目录号 | 产品详情 | 靶点 | |
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T60043 | Phospholipase | ||
DPTIP 是一种有效的中性鞘磷脂酶 2 抑制剂,IC50 值为 30 nM。 | |||
T7917 | Proteasome | ||
4'-Hydroxychalcone (2-Benzal-4-Hydroxyacetophenone) 是从甘草根中分离的一种查尔酮,具有保护肝脏的作用。它能诱导大鼠离体肝线粒体囊泡快速释放钾,并引起其线粒体呼吸控制和氧化磷酸化衰退。它能通过抑制蛋白酶体 (proteasome),抑制TNFα 诱导的 NF-κB 活性。 | |||
T77579 | IL Receptor Dehydrogenase ROS Caspase NOD-like Receptor (NLR) AIM2 | ||
JC2-11 是一种对炎症有抑制作用的化合物。JC2-11 对含有募集结构域的蛋白质 NLRC 4、黑色素瘤 2 中缺失 (AIM 2) 和非典型 (NC) 炎症小体有抑制作用,通过破坏活性氧的产生和 caspase-1 的活性来抑制炎症小体的活化。JC2-11 减少了炎症小体中 caspase-1 (p20) 的分泌、gasdermin D (GSDMD) 的裂解、IL-1β 和乳酸脱氢酶 (LDH) 的释放。 | |||
T6887 | NOD-like Receptor (NLR) NOD | ||
MCC950 sodium (CP-456773 sodium) 是一种炎症小体 NLRP3 的抑制剂 (IC50=7.5 nM in BMDMs; IC50=8.1 nM in HMDMs),具有高效选择性。MCC950 sodium 对其他炎症小体,如 AIM2、 NLRC4 或 NLRP1 没有作用。 | |||
T0719 | Others Dopamine Receptor Monoamine Transporter | ||
Tetrabenazine (Ro 1-9569) 是 VMAT 抑制剂,用作抗精神病药和治疗各种运动障碍。 | |||
T19554 | Others Sodium Channel Endogenous Metabolite | ||
L-Aspartic aicd sodium (Sodium L-aspartate) 是一种氨基酸,是一种结肠特异性活性分子输送的前体活性分子,可促进大鼠前脑膜囊泡的 Na+外排。 | |||
T13133 | Monoamine Transporter | ||
Tetrabenazine Metabolite ((-)-β-HTBZ) 是一种囊泡单胺转运蛋白 2 (VMAT2) 抑制剂,是 Tetrabenazine 的一种活性代谢物。Tetrabenazine Metabolite 对 VMAT2 具有高亲和力,其Ki 为13.4 nM。Tetrabenazine Metabolite 常常被用于研究与亨廷顿氏病和其他多动障碍相关的舞蹈病。 | |||
T2556 | Others HIV Protease | ||
Nandrolone decanoate (19-Nortestosterone decanoate) 是一种合成代谢雄激素,通过涉及谷氨酸诱导的 N-甲基-D-天冬氨酸受体过度兴奋的机制诱导攻击性行为表征。 | |||
T3534 | Monoamine Transporter | ||
Tetrabenazine Racemate (Rubigen) 是一种选择性和可逆的囊泡单胺转运蛋白 2(VMAT-2) 抑制剂。它阻断神经递质吸收到肾上腺素能储存囊泡中,并已被用作囊泡运输系统的高亲和力标记。 | |||
TF0112 | Others | ||
DPPS (12-Dipalmitoyl-sn-glycero-3-PS sodium salt) 是一种阴离子二酰基磷脂,是磷脂酰丝氨酸(PS)的一种形式,是一种位于细胞膜内小叶的带负电荷的磷脂。DPPS 被用来制作阳离子囊泡和脂质体。 |
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-00876 | Legumain Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
The Mammalian Legumain, also known as LGMN, also called asparaginyl endopeptidase (AEP), is a cysteine protease belonging to peptidase family C13 with strict specificity for hydrolysis of asparaginyl bonds. Known previously only from plants and invertebrates, Legumain is discovered as a lysosomal endopeptidase in mammals. Mammalian Legumain is a cysteine endopeptidase, inhibited by iodoacetamide and maleimides, but unaffected by compound E64. The Mammalian Legumain is involved in the processing of bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Legumain has been observed to be highly expressed in several types of solid tumors. It was demonstrated in membrane-associated vesicles concentrated at the invadopodia of tumor cells and on cell surfaces where it colocalized with integrins. Legumain was demonstrated to activate progelatinase A. Cells overexpressing Legumain possessed increased migratory and invasive activity in vitro and adopted an invasive and metastatic phenotype in vivo, inferring significance of Legumain in tumor invasion and metastasis. Also, Legumain is expressed in both murine and human atherosclerotic lesions. The macrophage-specific expression of Legumain in vivo and the ability of Legumain to induce chemotaxis of monocytes and endothelial cells in vitro suggest that Legumain may play a functional role in atherogenesis.
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TMPY-04922 | FAP Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
Seprase, also known as 17 kDa melanoma membrane-bound gelatinase , Fibroblast activation protein alpha, Integral membrane serine protease and FAP, is a single-pass type II membrane protein which belongs to thepeptidase S9B family. Seprase / FAP is found in cell surface lamellipodia, invadopodia and on shed vesicles. Seprase / FAP appears to act as a proteolytically active 17-kDa dimer, consisting of two 97-kDa subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. Seprase / FAP colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Seprase / FAP colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. In association with DPP4, Seprase / FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. Seprase / FAP has a dual function in tumour progression. The proteolytic activity of Seprase has been shown to promote cell invasiveness towards the ECM and also to support tumour growth and proliferation. Seprase / FAP may have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02154 | FAP Protein, Human, Recombinant (His) | Human | HEK293 | ||
Seprase, also known as 17 kDa melanoma membrane-bound gelatinase , Fibroblast activation protein alpha, Integral membrane serine protease and FAP, is a single-pass type II membrane protein which belongs to thepeptidase S9B family. Seprase / FAP is found in cell surface lamellipodia, invadopodia and on shed vesicles. Seprase / FAP appears to act as a proteolytically active 17-kDa dimer, consisting of two 97-kDa subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. Seprase / FAP colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Seprase / FAP colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. In association with DPP4, Seprase / FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. Seprase / FAP has a dual function in tumour progression. The proteolytic activity of Seprase has been shown to promote cell invasiveness towards the ECM and also to support tumour growth and proliferation. Seprase / FAP may have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04962 | FAP Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Seprase, also known as 17 kDa melanoma membrane-bound gelatinase , Fibroblast activation protein alpha, Integral membrane serine protease and FAP, is a single-pass type II membrane protein which belongs to thepeptidase S9B family. Seprase / FAP is found in cell surface lamellipodia, invadopodia and on shed vesicles. Seprase / FAP appears to act as a proteolytically active 17-kDa dimer, consisting of two 97-kDa subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. Seprase / FAP colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Seprase / FAP colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. In association with DPP4, Seprase / FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. Seprase / FAP has a dual function in tumour progression. The proteolytic activity of Seprase has been shown to promote cell invasiveness towards the ECM and also to support tumour growth and proliferation. Seprase / FAP may have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-02979 | SLC30A8 Protein, Mouse, Recombinant (His) | Mouse | in vitro E. coli expression system | ||
Facilitates the accumulation of zinc from the cytoplasm into intracellular vesicles, being a zinc-efflux transporter. May be a major component for providing zinc to insulin maturation and/or storage processes in insulin-secreting pancreatic beta-cells.
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TMPH-00083 | Dehydrin ERD14 Protein, Arabidopsis thaliana, Recombinant (His & Myc) | Arabidopsis thaliana | E. coli | ||
Intrinsically disordered protein acting as a chaperone. Prevents heat-induced aggregation and/or inactivation of various substrates. Binds to acidic phospholipid vesicles without affecting membrane fluidity.
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TMPH-00304 | SV2A Protein, Bovine, Recombinant (His & Myc) | Bovine | HEK293 | ||
Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles.
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TMPH-01100 | CLINT1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly.
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TMPH-02249 | TRIM72 Protein, Human, Recombinant (E. coli, His & Myc) | Human | E. coli | ||
Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles.
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TMPH-02951 | TRIM72 Protein, Mouse, Recombinant (His) | Mouse | Yeast | ||
Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles.
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TMPH-00317 | BipD Protein, Burkholderia pseudomallei, Recombinant (His & Myc) | Burkholderia pseudomallei | E. coli | ||
Required for invasion of epithelial cells, as well as for survival within host cells, escape from endocytic vesicles and subsequent actin-tail formation. Probably regulates the secretion of effectors BipB and BipC and their final integration into the target cell membrane.
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TMPH-01099 | CLTCL1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.
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TMPH-02248 | TRIM72 Protein, Human, Recombinant (His & Myc) | Human | Baculovirus | ||
Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles.
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TMPH-02323 | SLC30A8 Protein, Human, Recombinant (His) | Human | in vitro E. coli expression system | ||
Facilitates the accumulation of zinc from the cytoplasm into intracellular vesicles, being a zinc-efflux transporter. May be a major component for providing zinc to insulin maturation and/or storage processes in insulin-secreting pancreatic beta-cells.
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TMPK-01161 | LAMP5 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Lysosome-associated membrane protein 5 (LAMP5) is a mammalian ortholog of the Caenorhabditis elegans protein, UNC-46, which functions as a sorting factor to localize the vesicular GABA transporter UNC-47 to synaptic vesicles. LAMP5 deficiency led to a larger intensity-dependent increase of wave I, II and V peak amplitude of auditory brainstem response. LAMP5 plays a pivotal role in sensorimotor processing in the brainstem and spinal cord.
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TMPK-01234 | LAMP5 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Lysosome-associated membrane protein 5 (LAMP5) is a mammalian ortholog of the Caenorhabditis elegans protein, UNC-46, which functions as a sorting factor to localize the vesicular GABA transporter UNC-47 to synaptic vesicles. LAMP5 deficiency led to a larger intensity-dependent increase of wave I, II and V peak amplitude of auditory brainstem response. LAMP5 plays a pivotal role in sensorimotor processing in the brainstem and spinal cord.
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TMPH-02161 | Synapsin-1 Protein, Human, Recombinant (GST) | Human | E. coli | ||
Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level.
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TMPH-03446 | SSA1 Protein, S. cerevisiae, Recombinant (His & Myc) | Saccharomyces cerevisiae | E. coli | ||
May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.
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TMPH-02183 | CCT2 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
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TMPH-01255 | DNM1L Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes. While the recruitment by the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane. Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner. Plays an important role in mitochondrial fission during mitosis. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution. Rhythmic control of its activity following phosphorylation at Ser-637 is essential for the circadian control of mitochondrial ATP production.; Inhibits peroxisomal division when overexpressed.; Inhibits peroxisomal division when overexpressed.
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TMPY-00526 | VTI1A Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
Evolutionarily conserved SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptors) proteins form a complex that drives membrane fusion in eukaryotes. VTI1A and VTI1B are the only members of their SNARE subclass and the yeast homolog Vti1p is essential for cell survival. VTI1A is involved in regulating insulin-stimulated trafficking of secretory vesicles enriched with both GLUT4 (glucose transporter) and Acrp30 in adipocytes; it also plays key roles in neuronal development and in selectively maintaining spontaneous neurotransmitter release.
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TMPH-02952 | TRIM72 Protein, Mouse, Recombinant (E. coli, His) | Mouse | E. coli | ||
Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles.
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TMPK-00659 | LAMP5 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Lysosome-associated membrane protein 5 (LAMP5) is a mammalian ortholog of the Caenorhabditis elegans protein, UNC-46, which functions as a sorting factor to localize the vesicular GABA transporter UNC-47 to synaptic vesicles. In the mouse forebrain, LAMP5 is expressed in a subpopulation of GABAergic neurons in the olfactory bulb and the striato-nigral system, where it is required for fine-tuning of GABAergic synaptic transmission.
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TMPH-01209 | DENND1A Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Guanine nucleotide exchange factor (GEF) regulating clathrin-mediated endocytosis through RAB35 activation. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB35 into its active GTP-bound form. Regulates clathrin-mediated endocytosis of synaptic vesicles and mediates exit from early endosomes. Binds phosphatidylinositol-phosphates (PtdInsPs), with some preference for PtdIns(3)P.
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TMPK-01233 | LAMP5 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Lysosome-associated membrane protein 5 (LAMP5) is a mammalian ortholog of the Caenorhabditis elegans protein, UNC-46, which functions as a sorting factor to localize the vesicular GABA transporter UNC-47 to synaptic vesicles. In the mouse forebrain, LAMP5 is expressed in a subpopulation of GABAergic neurons in the olfactory bulb and the striato-nigral system, where it is required for fine-tuning of GABAergic synaptic transmission.
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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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TMPJ-00740 | PTH Protein, Human, Recombinant | Human | E. coli | ||
Parathyroid hormone is the most important endocrine regulator of calcium and phosphorus concentration in extracellular fluid. This hormone is secreted from cells of the parathyroid glands and finds its major target cells in bone and kidney. Another hormone, parathyroid hormone-related protein, binds to the same receptor as parathyroid hormone and has major effects on development. Like most other protein hormones, parathyroid hormone is synthesized as a preprohormone. After intracellular processing, the mature hormone is packaged within the Golgi into secretory vesicles, the secreted into blood by exocytosis. Parathyroid hormone is secreted as a linear protein of 84 amino acids.
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TMPH-02162 | Synaptotagmin-1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Calcium sensor that participates in triggering neurotransmitter release at the synapse. May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes.
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TMPH-02334 | RAB12 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy.
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TMPY-02217 | HSC70 Protein, Human, Recombinant (His) | Human | E. coli | ||
HSPA8, also known as HSC70, is a member of the heat shock protein family due to homology with other heat shock proteins. The heat shock protein 70 family is comprised of both heat-inducible and constitutively expressed members. The latter are called heat-shock cognate proteins. HSPA8 belongs to the heat-shock cognate subgroup. Members of the human heat-shock protein multigene family have several highly conserved proteins with structural and functional properties in common but vary in the extent of their inducibility in response to metabolic stress. HSPA8 is constitutively expressed and performs functions related to normal cellular processes. This protein binds to nascent polypeptides to facilitate correct protein folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during the transport of membrane components through the cell. Two alternatively spliced variants have been characterized to date. HSPA8 acts as a repressor of transcriptional activation. It inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing with the co-chaperones. It also is an ATPase that works with Auxilin to remove clathrin-coated vesicles. In neurons, synaptojanin is also an important protein involved in vesicle uncoating.
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TMPY-01476 | S100A13 Protein, Human, Recombinant | Human | E. coli | ||
S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from theneural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A13, also known as S100 calciumbinding protein A13, is a member of the S-100 family. It contains two EF-hand domains. S100A13 binds two calcium ions per subunit and one copper ion. Binding of one copper ion does not interfere with calcium-binding. S100A13 is required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine. S100A13 plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway.
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TMPY-03604 | VAMP3 Protein, Human, Recombinant (His) | Human | E. coli | ||
VAMP3, also known as cellubrevin, is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. Because of VAMP3 gene's high homology to other known VAMPs, its broad tissue distribution, and its subcellular localization, VAMP3 was shown to be the human equivalent of the rodent cellubrevin. In platelets VAMP3 resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.
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TMPH-02873 | RAB10 Protein, Mouse, Recombinant (His & SUMO) | Mouse | E. coli | ||
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane. In epithelial cells, it regulates transport from the Golgi to the basolateral membrane. May play a role in the basolateral recycling pathway and in phagosome maturation. May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion. Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis. When phosphorylated by LRRK2 on Thr-73, it binds RILPL1 and inhibits ciliogenesis.
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TMPY-04072 | VTI1A Protein, Human, Recombinant (His) | Human | HEK293 | ||
Evolutionarily conserved SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptors) proteins form a complex that drives membrane fusion in eukaryotes. VTI1A and VTI1B are the only members of their SNARE subclass and the yeast homolog Vti1p is essential for cell survival. VTI1A is involved in regulating insulin-stimulated trafficking of secretory vesicles enriched with both GLUT4 (glucose transporter) and Acrp30 in adipocytes; it also plays key roles in neuronal development and in selectively maintaining spontaneous neurotransmitter release.
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TMPJ-00193 | TREML1 Protein, Human, Recombinant (hFc) | Human | Human Cells | ||
Triggering Receptor Expressed on Myeloid Cells-Like Protein 1 (TREML1) is a single-pass type I membrane protein. TREML1 precursor contains a 15 amino acid signal peptide, a 147 amino acid extracellular domain with an Ig-like V-type (immunoglobulin-like) domain, and 128 amino acid cytoplasmic domain. It can be expressed exclusively in platelets and megakaryocytes (MKs). It is a cell surface receptor that may play a role in the innate and adaptive immune response. TREML1 Sequestered in cytoplasmic vesicles in resting platelets. TREML1 be transported to the cell surface after stimulation by thrombin. Soluble fragments can be released into the serum by proteolysis. The phosphorylated TREML1 can interact with PTPN6 and PTPN11. TREML1 may participate in maintaining vascular hemostasis and regulating coagulation and inflammation at sites of injury.
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TMPY-03699 | S100A13 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from theneural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A13, also known as S100 calciumbinding protein A13, is a member of the S-100 family. It contains two EF-hand domains. S100A13 binds two calcium ions per subunit and one copper ion. Binding of one copper ion does not interfere with calcium-binding. S100A13 is required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine. S100A13 plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway.
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TMPY-04861 | TMED1 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
TMED1 belongs to the EMP24/GP25L family. It contains 1 GOLD domain and is widely expressed. TMED1 binds to its receptor IL1RL1 and results in the activation of DNA binding by nuclear factor NF-kappa-B or transcription from the IL8 promoter and most likely requires other proteins to elicit these activities. Dendritic cells from Peyer's patches (but not from spleen) express TMED1 in response to treatment with LPS. TMED1 may play a role in vesicular protein trafficking, mainly in the early secretory pathway. It may act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side.
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TMPY-03108 | TMED1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
TMED1 belongs to the EMP24/GP25L family. It contains 1 GOLD domain and is widely expressed. TMED1 binds to its receptor IL1RL1 and results in the activation of DNA binding by nuclear factor NF-kappa-B or transcription from the IL8 promoter and most likely requires other proteins to elicit these activities. Dendritic cells from Peyer's patches (but not from spleen) express TMED1 in response to treatment with LPS. TMED1 may play a role in vesicular protein trafficking, mainly in the early secretory pathway. It may act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side.
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TMPH-03741 | BoNT/F Protein, Clostridium botulinum, Recombinant (His) | Clostridium botulinum | E. coli | ||
Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin F which may have 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of the HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release. Whole toxin only has protease activity after reduction, which releases LC. Requires complex eukaryotic host polysialogangliosides for full neurotoxicity. It is not clear whether a synaptic vesicle protein acts as its receptor; there is evidence for and against SV2 fulfilling this function.; Has proteolytic activity. After translocation into the eukaryotic host cytosol, inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '60-Gln-|-Lys-61' bond of synaptobrevin-1/VAMP1 and the equivalent 'Gln-|-Lys' sites in VAMP2 and VAMP3. Cleaves the '48-Gln-|-Lys-49' bond of A.californica synaptobrevin (AC P35589).; Responsible for host epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and the receptor protein SV2A, SV2B and SV2C in close proximity on host synaptic vesicles; although not all evidence indicates these are the receptors. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site; it may also prevent premature LC dissociation from the translocation channel and protect toxin prior to translocation. The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol.
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TMPY-03852 | Dopamine beta-Hydroxylase Protein, Human, Recombinant (His) | Human | HEK293 | ||
DBH is a 29 kDa copper-containing oxygenase. It can be detected in noradrenergic nerve terminals of the central and peripheral nervous systems, and is also expressed in chromaffin cells of the adrenal medulla. DBH contains our identical subunits, and its activity requires ascorbate as a cofactor. It functions in in the synthesis of small-molecule neurotransmitters that is membrane-bound, making norepinephrine the only transmitter synthesized inside vesicles. DBH has been shown to be associated with decision making and addictive behaviors such as alcohol and smoking, attention deficit hyperactivity disorder, and also with neurological diseases such as Schizophrenia and Alzheimer's.
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TMPJ-00448 | NRG1 beta 1 Protein, Human, Recombinant (aa 2-246) | Human | E. coli | ||
Pro-neuregulin-1,Neuregulin-1 beta 1(NRG1) is a single-pass type I membrane protein and belongs to the neuregulin family .It contains 1 EGF-like domain and 1 Ig-like C2-type (immunoglobulin-like) domain. Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. The protein concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Isoform 10 may play a role in motor and sensory neuron development.
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TMPY-00151 | Alpha SNAP Protein, Human, Recombinant (His) | Human | E. coli | ||
NAPA (NSF Attachment Protein Alpha) is a Protein Coding gene. This gene encodes a member of the soluble NSF attachment protein (SNAP) family. SNAP proteins play a critical role in the docking and fusion of vesicles to target membranes as part of the 20S NSF-SNAP-SNARE complex. NAPA represents an anti-apoptotic protein that promotes resistance to cisplatin in cancer cells by inducing the degradation of the tumor suppressor p53. NAPA overexpression decreased the ubiquitination and degradation of synoviolin and reduced p53 protein level. The combination of cisplatin and knockdown of NAPA represents a novel and attractive strategy to eradicate p53-sensitive cancer cells. NAPA-73 as one of the earliest neuronal markers may reflect a difference between the central and peripheral nervous systems.
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TMPY-03119 | TMED1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
TMED1 belongs to the EMP24/GP25L family. It contains 1 GOLD domain and is widely expressed. TMED1 binds to its receptor IL1RL1 and results in the activation of DNA binding by nuclear factor NF-kappa-B or transcription from the IL8 promoter and most likely requires other proteins to elicit these activities. Dendritic cells from Peyer's patches (but not from spleen) express TMED1 in response to treatment with LPS. TMED1 may play a role in vesicular protein trafficking, mainly in the early secretory pathway. It may act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side.
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TMPY-00728 | Carboxypeptidase E Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Carboxypeptidase E (CPE), also known as Carboxypeptidase H, is a peripheral membrane protein and a zinc metallocarboxypeptidase, and the conversion of proCPE into CPE occurs primarily in secretory vesicles. The active form of CPE cleaves C-terminal amino acid residues of the peptide, and is thus involved in the biosynthesis of peptide hormones and neurotransmitters including insulin, enkephalin, etc. The enzymatic activity is enhanced by millimolar concentrations of Co2+. It has also been proposed that membrane-associated carboxypeptidase E acts as a sorting receptor for targeting regulated secretory proteins which are mostly prohormones and neuropeptides in the trans-Golgi network of the pituitary and in secretory granules into the secretory pathway.Its interaction with glycosphingolipid-cholesterol rafts at the TGN facilitates the targeting. Mutations in this gene are implicated in type II diabetes due to impaired glucose clearance and insulin resistance.
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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-01960 | Munc18c/STXBP3 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
Syntaxin-binding protein 3, also known as Platelet Sec1 protein, Protein unc-18 homolog 3, Protein unc-18 homolog C, Unc-18C, Unc18-3 and STXBP3, is a cytoplasm protein which belongs to the STXBP/unc-18/SEC1 family. STXBP3 is expressed in cells that exhibit granule exocytosis, such as neutrophils, mast cells, platelets and endothelial cells. STXBP3, together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking / fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes. STXBP3 participates in the consolidation and secretion of secondary and tertiary granules. STXBP3 contains one SEC1 domain. Phosphorylation at Ser129 may stimulate granule release. Human STXBP3 shares 9% aa identity with mouse STXBP3. STXBP3 interacts with DOC2B; the interaction is direct, occurs at the cell membrane, excludes interaction with STX4 and regulates glucose-stimulated insulin secretion. Interacts with STX4.
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TMPH-02302 | VPS4A Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. Involved in cytokinesis: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission. VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan.; (Microbial infection) In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses).
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TMPJ-00684 | SNCA Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Alpha-synuclein (Snca) belongs to a family of proteins including a-, b-, and g-synucleins. Alpha-synuclein has been found to be implicated in the pathophysiology of many neurodegenerative diseases, including Parkinson's disease (PD) and Alzheimer's disease. Manyneurodegenerative diseases has shown that alpha-synuclein accumulates in dystrophic neurites and in Lewy bodies. The function of alpha-synuclein is closely correlated with its three-dimensional structure, especially for proteins important in the pathogenesis of neurodegenerative diseases. Alpha-synuclein is a dynamic molecule whose secondary structure depends on the environment. For example, it has an unfolded random coil structure in aqueous solution, forms a-helical structure upon binding to acidic phospholipid vesicles, and forms insoluble fibrils with a high b-sheet content that resemble the filaments found in Lewy bodies. Also, alpha-synuclein was known to associate with 14-3-3 proteins including protein kinase C, BAD, and extracellular regulated kinase, and overexpression of alpha-synuclein could contribute to cell death in neurodegenerative diseases.
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TMPY-01141 | Carboxypeptidase E Protein, Human, Recombinant (His) | Human | HEK293 | ||
Carboxypeptidase E (CPE), also known as Carboxypeptidase H, is a peripheral membrane protein and a zinc metallocarboxypeptidase, and the conversion of proCPE into CPE occurs primarily in secretory vesicles. The active form of CPE cleaves C-terminal amino acid residues of the peptide, and is thus involved in the biosynthesis of peptide hormones and neurotransmitters including insulin, enkephalin, etc. The enzymatic activity is enhanced by millimolar concentrations of Co2+. It has also been proposed that membrane-associated carboxypeptidase E acts as a sorting receptor for targeting regulated secretory proteins which are mostly prohormones and neuropeptides in the trans-Golgi network of the pituitary and in secretory granules into the secretory pathway.Its interaction with glycosphingolipid-cholesterol rafts at the TGN facilitates the targeting. Mutations in this gene are implicated in type II diabetes due to impaired glucose clearance and insulin resistance.
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