ-00991 | S100A8 Protein, Rat, Recombinant (His) | Rat | E. coli | ||
Protein S100-A8(Mrp8) contains 2 EF-hand domains and belongs to the S-100 family. Mrp8 binds two calcium ions per molecule with an affinity similar to that of the S-100 proteins. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. It may function in the inhibition of casein kinase and as a cytokine. Altered expression of this protein is associated with the disease cystic fibrosis.
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TMPH-00708 | DegP Protein, E. coli, Recombinant (His) | E. coli | Yeast | ||
DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated temperatures. It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP).
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TMPY-04137 | ATP6V1F Protein, Human, Recombinant (GST) | Human | E. coli | ||
ATP6V1F encodes a component of vacuolar ATPase mediating acidification. The cDNA and the genomic sequences of ATP6V1F were cloned successfully for the first time from the Giant Panda (Ailuropoda melanoleuca) using reverse transcription polymerase chain reaction and touchdown-polymerase chain reaction, respectively. Topology prediction showed that there is one protein kinase C phosphorylation site, two Casein kinase II phosphorylation sites, and one N-myristoylation site in the ATP6V1F protein. Up-regulated expression of mammary tumor 8 kDa protein (MAT-8), complement component C1S (C1S), ferritin heavy chain (FTH1), peptidyl-prolyl cis-trans isomerase A (PPIA), RNA-binding protein regulatory subunit DJ-1 protein (DJ-1) and vacuolar ATP synthase subunit F (ATP6V1F) was determined in prostate carcinoma and confirmed by using quantitative real-time RT-PCR analyses.
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TMPY-01948 | COQ7 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Ubiquinone biosynthesis protein COQ7 homolog, also known as Coenzyme Q biosynthesis protein 7 homolog, Timing protein clk-1 homolog and COQ7, is a mitochondrion inner membrane and peripheral membrane protein which belongs to theCOQ7 family. It is expressed dominantly in heart and skeletal muscle. COQ7 is synthesized as a preprotein that is imported into the mitochondrial matrix, where the sequence is cleaved off and the mature protein becomes loosely associated with the inner membrane. This enzyme is responsible for the hydroxylation of 5-demethoxyubiquinone to 5-hydroxyubiquinone. Human COQ7 protein is mostly helical, and contains an alpha-helical membrane insertion. It has a potential N-glycosylation site, a phosphorylation site for protein kinase C and another for casein kinase II, and three N-myristoylation sites. COQ7 is involved in lifespan determination in ubiquinone-independent manner. It is also involved in ubiquinone biosynthesis. COQ7 is potential central metabolic regulator.
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TMPY-02759 | Kallikrein 6/KLK6 Protein, Human, Recombinant (His) | Human | HEK293 | ||
KLK6 (kallikrein-related peptidase 6), also known as Klk7, belongs to the peptidase S1 family, Kallikrein subfamily. Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. KLK6 is a serine protease that exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Klk7 shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein, and extracellular matrix proteins such as fibronectin, laminin, vitronectin, and collagen. KLK6 degrades alpha-synuclein and prevents its polymerization, indicating that KLK6 may be involved in the pathogenesis of Parkinson's disease and other synucleinopathies. Klk7 may be involved in the regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralizing KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis.
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TMPY-03438 | Calsequestrin 1 Protein, Human, Recombinant | Human | E. coli | ||
Calsequestrin-1 is an isoform of calsequestrin. Calsequestrin is a calcium-binding protein of the sarcoplasmic reticulum. It helps hold calcium in the cisterna of the sarcoplasmic reticulum after a muscle contraction, even though the concentration of calcium in the sarcoplasmic reticulum is much higher than in the cytosol. Two forms of calsequestrin have been identified: Calsequestrin-2 and Calsequestrin-1. Calsequestrin-1 is found in fast skeletal muscle. The release of calsequestrin-bound calcium (through a calcium release channel) triggers muscle contraction. The active protein is not highly structured, more than 5% of it adopting a random coil conformation. When calcium binds there is a structural change whereby the alpha-helical content of the protein increases from 3 to 11%. Both forms of calsequestrin are phosphorylated by casein kinase 2, but the cardiac form is phosphorylated more rapidly and to a higher degree. Calsequestrin-1 is also secreted in the gut where it deprives bacteria of calcium ions.
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TMPY-01992 | Kallikrein 8/KLK8 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Kallikrein-8, also known as Neuropsin, Serine protease 19, Serine protease TADG-14, Tumor-associated differentially expressed gene 14 protein, and KLK8 is a secreted protein that belongs to the peptidase S1 family and Kallikrein subfamily. It is a serine protease that is capable of degrading some proteins such as casein, fibrinogen, kininogen, fibronectin, and collagen type IV. Kallikrein-8 / KLK8 plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway. It regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. It is involved in skin desquamation and keratinocyte proliferation and plays a role in the secondary phase of pathogenesis following spinal cord injury. It also cleaves L1CAM in response to increased neural activity. It induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Kallikrein-8 / KLK8 is expressed at high levels in serum, ascites fluid, and tumor cytosol of advanced-stage ovarian cancer patients and may serve as a marker of ovarian cancer. Kallikrein-8 / KLK8 may have potential clinical value for disease diagnosis or prognosis and it may also be a useful therapeutic target.
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