目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T13486 | Others | ||
Neurodegenerative Disorder-Targeting Compound 1 是一种靶向 calpain 的抑制剂。 | |||
TC0039 | Others | ||
Vasicinone 是一种喹唑啉类生物碱,分离自凡士林植物中。它是具有研究帕金森病和其他氧化应激相关神经退行性疾病的潜力。 | |||
T83527 | |||
(Rac)-Neurodegenerative Disorder-Targeting Compound 1为一种针对神经退行性疾病的化合物,具有calpain抑制活性。 | |||
T8849 | MAO | ||
PF-9601N 是一种单胺氧化酶 B (MAO-B) 抑制剂,在多种体内外模型中表现出抗帕金森病 (PD) 的神经保护作用。它可用于研究兴奋性毒性介导的神经退行性疾病。 | |||
T21883 | HSP | ||
Gedunin 是从印楝种子中提取的一种重要柠檬苦素,具有抗癌、抗病毒、抗炎和杀虫活性。它可阻断 SARS-CoV-2 病毒进入人宿主细胞,用于 COVID-19 研究。它是Hsp90抑制剂,诱导 Hsp90 依赖的蛋白降解,抑制卵巢癌细胞增殖。 | |||
T1880 | Others | ||
P7C3 是一种 aminopropyl carbazole 类化合物,具有口服活性,可透过血脑屏障,具有神经保护作用。它可用于神经退行性疾病,如帕金森病的研究。 | |||
T8860 | Androgen Receptor | ||
DSRM-3716 是选择性的SARM1 NADase 抑制剂,IC50为 75 nM,相较于其他 NAD+加工酶、受体和转运蛋白具有选择性。DSRM-3716显示出强大的轴突保护作用。 | |||
TN6953 | Endogenous Metabolite | ||
Lignoceric Acid (tetracosanoic acid) 是一种 24 碳饱和 (24:0) 脂肪酸,在发育中的大脑中合成,也是一种木质素生产的副产品。它能够用于研究 Zellweger 脑-肝-肾综合征和肾上腺脑白质营养不良。 | |||
T22043 | Others | ||
BCATc Inhibitor 2 是选择性分支链氨基转移酶抑制剂,可用于神经退行性疾病的研究。能够抑制 rBCATc (IC50:0.2 μM),hBCATc (IC50:0.8 μM)、 rBCATm (IC50:3.0 μM)。其中BCATc 也称为 BCAT1,存在于细胞质基质中的亚型。 | |||
T35856 | AAK1 (AP2 associated kinase 1) | ||
BMS-986176 是一种有效的AAK1 抑制剂,IC50为 2.2 nM。BMS-986176在神经退行性疾病中有研究的价值。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPJ-00135 | BDNF Protein, Human/Murine/Rat, Recombinant | Human,Mouse,Rat | E. coli | ||
Brain-Derived Neurotrophic Factor (BDNF) is a member of the neurotrophin family. Along with other structurally related neurotrophic factors NGF, NT-3 and NT-4, BDNF binds with high affinity to the TrkB kinase receptor. It also binds with the LNGFR (for low-affinity nerve growth factor receptor, also known as p75). BDNF promotes the survival, growth and differentiation of neurons. It serves as a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. BDNF expression is altered in neurodegenerative disorders such as Parkinson's and Alzheimer's disease.
|
|||||
TMPY-02881 | RAGE Protein, Human, Recombinant | Human | HEK293 | ||
Receptor for Advanced Glycosylation End Products (RAGE, or AGER) is a member of the immunoglobulin super-family transmembrane proteins, as a signal transduction receptor which binds advanced glycation endproducts, certain members of the S100/calgranulin family of proteins, high mobility group box 1 (HMGB1), advanced oxidation protein products, and amyloid (beta-sheet fibrils). Initial studies investigating the role of RAGE in renal dysfunction focused on diabetes, neurodegenerative disorders, and inflammatory responses. However, RAGE also has roles in the pathogenesis of renal disorders that are not associated with diabetes, such as obesity-related glomerulopathy, doxorubicin-induced nephropathy, hypertensive nephropathy, lupus nephritis, renal amyloidosis, and ischemic renal injuries. RAGE represents an important factor in innate immunity against pathogens, but it also interacts with endogenous ligands, resulting in chronic inflammation. RAGE signaling has been implicated in multiple human illnesses, including atherosclerosis, arthritis, Alzheimer's disease, atherosclerosis and aging associated diseases.
|
|||||
TMPY-01355 | Transglutaminase 2/TGM2 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Protein-glutamine gamma-glutamyltransferase 2, also known as Tissue transglutaminase, Transglutaminase C, Transglutaminase-2, and TGM2, is a member of the transglutaminase superfamily. TGM2 plays a role in cell growth and survival through the anti-apoptosis signaling pathway. It is a calcium-dependent acyltransferase that also undergoes a GTP-binding/GTPase cycle even though it lacks any obvious sequence similarity with canonical GTP-binding (G) proteins. TGM2 is a multi-functional protein which catalyzes transamidation reactions or acts as a G-protein in intracellular signalling. As an enzyme which is responsible for the majority of transglutaminase (TG) activity in the brain, TGM2 is likely to play a modulatory role in nervous system development and has regulatory effect on neuronal cell death as well. Most importantly, numerous studies have presented data demonstrating that dysregulation of TGM2 may contribute to the pathogenesis of many neurodegenerative disorders, including Huntington's disease, Alzheimer's disease, Parkinson's disease and amyotrophic lateral sclerosis as well as nervous system injuries.
|
|||||
TMPY-02078 | HtrA2/Omi Protein, Human, Recombinant (His) | Human | E. coli | ||
Serine protease HTRA2, also known as high-temperature requirement protein A2, Omi stress-regulated endoprotease, Serine protease 25, Serine proteinase OMI and HTRA2, is a single-pass membrane protein that belongs to the peptidase S1B family. HTRA2 contains one PDZ (DHR) domain. HTRA2 is a serine protease that shows proteolytic activity against a non-specific substrate beta-casein. It promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity or by a BIRC inhibition-independent, caspase-independent, and serine protease activity-dependent mechanism. HTRA2 cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 of HTRA2 seems to be proteolytically inactive. Defects in HTRA2 are the cause of Parkinson disease type 13 (PARK13) which is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity, and postural instability, as well as by a clinically significant response to treatment with levodopa.
|
|||||
TMPY-02767 | TPP1 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Tripeptidyl-peptidase 1 (TPP1 / CLN2) is a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. TPP1 / CLN2 may act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Defects in TPP1 / CLN2 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2), a form of neuronal ceroid lipofuscinosis which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy.
|
|||||
TMPY-02927 | RAGE Protein, Human, Recombinant (His) | Human | HEK293 | ||
Receptor for Advanced Glycosylation End Products (RAGE, or AGER) is a member of the immunoglobulin super-family transmembrane proteins, as a signal transduction receptor which binds advanced glycation endproducts, certain members of the S100/calgranulin family of proteins, high mobility group box 1 (HMGB1), advanced oxidation protein products, and amyloid (beta-sheet fibrils). Initial studies investigating the role of RAGE in renal dysfunction focused on diabetes, neurodegenerative disorders, and inflammatory responses. However, RAGE also has roles in the pathogenesis of renal disorders that are not associated with diabetes, such as obesity-related glomerulopathy, doxorubicin-induced nephropathy, hypertensive nephropathy, lupus nephritis, renal amyloidosis, and ischemic renal injuries. RAGE represents an important factor in innate immunity against pathogens, but it also interacts with endogenous ligands, resulting in chronic inflammation. RAGE signaling has been implicated in multiple human illnesses, including atherosclerosis, arthritis, Alzheimer's disease, atherosclerosis and aging associated diseases.
|
|||||
TMPY-01691 | Clusterin Protein, Human, Recombinant (CLU34, His) | Human | HEK293 | ||
Clusterin, also known as complement-associated protein SP-40, Complement cytolysis inhibitor, Apolipoprotein J, Testosterone-repressed prostate message 2, Aging-associated gene 4 protein, CLU and APOJ, is a secreted protein which belongs to the clusterin family. Clusterin/Apolipoprotein J/Apo-J is an enigmatic glycoprotein with a nearly ubiquitous tissue distribution and an apparent involvement in biological processes ranging from mammary gland involution to neurodegeneration in Alzheimer's disease. Its major form, a heterodimer, is secreted and present in physiological fluids, but truncated forms targeted to the nucleus have also been identified. Clusterin/Apolipoprotein J/Apo-J is a widely distributed glycoprotein with a wide range of biologic properties. A prominent and defining feature of clusterin is its marked induction in such disease states as glomerulonephritis, cystic renal disease, renal tubular injury, neurodegenerative conditions, atherosclerosis, and myocardial infarction. Upregulation of clusterin mRNA and protein levels detected in diverse disease states and in in vitro systems have led to suggestions that it functions in membrane lipid recycling, in apoptotic cell death, and as a stress-induced secreted chaperone protein, amongst others.
|
|||||
TMPY-01694 | Clusterin Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Clusterin, also known as complement-associated protein SP-40, Complement cytolysis inhibitor, Apolipoprotein J, Testosterone-repressed prostate message 2, Aging-associated gene 4 protein, CLU and APOJ, is a secreted protein which belongs to the clusterin family. Clusterin/Apolipoprotein J/Apo-J is an enigmatic glycoprotein with a nearly ubiquitous tissue distribution and an apparent involvement in biological processes ranging from mammary gland involution to neurodegeneration in Alzheimer's disease. Its major form, a heterodimer, is secreted and present in physiological fluids, but truncated forms targeted to the nucleus have also been identified. Clusterin/Apolipoprotein J/Apo-J is a widely distributed glycoprotein with a wide range of biologic properties. A prominent and defining feature of clusterin is its marked induction in such disease states as glomerulonephritis, cystic renal disease, renal tubular injury, neurodegenerative conditions, atherosclerosis, and myocardial infarction. Upregulation of clusterin mRNA and protein levels detected in diverse disease states and in in vitro systems have led to suggestions that it functions in membrane lipid recycling, in apoptotic cell death, and as a stress-induced secreted chaperone protein, amongst others.
|
|||||
TMPY-00767 | Cystatin C Protein, Human, Recombinant (His) | Human | HEK293 | ||
Cystatin C, also known as Cystatin-3 (CST3) is a secreted type 2 cysteine protease inhibitor synthesized in all nucleated cells, has been proposed as a replacement for serum creatinine for the assessment of renal function, particularly to detect small reductions in glomerular filtration rate. The mature, active form of human cystatin C is a single non-glycosylated polypeptide chain consisting of 120 amino acid residues, with a molecular mass of 13,343-13,359 Da, and containing four characteristic disulfide-paired cysteine residues. Cystatin C is a low-molecular-weight protein that has been proposed as a marker of renal function that could replace creatinine. Indeed, the concentration of Cystatin C is mainly determined by glomerular filtration and is particularly of interest in clinical settings where the relationship between creatinine production and muscle mass impairs the clinical performance of creatinine. Since the last decade, numerous studies have evaluated its potential use in measuring renal function in various populations. More recently, other potential developments for its clinical use have emerged. In almost all the clinical studies, Cystatin C demonstrated a better diagnostic accuracy than serum creatinine in discriminating normal from impaired kidney function, but controversial results have been obtained by comparing this protein with other indices of kidney disease, especially serum creatinine-based equations, such as early atherosclerosis, Alzheimer's dementia, vascular aneurysms, hyperhomocysteinaemia and other neurodegenerative diseases. Cystatin C could be a useful clinical tool to identify HIV-infected persons. In addition, its expression is up-regulated in malignance of certain tumor progression.
|
|||||
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.
|
|||||
TMPH-01272 | TRIM9 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation.
|
|||||
TMPK-01530 | HLA-A*02:01&B2M&LMP2 (CLGGLLTMV) Monomer Protein, Human, MHC (His & Avi), Biotinylated | Human | HEK293 | ||
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of malignant tumors that highly express LMP2.
|
|||||
TMPK-01534 | Chimeric HLA-A*02:01 (mα3) &B2M&LMP2 (CLGGLLTMV) Monomer Protein, Human&Mouse, MHC (His & Avi) | Human & Mouse | HEK293 | ||
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of malignant tumors that highly express LMP2.
|
|||||
TMPK-00191 | PILRA Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Alzheimer's disease (AD) is a neurodegenerative disease characterized by a progressive decline in cognitive performance; Mild Cognitive Impairment (MCI) is instead an objective decline in cognitive performance that does not reach pathology. Paired immunoglobulin-like type 2 receptor alpha (PILRA) is a cell surface inhibitory receptor that was recently suggested to be involved in AD pathogenesis. In particular, the arginine-to-glycine substitution in position 78 (R78, rs1859788) was shown to be protective against AD.
|
|||||
TMPJ-00278 | Clusterin Protein, Human, Recombinant (hFc & His) | Human | Human Cells | ||
Clusterin is a secreted protein which belongs to the Clusterin family. Clusterin is expressed in adult testis, heart, ovary, adrenal gland, brain and liver. Clusterin has been suggested to be involved in several basic biological events such as cell death, tumor progression, and neurodegenerative disorders. In addition,Clusterin is up/ down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.
|
|||||
TMPJ-00279 | Clusterin Protein, Human, Recombinant (His) | Human | Human Cells | ||
Clusterin is a secreted protein which belongs to the Clusterin family. Clusterin is expressed in adult testis, heart, ovary, adrenal gland, brain and liver. Clusterin has been suggested to be involved in several basic biological events such as cell death, tumor progression, and neurodegenerative disorders. In addition,Clusterin is up/ down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.
|
|||||
TMPK-01502 | HLA-A*11:01&B2M&LMP2 (SSCSSCPLTK) Monomer Protein, Human, MHC (His & Avi), Biotinylated | Human | HEK293 | ||
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of malignant tumors that highly express LMP2.
|
|||||
TMPK-01535 | Chimeric HLA-A*02:01 (mα3) &B2M&LMP2 (CLGGLLTMV) Tetramer Protein, Human&Mouse, MHC (His & Avi) | Human & Mouse | HEK293 | ||
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of malignant tumors that highly express LMP2.
|
|||||
TMPY-02043 | PARK7/DJ-1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Parkinson's disease locus DJ-1 (PARK7) is a differentially expressed transcript. DJ-1 plays a physiologic role in protection of erythroid cells from oxidant damage, a function unmasked in the context of oxidative stress. PARK7 belongs to the peptidase C56 family of proteins. It acts as a positive regulator of androgen receptor-dependent transcription. It may also function as a redox-sensitive chaperone, as a sensor for oxidative stress, and it apparently protects neurons against oxidative stress and cell death. Mutations in the DJ-1 gene are associated with rare forms of autosomal recessive early-onset Parkinson's disease (PD). DJ-1/p53 interactions contribute to apoptosis resistance in clonal myeloid cells and may serve as a prognostic marker in patients with myelodysplastic syndromes (MDS). DJ-1 regulates redox signaling kinase pathways and acts as a transcriptional regulator of antioxidative gene batteries. Therefore, DJ-1 is an important redox-reactive signaling intermediate controlling oxidative stress after ischemia, upon neuroinflammation, and during age-related neurodegenerative processes. Augmenting DJ-1 activity might provide novel approaches to treating chronic neurodegenerative illnesses such as Parkinson's disease and acute damage such as stroke.
|
|||||
TMPK-01542 | HLA-A*02:01&B2M&LMP2 (CLGGLLTMV) Tetramer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of malignant tumors that highly express LMP2.
|
|||||
TMPK-01498 | HLA-A*11:01&B2M&LMP2 (SSCSSCPLTK) Tetramer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of malignant tumors that highly express LMP2.
|
|||||
TMPK-01533 | HLA-A*02:01&B2M&LMP2 (CLGGLLTMV) Monomer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of malignant tumors that highly express LMP2.
|
|||||
TMPJ-00023 | SNCA Protein, Human, Recombinant (His) | Human | E. coli | ||
Alpha-Synuclein (SNCA) is a member of the Synuclein family. SNCA is expressed principally in brain but also expressed in low concentrations in all tissues except liver. SNCA interacts with UCHL1, Phospholipase D and histones. SNCA can include beta- and gamma-synuclein. In addition, SNCA is an important regulatory component of vesicular transport in neuronal cells. It has been suggested that SNCA is related to the pathogenesis of Parkinson's Disease and neurodegenerative disorders. Defects in SNCA will lead to Dementia Lewy Body (DLB).
|
|||||
TMPJ-00683 | SNCA Protein, Mouse, Recombinant | Mouse | E. coli | ||
Alpha-Synuclein (SNCA) is a member of the Synuclein family. SNCA is expressed principally in brain but also expressed in low concentrations in all tissues except liver. SNCA interacts with UCHL1, Phospholipase D and histones. SNCA can include beta- and gamma-synuclein. In addition, SNCA is an important regulatory component of vesicular transport in neuronal cells. It has been suggested that SNCA is related to the pathogenesis of Parkinson's Disease and neurodegenerative disorders. Defects in SNCA will lead to Dementia Lewy Body (DLB).
|
|||||
TMPJ-00706 | SNCG Protein, Human, Recombinant | Human | E. coli | ||
Gamma-Synuclein (SNCG) is a member of the Synuclein protein family. Gamma-Synuclein is mostly expressed in the peripheral nervous system and retina. Gamma-Synuclein plays a role in neurofilament network integrity and may be involved in modulating axonal architecture during development and in the adult. In addition, it may also function in modulating the keratin network in skin. SNCG expression in breast tumors has been as a marker for tumor progression. SNCG is also believed to be involved in the pathogenesis of neurodegenerative diseases.
|
|||||
TMPY-00475 | PPT1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Mutations in the depalmitoylating enzyme gene, PPT1, cause the infantile form of Neuronal Ceroid Lipofuscinosis (NCL), an early onset neurodegenerative disease. Mutations in palmitoyl protein thioesterase-1 (PPT1) have been found to cause the infantile form of neuronal ceroid lipofuscinosis, which is a lysosomal storage disorder characterized by impaired degradation of fatty acid-modified proteins with accumulation of amorphous granular deposits in cortical neurons, leading to mental retardation and death. PPT1 catalyzes the cleavage of thioester linkages in S-acylated (palmitoylated) proteins and its deficiency leads to abnormal accumulation of thioesterified polypeptides (ceroid) in lysosomes causing INCL pathogenesis.
|
|||||
TMPY-04055 | PPT1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Mutations in the depalmitoylating enzyme gene, PPT1, cause the infantile form of Neuronal Ceroid Lipofuscinosis (NCL), an early onset neurodegenerative disease. Mutations in palmitoyl protein thioesterase-1 (PPT1) have been found to cause the infantile form of neuronal ceroid lipofuscinosis, which is a lysosomal storage disorder characterized by impaired degradation of fatty acid-modified proteins with accumulation of amorphous granular deposits in cortical neurons, leading to mental retardation and death. PPT1 catalyzes the cleavage of thioester linkages in S-acylated (palmitoylated) proteins and its deficiency leads to abnormal accumulation of thioesterified polypeptides (ceroid) in lysosomes causing INCL pathogenesis.
|
|||||
TMPJ-00828 | Tau-F Protein, Human, Recombinant | Human | E. coli | ||
Tau proteins are proteins which contain four Tau/MAP repeats. They promote microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. They are abundant in neurons of the central nervous system and are less common elsewhere, but are also expressed at very low levels in CNS astrocytes and oligodendrocytes. The tau proteins are the product of alternative splicing from a single gene that in humans is designated MAPT. When tau proteins are defective, and no longer stabilize microtubules properly, they can result in several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.
|
|||||
TMPK-01503 | HLA-A*11:01&B2M&LMP2 (SSCSSCPLTK) Monomer Protein, Human, MHC (His & Avi) | Human | HEK293 | ||
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of malignant tumors that highly express LMP2.
|
|||||
TMPY-03653 | CTRL Protein, Human, Recombinant (His) | Human | HEK293 | ||
CTRL-1, also known as chymotrypsin-like protease, belongs to thepeptidase S1 family. CTRL-1 contains 1peptidase S1 domain. Its expression is increased in preeclampsia (PE). Placental-derived chymotrypsin-like protease is responsible for inducing endothelial inflammatory phenotypic changes possibly by upregulation of cell adhesion molecule expressions, activation of cellular protease, and induction of extracellular regulated kinase phosphorylation. Activated microglia have been observed in various neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, and multiple sclerosis. Five structurally distinct inhibitors that are known to inhibit chymotrypsin-like proteases were partially protective. They might represent a novel class of drugs with benefit in diseases where overactivity of microglia contributes to the pathogenesis.
|
|||||
TMPJ-00761 | FTH Protein, Human, Recombinant (His) | Human | E. coli | ||
Ferritin heavy polypeptide 1(FTH1), is a ubiquitous intracellular protein which stores iron in a soluble, non-toxic, readily available form. FTH1 has ferroxidase activity and is important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Ferritin is composed of 24 subunits of the light and heavy ferritin chains. It plays a role in delivery of iron to cells and mediates iron uptake in capsule cells of the developing kidney. Variation of ferritin subunit composition may affect iron absorption and release in different tissues. Deficiency of ferritin proteins may cause several neurodegenerative diseases. Almost all living organisms can produce this protein, including algae, bacteria, higher plants, and animals.
|
|||||
TMPY-02653 | LRP-10 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
LRP10 (low-density lipoprotein Receptor Related Protein 10) is a Protein Coding gene. 2 alternatively spliced human isoforms have been reported. This gene encodes a low-density lipoprotein receptor family protein. A similar protein in mouse is thought to play a role in the uptake of apolipoprotein E-containing lipoproteins. Human LRP10 cDNA encodes a 1905 amino acid type I membrane protein consisting of five functional domains characteristic of the LDLR gene family. It is widely expressed in the esophagus, colon, and other tissues. LRP10 plays a significant role in brain physiology other than lipoprotein metabolism. It is associated with a series of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease which share genetic risk factors and pathophysiological processes with amyotrophic lateral sclerosis (ALS).
|
|||||
TMPY-02748 | LRP-10 Protein, Human, Recombinant (His) | Human | HEK293 | ||
LRP10 (low-density lipoprotein Receptor Related Protein 10) is a Protein Coding gene. 2 alternatively spliced human isoforms have been reported. This gene encodes a low-density lipoprotein receptor family protein. A similar protein in mouse is thought to play a role in the uptake of apolipoprotein E-containing lipoproteins. Human LRP10 cDNA encodes a 1905 amino acid type I membrane protein consisting of five functional domains characteristic of the LDLR gene family. It is widely expressed in the esophagus, colon, and other tissues. LRP10 plays a significant role in brain physiology other than lipoprotein metabolism. It is associated with a series of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease which share genetic risk factors and pathophysiological processes with amyotrophic lateral sclerosis (ALS).
|
|||||
TMPY-00146 | RKIP/PEBP1 Protein, Human, Recombinant | Human | E. coli | ||
Phosphatidylethanolamine-binding protein 1 (PEBP1), also known as Raf kinase inhibitor protein, belongs to PEBP family of proteins. It is known to interact with many proteins that are mainly involved in pathways that monitor cell proliferation and differentiation. PEBP1 in many cells interacts with several pathways, namely MAPK, GRK2, NF-small ka, CyrillicB, etc. that keeps the cell proliferation and differentiation in check. This protein is expressed by many cells in humans, including neurons where it is predominantly involved in production of choline acetyltransferase. Deregulated PEBP1 is known to cause cancer, diabetic nephropathy and neurodegenerative diseases like Alzheimer's and dementia.
|
|||||
TMPY-00131 | Niemann Pick C1/NPC1 Protein, Human, Recombinant (His & FLAG) | Human | HEK293 | ||
Niemann-Pick C1 (NPC1), a host receptor involved in the envelope glycoprotein (GP)-mediated entry of filoviruses into cells, is believed to be a major determinant of cell susceptibility to filovirus infection. Niemann-Pick C1 (NPC1), a membrane protein of lysosomes, is required for the export of cholesterol derived from receptor-mediated endocytosis of LDL. The NPC1 protein is a multipass transmembrane protein whose deficiency causes the autosomal recessive lipid storage disorder Niemann-Pick type C1. NPC1 localizes predominantly to late endosomes and has a dileucine motif located within a small cytoplasmic tail thought to target the protein to this location. Niemann-Pick disease type C1 (NPC1) is a rare progressive neurodegenerative disorder caused by mutations in the NPC1 gene. On the cellular level, NPC1 mutations lead to an accumulation of cholesterol and gangliosides.
|
|||||
TMPY-02196 | VAPB Protein, Human, Recombinant (His) | Human | E. coli | ||
Vesicle-associated membrane protein-associated protein B / C, also known as VAMP-B/VAMP-C, VAMP-associated protein B/C, VAP-B/VAP-C and VAPB, is a single-pass type IV membrane protein that belongs to the VAMP-associated protein (VAP) family. VAPB contains one MSP domain. VAPB may play a role in vesicle trafficking. VAPB forms a heterodimer with VAPA. VAPB interacts with VAMP1 and VAMP2. Defects in VAPB are the cause of amyotrophic lateral sclerosis type 8 ( ALS8 ) which is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Defects in VAPB are also a cause of spinal muscular atrophy autosomal dominant Finkel type (SMAF) which is characterized by proximal muscle weakness that begins in the lower limbs and then progresses to upper limbs.
|
|||||
TMPY-01675 | RAGE Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Receptor for Advanced Glycosylation End Products (RAGE, or AGER) is a member of the immunoglobulin super-family transmembrane proteins, as a signal transduction receptor which binds advanced glycation endproducts, certain members of the S100/calgranulin family of proteins, high mobility group box 1 (HMGB1), advanced oxidation protein products, and amyloid (beta-sheet fibrils). Initial studies investigating the role of RAGE in renal dysfunction focused on diabetes, neurodegenerative disorders, and inflammatory responses. However, RAGE also has roles in the pathogenesis of renal disorders that are not associated with diabetes, such as obesity-related glomerulopathy, doxorubicin-induced nephropathy, hypertensive nephropathy, lupus nephritis, renal amyloidosis, and ischemic renal injuries. RAGE represents an important factor in innate immunity against pathogens, but it also interacts with endogenous ligands, resulting in chronic inflammation. RAGE signaling has been implicated in multiple human illnesses, including atherosclerosis, arthritis, Alzheimer's disease, atherosclerosis and aging associated diseases.
|
|||||
TMPY-05215 | TPP1 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Tripeptidyl-peptidase 1 (TPP1 / CLN2) is a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. TPP1 / CLN2 may act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Defects in TPP1 / CLN2 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2), a form of neuronal ceroid lipofuscinosis which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy.
|
|||||
TMPY-01716 | RAGE Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Receptor for Advanced Glycosylation End Products (RAGE, or AGER) is a member of the immunoglobulin super-family transmembrane proteins, as a signal transduction receptor which binds advanced glycation endproducts, certain members of the S100/calgranulin family of proteins, high mobility group box 1 (HMGB1), advanced oxidation protein products, and amyloid (beta-sheet fibrils). Initial studies investigating the role of RAGE in renal dysfunction focused on diabetes, neurodegenerative disorders, and inflammatory responses. However, RAGE also has roles in the pathogenesis of renal disorders that are not associated with diabetes, such as obesity-related glomerulopathy, doxorubicin-induced nephropathy, hypertensive nephropathy, lupus nephritis, renal amyloidosis, and ischemic renal injuries. RAGE represents an important factor in innate immunity against pathogens, but it also interacts with endogenous ligands, resulting in chronic inflammation. RAGE signaling has been implicated in multiple human illnesses, including atherosclerosis, arthritis, Alzheimer's disease, atherosclerosis and aging associated diseases.
|
|||||
TMPY-01847 | REG3D Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Regenerating islet-derived 3 delta (REG3D) is a member of the secreted Reg superfamily and contains one typical C-type lectin domain. Regenerating gene (Reg), first isolated from a regenerating islet cDNA library, encodes a secretory protein with a growth stimulating effect on pancreatic beta cells. Reg and Reg-related genes which were expressed in various organs have been revealed to constitute a multigene family, the Reg family, which consists of four subtypes (types I, II, III, IV) based on the primary structures of the encoded proteins of the genes, which are associated with tissue repair and have been directly implicated in pancreatic beta-cell regeneration. Reg proteins are expressed in various organs and are involved in cancers and neurodegenerative diseases. They display a typical C-type lectin-like domain but possess additional highly conserved amino acids.
|
|||||
TMPY-02752 | SPG21 Protein, Mouse, Recombinant (His & GST) | Mouse | Baculovirus-Insect Cells | ||
Spastic paraplegia 21 (SPG21), also known as acid Cluster Protein 33 (ACP33) and Mast syndrome protein, is a member of the AB hydrolase superfamily. Human SPG21 is a 38 amino acid residue protein widely expressed in all tissues, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. SPG21 binds to the hydrophobic C-terminal amino acids of CD4 which are involved in repression of T cell activation via the noncatalytic alpha/beta hydrolase fold domain. SPG21 thus is proposed to play a role as a negative regulatory factor in CD4-dependent T-cell activation of CD4. Defects in SPG21 are the cause of spastic paraplegia autosomal recessive type 21, also known as Mast syndrome, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. SPG21 is also associated with dementia and other central nervous system abnormalities.
|
|||||
TMPY-05241 | SIRT5 Protein, Human, Recombinant (Flag) | Human | E. coli | ||
The sirtuin SIRT5 resides primarily in the mitochondrial matrix and catalyzes the removal of negatively charged lysine acyl modifications; succinyl, malonyl, and glutaryl groups SIRT5 as a significant regulator of cellular homeostasis, in a context- and cell-type specific manner, as has been observed previously for other sirtuin family members. SIRT5 regulates protein substrates involved in glycolysis, the TCA cycle, fatty acid oxidation, electron transport chain, ketone body formation, nitrogenous waste management, and ROS detoxification, among other processes. SIRT5 plays pivotal roles in cardiac physiology and stress responses and is involved in the regulation of numerous aspects of myocardial energy metabolism. SIRT5 is implicated in neoplasia, as both a tumor promoter and suppressor in a context-specific manner, and may serve a protective function in the setting of neurodegenerative disorders. The SIRT5 downregulation is associated with increased succinylation and activity of ACOX1 and oxidative DNA damage response in hepatocellular carcinoma (HCC).
|
|||||
TMPY-01057 | SPG21 Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
Spastic paraplegia 21 (SPG21), also known as acid Cluster Protein 33 (ACP33) and Mast syndrome protein, is a member of the AB hydrolase superfamily. Human SPG21 is a 38 amino acid residue protein widely expressed in all tissues, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. SPG21 binds to the hydrophobic C-terminal amino acids of CD4 which are involved in repression of T cell activation via the noncatalytic alpha/beta hydrolase fold domain. SPG21 thus is proposed to play a role as a negative regulatory factor in CD4-dependent T-cell activation of CD4. Defects in SPG21 are the cause of spastic paraplegia autosomal recessive type 21, also known as Mast syndrome, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. SPG21 is also associated with dementia and other central nervous system abnormalities.
|
|||||
TMPY-02711 | Ferritin heavy chain 1/FTH1 Protein, Human, Recombinant | Human | E. coli | ||
FTH1 (ferritin, heavy polypeptide 1) is the heavy subunit of ferritin which is the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in ferritin proteins are associated with several neurodegenerative diseases. FTH1 gene has multiple pseudogenes. Several alternatively spliced transcript variants have been observed, but their biological validity has not been determined. FTH1 stores iron in a soluble, non-toxic, readily available form. It is important for iron homeostasis. It has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. It also plays a role in delivery of iron to cells. FTH1 mediates iron uptake in capsule cells of the developing kidney.
|
|||||
TMPY-06211 | Clusterin Protein, Chinese hamster, Recombinant (His) | Chinese hamster | CHO | ||
Clusterin, also known as complement-associated protein SP-40, Complement cytolysis inhibitor, Apolipoprotein J, Testosterone-repressed prostate message 2, Aging-associated gene 4 protein, CLU and APOJ, is a secreted protein which belongs to the clusterin family. Clusterin/Apolipoprotein J/Apo-J is an enigmatic glycoprotein with a nearly ubiquitous tissue distribution and an apparent involvement in biological processes ranging from mammary gland involution to neurodegeneration in Alzheimer's disease. Its major form, a heterodimer, is secreted and present in physiological fluids, but truncated forms targeted to the nucleus have also been identified. Clusterin/Apolipoprotein J/Apo-J is a widely distributed glycoprotein with a wide range of biologic properties. A prominent and defining feature of clusterin is its marked induction in such disease states as glomerulonephritis, cystic renal disease, renal tubular injury, neurodegenerative conditions, atherosclerosis, and myocardial infarction. Upregulation of clusterin mRNA and protein levels detected in diverse disease states and in in vitro systems have led to suggestions that it functions in membrane lipid recycling, in apoptotic cell death, and as a stress-induced secreted chaperone protein, amongst others.
|
|||||
TMPY-03736 | REG1B Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
Regenerating gene (Reg), first isolated from a regenerating islet cDNA library, encodes a secretory protein with a growth stimulating effect on pancreatic beta cells, and could be associated with fibrocalculous pancreatopathy. Reg and Reg-related genes which were expressed in various organs have been revealed to constitute a multigene family, the Reg family consisting of four subtypes (types I, II, III, IV) and are involved in cancers and neurodegenerative diseases. Regenerating islet-derived 1 beta (REG1B), also known as Lithostathine-1-beta and Pancreatic stone protein 2 (PSPS2), is a types I Reg protein and contains one typical C-type lectin domain. REG1B is a 166-amino acid protein that has 22 amino acid substitutions in comparison with the previously isolated human REG1A, and it is was expressed only in pancreas. REG1B Is normally found in the exocrine pancreas, whereas in other tissues it appears either only under pathological conditions, such as Alzheimer's disease (brain), cancer (colon), or during regeneration such as neuronal sprouting in brain and pancreas regeneration. REG1B might act as an inhibitor of spontaneous calcium carbonate precipitation. The REG1A and REG1B gene and proteins could play different roles in the pancreas.
|
|||||
TMPY-06954 | SIRT5 Protein, Human, Recombinant (His) | Human | E. coli | ||
The sirtuin SIRT5 resides primarily in the mitochondrial matrix and catalyzes the removal of negatively charged lysine acyl modifications; succinyl, malonyl, and glutaryl groups SIRT5 as a significant regulator of cellular homeostasis, in a context- and cell-type specific manner, as has been observed previously for other sirtuin family members. SIRT5 regulates protein substrates involved in glycolysis, the TCA cycle, fatty acid oxidation, electron transport chain, ketone body formation, nitrogenous waste management, and ROS detoxification, among other processes. SIRT5 plays pivotal roles in cardiac physiology and stress responses and is involved in the regulation of numerous aspects of myocardial energy metabolism. SIRT5 is implicated in neoplasia, as both a tumor promoter and suppressor in a context-specific manner, and may serve a protective function in the setting of neurodegenerative disorders. The SIRT5 downregulation is associated with increased succinylation and activity of ACOX1 and oxidative DNA damage response in hepatocellular carcinoma (HCC).
|
|||||
TMPY-01596 | Butyrylcholinesterase Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Butyrylcholinesterase (BCHE), also known as cholinesterase or BuChE, is an enzyme defined as "pseudo" or "non-neuronal" cholinesterase. Butyrylcholinesterase (BCHE) is widely distributed in the nervous system as well as blood plasma. It is constitutively similar to the neuronal acetylcholinesterase, and is a non-specific cholinesterase which hydrolyses many different choline esters. Butyrylcholinesterase (BCHE) is a glycoprotein of 4 identical subunits, that were arranged as a dimer of dimers with each dimer composed of two identical subunits joined by interchain disulfide bonds. Butyrylcholinesterase (BCHE) behaves principally similar to the true enzyme and thus can play a similar role in nerve conduction, although it participates probably only in relatively slow conductive processes and could be involved in other nervous system functions and in neurodegenerative diseases. It can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents. Purified human serum cholinesterase combines in its active surface an anionic and an esteratic site, similar to true cholinesterase. It has been demonstrated that butyrylcholinesterase (BCHE) may have a greater role in cholinergic transmission than previously surmised, making BChE inhibition an important therapeutic goal in Alzheimer's disease.
|
|||||
TMPH-02178 | TARDBP Protein, Human, Recombinant | Human | E. coli | ||
RNA-binding protein that is involved in various steps of RNA biogenesis and processing. Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs. In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases. Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts. Regulates also mRNA stability by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail deadenylation and thus shortening. In response to oxidative insult, associates with stalled ribosomes localized to stress granules (SGs) and contributes to cell survival. Participates also in the normal skeletal muscle formation and regeneration, forming cytoplasmic myo-granules and binding mRNAs that encode sarcomeric proteins. Plays a role in the maintenance of the circadian clock periodicity via stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner. Negatively regulates the expression of CDK6. Regulates the expression of HDAC6, ATG7 and VCP in a PPIA/CYPA-dependent manner.
|
|||||
TMPY-01693 | Butyrylcholinesterase Protein, Human, Recombinant (His) | Human | HEK293 | ||
Butyrylcholinesterase (BCHE), also known as cholinesterase or BuChE, is an enzyme defined as "pseudo" or "non-neuronal" cholinesterase. Butyrylcholinesterase (BCHE) is widely distributed in the nervous system as well as blood plasma. It is constitutively similar to the neuronal acetylcholinesterase, and is a non-specific cholinesterase which hydrolyses many different choline esters. Butyrylcholinesterase (BCHE) is a glycoprotein of 4 identical subunits, that were arranged as a dimer of dimers with each dimer composed of two identical subunits joined by interchain disulfide bonds. Butyrylcholinesterase (BCHE) behaves principally similar to the true enzyme and thus can play a similar role in nerve conduction, although it participates probably only in relatively slow conductive processes and could be involved in other nervous system functions and in neurodegenerative diseases. It can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents. Purified human serum cholinesterase combines in its active surface an anionic and an esteratic site, similar to true cholinesterase. It has been demonstrated that butyrylcholinesterase (BCHE) may have a greater role in cholinergic transmission than previously surmised, making BChE inhibition an important therapeutic goal in Alzheimer's disease.
|