目录号 | 产品详情 | 靶点 | |
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T76800 | |||
Dalotuzumab (MK-0646) 是一种靶向IGF-1R 的重组人源化单克隆抗体 (IgG1 型)。Dalotuzumab 通过抑制IGF-1和IGF-2介导的肿瘤细胞增殖、IGF-1R 自体磷酸化和Akt 磷酸化而发挥作用。Dalotuzumab 还可诱导细胞凋亡和周期停滞。Dalotuzumab 与其他抗癌活性分子(如他汀类活性分子)共同使用,可增强 Dalotuzumab 的体外和体内抗肿瘤活性。 | |||
T82758 | CDK | ||
CDK9-Cyclin T1 PPI-IN-1 (Compound B19) 是CDK9-Cyclin T1蛋白-蛋白相互作用的选择性抑制剂。该化合物能够有效抑制TNBC MDA-MB-231细胞系的细胞增殖(IC50: 0.044 μM),诱导细胞凋亡,同时降低CDK9的转录活性并减少RNA Pol II CTD ser2的磷酸化,有效地抑制了4T1移植瘤模型小鼠中肿瘤的生长。 | |||
T81038 | |||
TAT-DEF-Elk-1 TFA (TDE TFA) 是一种Elk-1的细胞穿透性肽抑制剂,通过模仿Elk-1的DEF域并特异性地阻断其功能来抑制Elk-1。该化合物能够抑制Elk-1的磷酸化作用,阻止其核内转位,同时不影响ERK和MSK1的活化。TAT-DEF-Elk-1 TFA作为一种研究工具,对于探究神经元可塑性及Elk-1在该进程中的角色具有重要价值。 | |||
T78843 | c-Met/HGFR | ||
MET/PDGFRA-IN-1 (compound 8c) 作为MET和PDGFRA蛋白的抑制剂,以36 μM对MET的IC50值显示活性。该化合物能够抑制MET磷酸化并触发细胞凋亡(apoptosis)。此外,MET/PDGFRA-IN-1有效抑止了多种MET阳性细胞系的增殖,包括AsPc-1、EBC-1、MKN-45、Mia-Paca-2、HT-29和K562,其IC50s分别为15.3、19.0、22.0、25.6、21.0、31.5 μM。 | |||
T79285 | HSP | ||
TRAP1-IN-1(化合物35)是一种高效、具有高选择性的TRAP1抑制剂,其中TRAP1为Hsp90蛋白质家族中的一种线粒体同源体。该抑制剂对TRAP1的选择性优于Grp94超过250倍,能够破坏TRAP1四聚体的稳定性,并诱导下游蛋白质的降解。此外,TRAP1-IN-1能够抑制线粒体氧化磷酸化复合体(OXPHOS),破坏线粒体膜电位,并促进糖酵解过程。 | |||
TN5431 | Antioxidant AMPK Liver X Receptor Lipid Fatty Acid Synthase | ||
Icariside E4是一种从小叶榆中提取得到天然化合物, 通过AMPK 磷酸化和抑制HepG1细胞中MID1IP2的低脂化作用。Icariside E4具有抗伤害,抗氧化,抗阿尔茨海默氏症和抗炎作用,抑制了SREBP-1c,肝脏X 受体-α(LXR)和FASN 在HepG2细胞中从头脂肪生成的表达。Icariside E4是治疗脂肪肝疾病的有效候选药物,在HepG1细胞中具有低脂化潜力。 | |||
T79710 | HDAC | ||
PI3Kα/HDAC6-IN-1(化合物21j)是一种针对PI3Kα/HDAC6的双重抑制剂,其IC50值分别为2.9 nM和26 nM。该化合物还能抑制AKT(Ser473)的磷酸化,诱导α-微管蛋白的积累,并促进其乙酰化,但对乙酰化组蛋白H3和H4无显著影响。在L-363细胞系中,PI3Kα/HDAC6-IN-1显示了高效的抑制活性(IC50=0.17 μM),表现出良好的抗癌潜力。 | |||
T72237 | |||
JBJ-09-063 hydrochloride 是一种突变选择性变构EGFR 抑制剂,对EGFRL858R、EGFR L858R/T790M、EGFR L858R/T790M/C797S 和 EGFRLT/L747S 的IC50分别为 0.147 nM、0.063 nM、0.083 nM 和 0.396 nM。JBJ-09-063 hydrochloride 有效降低 EGFR、Akt 和 ERK1/2 磷酸化。JBJ-09-063 hydrochloride 对EGFR 酪氨酸激酶抑制剂 (TKI) 敏感和耐药模型均有效。JBJ-09-063 hydrochloride 可用于EGFR 突变型肺癌研究。 | |||
T79489 | JNK | ||
JNK-1-IN-2(Compound c6)是一种选择性JNK-1抑制剂,其IC50值为33.5 nM。同时,该化合物对JNK-2和JNK-3也具有抑制作用,其IC50值分别为112.9 nM和33.2 nM。通过抑制c-Jun蛋白的磷酸化,JNK-1-IN-2能够逆转肺部损伤,并且可以被应用于肺纤维化的相关研究。 | |||
T79296 | JNK | ||
JNK-IN-12(compound P2)是一种针对线粒体的JNK抑制剂,其IC50为66.3 nM,由线粒体特异性细胞穿透肽与特异性JNK抑制剂SP600125构成。该化合物特异性作用于线粒体JNK不影响核内JNK信号,能够抑制线粒体JNK磷酸化。JNK-IN-12在体内外模型中对帕金森病的改善显示出潜在效果。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-04380 | DYRK3 Protein, Human, Recombinant (His & GST) | Human | Baculovirus Insect Cells | ||
Dual specificity tyrosine-phosphorylation-regulated kinase 3, also known as Regulatory erythroid kinase, REDK and DYRK3, is a nucleus protein which belongs to theprotein kinase superfamily, CMGC Ser/Thr protein kinase family and MNB/DYRK subfamily. DYRKs are an emerging family of dual-specificity kinases that play key roles in cell proliferation, survival, and development. DYRK3 contains oneprotein kinase domain. Isoform 1 and isoform 2 of DYRK3 are highly expressed in testis and in hematopoietic tissue such as fetal liver, and bone marrow. Isoform 2 of DYRK3 is the predominant form in testis. Isoform 1 of DYRK3 is the predominant form in fetal liver and bone marrow. Isoform 1 and isoform 2 are present at low levels in heart, pancreas, lymph node, and thymus. DYRK3 is a negative regulator of EPO-dependent erythropoiesis. It may place an upper limit on red cell production during stress erythropoiesis. DYRK3 inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells. It may also act by regulating CREB/CRE signaling. DYRK3 proved to effectively inhibit NFAT (nuclear factor of activated T cells) transcriptional response pathways and to co-immunoprecipitate with NFATc3. DYRK3 attenuates (and possibly apportions) red cell production selectively during anemia.
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TMPY-01085 | VLDLR Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
The very low density lipoprotein receptor, known as VLDLR, is a single-pass type 1 integral membrance protein and a member of the LDL receptor family. This receptor family includes LDL receptor, LRP, megalin, VLDLR and ApoER2, and is characterized by a cluster of cysteine-rich class A repeats, epidermal growth factor (EGF)-like repeats, YWTD repeats and an O-linked sugar sdomain. VLDLR contains 3 EGF-like domains, 8 LDL-receptor class A domains, as well as 6 LDL-receptor class B repeats, and is abundant in heart, skeletal muscle, also ovary and kidney, but not in liver. VLDLR binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. VLDLR mediates the phosphorylation of mDab1 (mammalian disabled protein) via binding to Reelin, and induces the modulation of Tau phosphorylation. This pathway regulates the migration of neurons along with the radial glial fiber network during brain development. Defects of VLDLR may be the cause of VLDLR-associated cerebellar hypoplasia (VLDLRCH), a syndrome characterized by moderate-to-profound mental retardation, delayed ambulation, and predominantly truncal ataxia.
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TMPY-04548 | CDK4 Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
CDK4 is a member of the Ser/Thr protein kinase family. It is highly similar to the gene products of S. cerevisiae cdc28 and S. pombe cdc2. It is a catalytic subunit of the protein kinase complex that is important for cell cycle G1 phase progression. The activity of CDK4 is restricted to the G1-S phase, which is controlled by the regulatory subunits D-type cyclins and CDK inhibitor p16(INK4a). CDK4 was shown to be responsible for the phosphorylation of retinoblastoma gene product. CDK4 is the ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. CDK4 has been shown to be mutated in some types of cancer, whilst a chromosomal rearrangement can lead to Cdk6 overexpression in lymphoma, leukemia and melanoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPJ-00166 | SCF Protein, Mouse, Recombinant | Mouse | E. coli | ||
Mouse stem cell factor (SCF), is the ligand for the receptor-type protein-tyrosine kinase KIT. It plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. It also promotes phosphorylation of PIK3R1, which is the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5.
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TMPY-02603 | STAT6 Protein, Human, Recombinant (His) | Human | Baculovirus Insect Cells | ||
Signal transducer and activator of transcription 6 (STAT6) is a transcription factor that is activated by interleukin-4 (IL-4)-induced tyrosine phosphorylation and mediates most of the IL-4-induced gene expression. STAT6 plays a central role in exerting interleukin-4 (IL-4) mediated biological responses and is found to induce the expression of BCL2L1/BCL-XL, which is responsible for the anti-apoptotic activity of IL4. Transcriptional activation by STAT6 requires the interaction with coactivators like p300 and the CREB-binding protein (CBP). NF-κB and tyrosine-phosphorylated Stat6 can directly bind each other in vitro and in vivo, which suggests that the direct interaction between Stat6 and NF-κB may provide a basis for synergistic activation of transcription by IL-4 and activators of NF-κB.
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TMPY-05004 | FGF-4 Protein, Human, Recombinant | Human | E. coli | ||
FGF (fibroblast growth factor) signalling is known to be required for many aspects of mesoderm formation and patterning during Xenopus development and has been implicated in regulating genes required for the specification of both blood and skeletal muscle lineages. Fibroblast growth factor 4 (FGF4) signaling induces differentiation from embryonic stem cells (ESCs) via the phosphorylation of downstream molecules such as mitogen-activated protein kinase/extracellular signal-related kinase (MEK) and extracellular signal-related kinase 1/2 (ERK1/2). Fibroblast Growth Factor 4 (FGF-4) could not only increase the proliferation of bone marrow mesenchymal stem cells (BMSCs), but also induce BMSCs into hepatocyte-like cells in vitro. FGF4 transduced BMSCs contributed to liver regeneration might by the transplanted microenvironment. The FGF4-bFGF BMSCs thus can enhance the survival of the transplanted cells, diminish myocardial fibrosis, promote myocardial angiogenesis, and improve cardiac functions.
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TMPY-04572 | MKK4 Protein, Mouse, Recombinant (His & GST) | Mouse | Baculovirus Insect Cells | ||
Dual specificity mitogen-activated protein kinase kinase 4, also known as MAP kinase kinase 4, MAPKK4, JNK-activating kinase 1, MAPK/ERK kinase 4, SAPK/ERK kinase 1, c-Jun N-terminal kinase kinase 1, JNKK, and MAP2K4, is a protein that belongs to the protein kinase superfamily, STE Ser/Thr protein kinase family and MAP kinase kinase subfamily. MAP2K4 / JNKK1 is a protein kinase that is a direct activator of MAP kinases in response to various environmental stresses or mitogenic stimuli. MAP2K4 / JNKK1 has been shown to activate MAPK8 / JNK1, MAPK9 / JNK2, and MAPK14 / p38, but not MAPK1 / ERK2 or MAPK3 / ERK1. MAP2K4 / JNKK1 is phosphorylated, and thus activated by MAP3K1 / MEKK. The stress-activated protein kinase (SAPK) pathways represent phosphorylation cascades that convey pro-apoptotic signals. The mitogen-activated protein kinase kinase (MAPKK) homolog MAP2K4 ( MKK4, SEK, JNKK1 ) is a centrally-placed mediator of the SAPK pathways.
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TMPY-04544 | MEK2 Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
Dual specificity mitogen-activated protein kinase kinase 2, also known as MAP kinase kinase 2, MAPKK2, ERK activator kinase 2, MAPK / ERK kinase 2, MEK2 and MAP2K2, is a member of the protein kinase superfamily, STE Ser/Thr protein kinase family and MAP kinase kinase subfamily. MAP2K2 / MEK2 contains one protein kinase domain. MEK1 and MEK2 (also known as MAP2K1 and MAP2K2, respectively) are evolutionarily conserved, dual-specificity kinases that mediate Erk1 and Erk2 activation during adhesion and growth factor signaling. MAP2K1 / MEK1 is a crucial modulator of Mek and Erk signaling and have potential implications for the role of MEK1 and MEK2 in tumorigenesis. MAP2K2 / MEK2 catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. It also activates the ERK1 and ERK2 MAP kinases. Defects in MAP2K2 are a cause of Cardiofaciocutaneous Syndrome (CFC Syndrome) which is characterized by a distinctive facial appearance, heart defects, and mental retardation. Heart defects include pulmonic stenosis, atrial septal defects, and hypertrophic cardiomyopathy.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04396 | C-ABL/ABL1 Protein, Human, Recombinant (GST) | Human | Baculovirus Insect Cells | ||
c-Abl belongs to the class of tyrosine kinases and is the prototype of a subfamily which includes two members, c-Abl and Arg (Abl-related gene). Both proteins are localized at the cell membrane, actin cytoskeleton and cytosol, and c-Abl is present in the nucleus as well. c-Abl is a non-receptor tyrosine kinase that participates in multiple signaling pathways linking the cell surface, cytoskeleton, and the nucleus. Recent in vitro studies have also linked c-Abl to amyloid-beta-induced toxicity and tau phosphorylation. c-Abl has been implicated in many cellular processes including differentiation, division, adhesion, death, and stress response. c-Abl is a latent tyrosine kinase that becomes activated in response to numerous extra- and intra-cellular stimuli. The c-Abl protein is a ubiquitously expressed nonreceptor tyrosine kinase involved in the development and function of many mammalian organ systems, including the immune system and bone. It regulates the cellular response to TAM through functional interaction with the estrogen receptor, which suggests c-Abl as a therapeutic target and a prognostic tumor marker for breast cancer. c-Abl also plays a key role in signaling chemokine-induced T-cell migration. In addition, c-Abl contains NLSs (nuclear localization signals) and DNA-binding sequences important for nuclear functions. c-Abl has become an important therapeutic target in human chronic myeloid leukaemia.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-00720 | PsuK Protein, E. coli, Recombinant (His & Myc) | E. coli | E. coli | ||
Catalyzes the phosphorylation of pseudouridine to pseudouridine 5'-phosphate (PsiMP).
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TMPH-00710 | PEP synthase Protein, E. coli, Recombinant (His & SUMO) | E. coli | E. coli | ||
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
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TMPY-04568 | PDK1 Protein, Human, Recombinant (His) | Human | Baculovirus Insect Cells | ||
Pyruvate dehydrogenase kinase, isozyme 1, also known as [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial and PDK1, is a member of the PDK / BCKDK protein kinase family. PDK-1 is expressed predominantly in the heart. It contains one histidine kinase domain. Pyruvate dehydrogenase kinase (PDK) isoforms are molecular switches that downregulate the pyruvate dehydrogenase complex (PDC) by reversible phosphorylation in mitochondria. An inhibitory effect of lipoic acid on PDKs would result in less phosphorylation of E1 and hence increased PDC activity. At least two isoenzymic forms of pyruvate dehydrogenase kinase ( PDK-1 and PDK-2 ) may be involved in the regulation of enzymatic activity of mammalian pyruvate dehydrogenase complex by phosphorylation. PDK-3 appears to have the highest specific activity among the three isoenzymes. PDK-1 inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism.
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TMPH-02214 | Tomoregulin-1 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
May be a survival factor for hippocampal and mesencephalic neurons. The shedded form up-regulates cancer cell proliferation, probably by promoting ERK1/2 phosphorylation.
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TMPH-00400 | DHAK Protein, Citrobacter freundii, Recombinant (His & SUMO) | Citrobacter freundii | E. coli | ||
Catalyzes the phosphorylation of dihydroxyacetone. DHAK Protein, Citrobacter freundii, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 35.9 kDa and the accession number is P45510.
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TMPH-00515 | PPDK Protein, Entamoeba histolytica, Recombinant (His & SUMO) | Entamoeba histolytica | E. coli | ||
Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.
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TMPJ-01121 | MORF4L2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Mortality Factor 4-Like Protein 2 (MORF4L2) is a member of the mortality factor (MORF) family. MORF4L2 localizes in the nucleus, possessing a protein kinase C phosphorylation site and a tyrosine phosphorylation site. MORF4L2 interacts with the Rb tumor suppressor and it has histone deacetylase activity which can either repress or promote the activity of the B-Myb promoter depending on the tissue. In addition, MORF4L2 is involved in cell growth, regulation, and senescence.
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TMPH-02811 | NRK1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN).
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TMPY-02032 | FLRT1 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
The three fibronectin leucine-rich repeat transmembrane (FLRT) proteins contain 10 leucine-rich repeats (LRR), a type III fibronectin (FN) domain, followed by the transmembrane region, and a short cytoplasmic tail. FLRT1 is expressed in kidney and brain, which is a target for tyrosine phosphorylation mediated by FGFR1 and implicates a non-receptor Src family kinase (SFK). All FLRTs can interact with FGFR1 and FLRTs can be induced by the activation of FGF signalling by FGF-2. The phosphorylation state of FLRT1, which is itself FGFR1 dependent, may play a critical role in the potentiation of FGFR1 signalling and may also depend on a SFK-dependent phosphorylation mechanism acting via the FGFR. This is consistent with an 'in vivo' role for FLRT1 regulation of FGF signalling via SFKs. Furthermore, the phosphorylation-dependent futile cycle mechanism controlling FGFR1 signalling is concurrently crucial for regulation of FLRT1-mediated neurite outgrowth. FLRT1, FLRT2 and FLRT3 are members of the fibronectin leucine rich transmembrane protein (FLRT) family. They may function in cell adhesion and/or receptor signalling. Their protein structures resemble small leucine-rich proteoglycans found in the extracellular matrix. FLRT3 shares 55% amino acid sequence identity with FLRT1.
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TMPH-00639 | Hygromycin-B 4-O-kinase Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation. Only phosphorylates hygromycin and closely related compounds such as demethyl analogs and destomycin.
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TMPH-02135 | SPRED1 Protein, Human, Recombinant (His & Myc & SUMO) | Human | E. coli | ||
Tyrosine kinase substrate that inhibits growth-factor-mediated activation of MAP kinase. Negatively regulates hematopoiesis of bone marrow. Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2. Attenuates actin stress fiber formation via inhibition of TESK1-mediated phosphorylation of cofilin. Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells. SPRED1 Protein, Human, Recombinant (His & Myc & SUMO) is expressed in E. coli expression system with N-10xHis-SUMO and C-Myc tag. The predicted molecular weight is 70.3 kDa and the accession number is Q7Z699.
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TMPH-02648 | PKDCC Protein, Mouse, Recombinant (His & Myc) | Mouse | Baculovirus Insect Cells | ||
Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential for patterning at organogenesis stages. Mediates phosphorylation of MMP1, MMP13, MMP14, MMP19 and ERP29. May also have serine/threonine protein kinase activity. Required for longitudinal bone growth through regulation of chondrocyte differentiation. May be indirectly involved in protein transport from the Golgi apparatus to the plasma membrane. Probably plays a role in platelets: rapidly and quantitatively secreted from platelets in response to stimulation of platelet degranulation.
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TMPJ-00922 | DCK Protein, Human, Recombinant (His & T7) | Human | E. coli | ||
Deoxycytidine Kinase (DCK) is a member of the DCK/DGK family. DCK exists as a homodimer and is localized to the nucleus. DCK is required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG), and deoxyadenosine (dA). DCK has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. In addition, DCK is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents. DCK is clinically important because of its relationship to drug resistance and sensitivity.
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TMPY-04425 | PRAK/MAPKAPK5 Protein, Human, Recombinant (His & GST) | Human | Baculovirus Insect Cells | ||
MAPKAPK5 contains 1 protein kinase domain and belongs to the protein kinase superfamily, CAMK Ser/Thr protein kinase family. MAPKAPK5 has significant sequence homology to mitogen-activated protein kinase (MAPK)-activated protein kinase (MAPKAPK). It is widely distributed. MAPKAPK5 can be phosphorylated by an extracellular-regulated kinase (ERK), and p38 kinase but not by c-jun N-terminal kinase (JNK)in vitro. Recombinant GST-MAPKAPK5 protein can phosphorylate a peptide derived from the regulatory light chain of myosin II. Phosphorylation of MAPKAPK5 by ERK and p38 kinase increased its activity by 9 and 15 fold respectively. Taken together, these data suggest that MAPKAPK5 is a novel in vitro substrate for ERK and p38 kinase. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. MAPKAPK5 also mediates stress-induced small heat shock protein 27 phosphorylation.
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TMPH-02126 | SORBS2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1. May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12. Isoform 6 increases water and sodium absorption in the intestine and gall-bladder. SORBS2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 33.1 kDa and the accession number is O94875.
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TMPH-00157 | Thymidylate kinase Protein, Bacillus anthracis, Recombinant (His) | Bacillus anthracis | E. coli | ||
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. Thymidylate kinase Protein, Bacillus anthracis, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 27.8 kDa and the accession number is C3LJ02.
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TMPH-01585 | Ketohexokinase/KHK Protein, Human, Recombinant (GST) | Human | E. coli | ||
Catalyzes the phosphorylation of the ketose sugar fructose to fructose-1-phosphate. Ketohexokinase/KHK Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 59.7 kDa and the accession number is P50053.
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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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TMPY-03261 | CNPY2 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
CNPY2 is a novel MIR-interacting protein that enhances neurite outgrowth and increases myosin regulatory light chain. CNPY2 enhances migration of C6 glioma cells through phosphorylation of the myosin regulatory light chain. It is expressed in different tissues, including brain. Overexpression of CNPY2 enhanced the motility of glioma cells measured in matrigel invasion chambers and using a scratch assay. Downregulation of CNPY2 by RNA interference significantly decreased glioma cell migration and phosphorylation of MRLC. Inhibition of the corresponding MRLC kinase by ML-7 did not affect migration of CNPY2-overexpressing cells.
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TMPY-04566 | CAMKV Protein, Human, Recombinant (His & GST) | Human | Baculovirus Insect Cells | ||
CaM kinase-like vesicle-associated protein, also known as CAMKV, is a peripheral membrane protein and Cytoplasmic vesicle membrane protein which belongs to theprotein kinase superfamily and CAMK Ser/Thr protein kinase family. CAMKV contains oneprotein kinase domain. It is predominantly observed in association with the plasma membrane of soma and in neurites, both axons and dendrites. CAMKV may be associated with vesicular structures. It does not appear to have detectable kinase activity. Protein kinases are a group of enzymes that move a phosphate group onto proteins, in a process called phosphorylation. Protein kinases function as an on/off switch for many cellular processes, including metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. They also function in embryonic development, physiological responses, and in the nervous and immune system. Abnormal phosphorylation causes many human diseases, including cancer, and drugs that affect phosphorylation can treat those diseases. The protein kinase domain is a structurally conserved protein domain containing the catalytic function of protein kinases. Protein kinases play a role in a mulititude of cellular processes, including division, proliferation, apoptosis, and differentiation. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins.
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TMPK-01386 | TK1 Potein, Canine, Recombinant (His) | Canine | E. coli | ||
Thymidine kinase 1 (TK1) catalyzes the initial phosphorylation of thymidine in the salvage pathway synthesis of dTTP, an essential building block of DNA. TK1 is a cytosolic enzyme with its highest level during the S-phase of the cell cycle.
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TMPY-04445 | PDK4 Protein, Mouse, Recombinant (His & GST) | Mouse | Baculovirus Insect Cells | ||
Pyruvate dehydrogenase kinase 4 (PDK4) is a mitochondrial protein that regulates the TCA cycle.PDK4, a vital mitochondrial protein, controls the switch between glycolysis and oxidative phosphorylation based upon nutrient availability.Pyruvate dehydrogenase kinase 4 (PDK4) mRNA has been reported as an up-regulated gene in the heart and skeletal muscle of carnitine-deficient juvenile visceral steatosis (JVS) mice under fed conditions. PDK4 plays an important role in the inhibition of glucose oxidation via the phosphorylation of pyruvate dehydrogenase complex (PDC).PDK4 gene expression is stimulated by thyroid hormone (T(3)), glucocorticoids, and long chain fatty acids.
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TMPY-03507 | PPC-DC Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
PPC-DC, also known as PPCDC, belongs to the HFCD (homo oligomeric flavin containing Cys decarboxylase) superfamily which takes a part in the biosynthesis of coenzyme A (CoA) from pantothenate (Vitamin B). Biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5) is an essential universal pathway in prokaryotes and eukaryotes. This process include several steps: the phosphorylation of pantothenate, the conversion of 4’-hosphopantothenate to 4''-phosphopantetheine, the adenylation by phosphopantetheine adenylyltransferase to form dephospho-CoA and the phosphorylation by dephospho-CoA kinase to form CoA. PPC-DC, one of the last enzymes in this pathway, converts phosphopantothenoylcysteine to 4-prime-phosphopantetheine.
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TMPY-02002 | PHPT1 Protein, Human, Recombinant (His) | Human | E. coli | ||
PHPT1, also known as 14 kDa phosphohistidine phosphatase, phosphohistidine phosphatase 1, protein janus-A homolog, PHP14, is a cytoplasm protein which belongs to the janus family. PHPT1 / PHP14 is expressed abundantly in heart and skeletal muscle. Phosphatases are a diverse group of enzymes that regulate numerous cellular processes. Much of what is known relates to the tyrosine, threonine, and serine phosphatases, whereas the histidine phosphatases have not been studied as much. Protein histidine phosphorylation exists widely in vertebrates, and it plays important roles in signal transduction and other cellular functions. Protein histidine phosphorylation accounts for about 6% of the total protein phosphorylation in eukaryotic cells. The knowledge about eukaryotic PHPT (protein histidine phosphatase) is still very limited. To date, only one vertebrate PHPT has been discovered, and two crystal structures of human PHPT1 have been solved. PHPT1 / PHP14 can dephosphorylate a variety of proteins (e.g. ATP-citrate lyase and the beta-subunit of G proteins). A putative active site has been identified by its electrostatic character, ion binding, and conserved protein residues.
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TMPY-04073 | MRPL44 Protein, Human, Recombinant (His) | Human | Baculovirus Insect Cells | ||
MRPL44 (Mitochondrial Ribosomal Protein L44) is a Protein Coding gene. MRPL44 encodes a protein in the large subunit of the mitochondrial ribosome and is suggested to locate near the tunnel exit of the yeast mitochondrial ribosome. It belongs to the mitochondrion-specific ribosomal protein mL44 subfamily. In the patient fibroblasts, decreased MRPL44 affected assembly of the large ribosomal subunit and stability of 16S rRNA leading to complex IV deficiency. It may have a function in the assembly/stability of nascent mitochondrial polypeptides exiting the ribosome. MRPL44 is widely expressed in the bone marrow, lymph node, and other tissues. Diseases associated with MRPL44 include Combined Oxidative Phosphorylation Deficiency 16 and Combined Oxidative Phosphorylation Deficiency 1.
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TMPH-00726 | Ribokinase Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
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TMPH-02267 | AGTRAP Protein, Human, Recombinant (His & Myc & SUMO) | Human | E. coli | ||
Appears to be a negative regulator of type-1 angiotensin II receptor-mediated signaling by regulating receptor internalization as well as mechanism of receptor desensitization such as phosphorylation. Induces also a decrease in cell proliferation and angiotensin II-stimulated transcriptional activity.
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TMPH-03021 | PstP Protein, Mycobacterium tuberculosis, Recombinant (His) | Mycobacterium tuberculosis | E. coli | ||
Plays an important role in regulating cell division and growth by reversible phosphorylation signaling. May play important roles in regulating cellular metabolism and signaling pathways, which could mediate the growth and development of the cell. Plays a role in establishing and maintaining infection.
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TMPH-03671 | Vaccinia virus (strain Western Reserve) K3 Protein (His) | VACV | P. pastoris (Yeast) | ||
Viral mimic of eIF-2-alpha that acts as a pseudosubstrate for EIF2AK2/PKR kinase. Inhibits therefore eIF-2-alpha phosphorylation by host EIF2AK2/PKR kinase and prevents protein synthesis shutoff. Vaccinia virus (strain Western Reserve) K3 Protein (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 12.6 kDa and the accession number is P18378.
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TMPH-00422 | Ppdk Protein, Clostridium symbiosum, Recombinant (His & Myc) | Clostridium symbiosum | E. coli | ||
Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis. Ppdk Protein, Clostridium symbiosum, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 20.5 kDa and the accession number is P22983.
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TMPY-03442 | MOB4A/MOB1B Protein, Human, Recombinant (GST) | Human | E. coli | ||
MST1 and MST2 are the mammalian Ste2-related protein kinases most closely related to Drosophila Hippo, a major regulator of cell proliferation and survival during development. Overexpression of MST1 or MST2 in mammalian cells is proapoptotic. MST1 and MST2 activity increase during mitosis, especially in nocodazole-arrested mitotic cells, where these kinases exhibit an increase in both abundance and activation. MST1 and MST2 also can be activated nonphysiologically by okadaic acid or H2O2. The MOB1B and MOBKL1B polypeptides, homologs of the Drosophila MATS polypeptide, are identified as preferred MST1/MST2 substrates in vitro and are phosphorylated in cells in an MST1/MST2-dependent manner in mitosis and response to okadaic acid or H2O2. MST1/MST2-catalyzed MOB1B/MOBKL1B phosphorylation alters the ability of MOB1B/MOBKL1B to bind and regulate downstream targets such as the NDR-family protein kinases. Thus, MOB1B/MOBKL1B phosphorylation in cells promotes MOB1B/MOBKL1B binding to the LATS1 kinase and enables H2O2-stimulated LATS1 activation loop phosphorylation. Most importantly, the replacement of endogenous MOB1B/MOBKL1B by a non-phosphorylatable mutant is sufficient to accelerate cell proliferation substantially by speeding progression through G1/S as well as mitotic exit.
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TMPK-01132 | PRL-1/PTP4A1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Phosphatases of regenerating liver (PRL-1, PRL-2, and PRL-3, also known as PTP4A1, PTP4A2, and PTP4A3) control magnesium homeostasis through an association with the CNNM magnesium transport regulators. PRL-1 (PTP4A1) is a key molecule that activates tyrosine phosphorylation, which is important for cancer progression and metastasis.
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TMPH-03194 | GCK Protein, Pyrococcus horikoshii, Recombinant (His & Myc) | Pyrococcus horikoshii | E. coli | ||
Catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-phosphoglycerate. It can also utilize GTP, CTP, UTP, ADP or pyrophosphate as phosphate donor. GCK Protein, Pyrococcus horikoshii, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 54.8 kDa and the accession number is O58231.
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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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TMPH-02855 | PML Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum. Regulates RB1 phosphorylation and activity. Acts as both a negative regulator of PPARGC1A acetylation and a potent activator of PPAR signaling and fatty acid oxidation. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates PER2 nuclear localization and circadian function. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. Required for normal development of the brain cortex during embryogenesis. Plays a role in granulopoiesis or monopoiesis of myeloid progenitor cells. May play a role regulating stem and progenitor cell fate in tissues as diverse as blood, brain and breast. Shows antiviral activity towards lymphocytic choriomeningitis virus (LCMV) and the vesicular stomatitis virus (VSV).
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TMPH-03672 | Vaccinia virus (strain Western Reserve) K3 Protein (His & SUMO) | VACV | E. coli | ||
Viral mimic of eIF-2-alpha that acts as a pseudosubstrate for EIF2AK2/PKR kinase. Inhibits therefore eIF-2-alpha phosphorylation by host EIF2AK2/PKR kinase and prevents protein synthesis shutoff. Vaccinia virus (strain Western Reserve) K3 Protein (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 26.6 kDa and the accession number is P18378.
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TMPJ-00218 | SLAMF6 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 Cells | ||
SLAM Family Member 6 (SLAMF6) is a 60 kD single-pass type I membrane protein that belongs to the SLAM subgroup of the CD2 family. Human SLAMF6/ NTB-A contains a 205 amino acid extracellular domain (ECD) with one Ig-like V-set and one Ig-like C2-set domain, a 21 amino acid transmembrane segment and an 84 amino acid cytoplasmic domain, with two immunoreceptor tyrosine-based switch motifs. SLAMF6 is a homodimer. SLAMF6 can interact with PTN6 and, upon phosphorylation, with PTN11 and SH2D1A/SAP. Phosphorylation-dependent NTB-A association with SAP is required for full production of IFN-γ by NK cells and independent of EAT-2 binding. It Triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors. On B cells, NTB-A modulates immunoglobulin class switching and the balance between tolerance and autoimmunity.
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TMPH-03670 | Vaccinia virus (strain Copenhagen) K3 Protein (His & SUMO) | VACV | E. coli | ||
Viral mimic of eIF-2-alpha that acts as a pseudosubstrate for EIF2AK2/PKR kinase. Inhibits therefore eIF-2-alpha phosphorylation by host EIF2AK2/PKR kinase and prevents protein synthesis shutoff. Vaccinia virus (strain Copenhagen) K3 Protein (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 26.5 kDa and the accession number is P20639.
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TMPJ-00978 | PIP4K2A Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha (PIP4K2A) is a member of the phosphatidylinositol-4-phosphate 5-kinase family. It contains 1 PIPK domain and is expressed ubiquitously, with high levels in the brain. It catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). It may exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. It may regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation, negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P. It also involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size.
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TMPH-01694 | MLKL Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process. Does not have protein kinase activity. Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. In addition to TNF-induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: following activation by ZBP1, MLKL is phosphorylated by RIPK3 in the nucleus, triggering disruption of the nuclear envelope and leakage of cellular DNA into the cytosol.following ZBP1 activation, which senses double-stranded Z-RNA structures, nuclear RIPK3 catalyzes phosphorylation and activation of MLKL, promoting disruption of the nuclear envelope and leakage of cellular DNA into the cytosol. Binds to highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which is essential for its necroptotic function.
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TMPK-01095 | MEPE Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
Matrix extracellular phosphoglycoprotein (MEPE) is expressed in bone and teeth where it has multiple functions. The C-terminus of MEPE contains a mineral-binding, acidic serine- and aspartate-rich motif (ASARM) that is also present in other noncollagenous proteins of mineralized tissues.MEPE-derived ASARM peptides function in phosphate homeostasis and direct inhibition of bone mineralization in a phosphorylation-dependent manner.
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