目录号 | 产品详情 | 靶点 | |
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TP1229 | Beta Amyloid | ||
β-Amyloid (1-15) (Amyloid β-Protein (1-15)) 是 β-淀粉样蛋白片段,可用于研究阿尔茨海默病。 | |||
T7562 | Beta Amyloid | ||
β-Amyloid (31-35) (β-Amyloid 31-35) 是一种天然 Amyloid-β 肽的最短序列,具有神经毒性。 | |||
T14284 | Beta Amyloid | ||
β-Amyloid (25-35) (Aβ25-35) 是一种阿尔茨海默氏淀粉样蛋白β肽的Aβ(25-35) 片段,在培养细胞中显示出神经毒性作用。 | |||
TP1214L | Beta Amyloid | ||
β-Amyloid 15-21 acetate (Beta-Amyloid(15-21) acetate) 是 Amyloid-β 肽的片段,可用于神经系统疾病的研究。该片段参与β折叠形成。 | |||
TP1359L | Beta Amyloid | ||
Amyloid β Peptide (42-1)(human) acetate 是淀粉样蛋白 β 肽 (1-42) 的无活性形式。Amyloid β Peptide (42-1)(human) acetate 是由 42 个氨基酸组成的肽,其在阿尔茨海默病的发病机制中起关键作用。 | |||
TP1786L | Beta Amyloid | ||
Amyloid β-Protein 10-20 acetate (Amyloid β-Protein 10-20 acetate (152286-31-2 free base)) 是 Amyloid-β 肽的片段,可能用于神经系统疾病的研究。Amyloid β 蛋白片段含有 α-分泌酶加工位点(Lys16-Leu17 键)。它还包含负责与小胶质细胞结合的 HHQK 结构域(残基 13-16)。 | |||
T35499 | |||
β-Amyloid (1-42), (rat/mouse) (TFA) 是由 42 个氨基酸组成的多肽片段,可用于研究阿尔茨海默症。 | |||
TP1007L | |||
β-Amyloid (1-42), acetate (human) 是由 42 个氨基酸组成的肽,是 β-Amyloid 的一部分,常用于阿尔茨海默病造模。 | |||
TP1866L | Beta Amyloid | ||
β-amyloid 1-11 acetate(190436-05-6 free base) 是 Amyloid-β 肽的片段,可用于神经系统疾病的研究。 | |||
T21890 | Gamma-secretase | ||
JLK-6 是一种γ分泌酶抑制剂,选择性作用于 HEK293细胞的淀粉样β前体蛋白(APP)的γ-分泌酶裂解 APP,抑制 Aβ的生成,但对不 Notch 受体的裂解无影响。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-04693 | APLP1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
APLP1, also known as amyloid-like protein 1, is a member of the highly conserved amyloid precursor protein gene family. APLP1 is a membrane-associated glycoprotein that is cleaved by secretases in a manner similar to amyloid beta A4 precursor protein cleavage. APLP1, together with APLP2, are important modulators of glucose. APLP1 may also play a role in synaptic maturation during cortical development. Alternatively spliced transcript variants encoding different isoforms have been described. APLP1 also is a mammalian homologue of amyloid precursor protein (APP). APP is a type I membrane protein that is genetically linked to Alzheimer's disease.
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TMPY-03628 | APLP1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
APLP1, also known as amyloid-like protein 1, is a member of the highly conserved amyloid precursor protein gene family. APLP1 is a membrane-associated glycoprotein that is cleaved by secretases in a manner similar to amyloid beta A4 precursor protein cleavage. APLP1, together with APLP2, are important modulators of glucose. APLP1 may also play a role in synaptic maturation during cortical development. Alternatively spliced transcript variants encoding different isoforms have been described. APLP1 also is a mammalian homologue of amyloid precursor protein (APP). APP is a type I membrane protein that is genetically linked to Alzheimer's disease.
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TMPY-03884 | Beta-amyloid 39/Beta-APP39 Protein, Human, Recombinant (aa 672-710, His & GST) | Human | E. coli | ||
Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli.
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TMPY-02221 | Beta-amyloid 42/Beta-APP42 Protein, Human, Recombinant (His & GST) | Human | E. coli | ||
Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli.
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TMPY-02110 | Beta-amyloid 40/Beta-APP40 Protein, Human, Recombinant (His & GST) | Human | E. coli | ||
Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli.
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TMPY-03885 | Beta-amyloid 38/Beta-APP38 Protein, Human, Recombinant (aa 672-709, His & GST) | Human | E. coli | ||
Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli.
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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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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).
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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).
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TMPY-00668 | APP/Protease nexin-II Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli.
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TMPJ-00338 | LRRC15 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | Human Cells | ||
The type I transmembrane protein 15-leucine-rich repeat containing membrane protein (LRRC15) is a member of the LRR superfamily. The LRR family is a structural module for protein-protein and protein-matrix interactions used for molecular recognition process such as cell adhesion, signal transduction, DNA repair, and RNA processing. The LRRC15 is also a transmembrane protein demonstrated to play important roles in cancer. LRRC15 expression was notably increased 4.6-fold in cariesdiseased pulpal tissue. Remarkably, LRRC15 was relatively abundant in mineralized tissues. That LRRC15 was significantly induced after osteogenic differentiation, while in the MSCs from bone marrow of ovariectomized mice the expression of LRRC15 was remarkably decreased and LRRC15 regulated osteogenic differentiation in a p65-dependent manner.
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TMPJ-00722 | APBA3 Protein, Human, Recombinant (His) | Human | E. coli | ||
Amyloid β A4 Precursor Protein-Binding Family A Member 3 (APBA3) is an adapter protein that belongs to the X11 family. APBA3 contains 2 PDZ (DHR) domains and 1 PID domain and interacts with the Alzheimer's disease amyloid precursor protein.. APBA3 is believed to be involved in signal transduction processes. Unlike X11-α and -β which are generally neuronal proteins, APBA3 is widely expressed in all tissues examined with lower levels in brain and testis. It binds to the cytoplasmic domain of amyloid protein (APP) in vivo and may modulate processing of the β-amyloid precursor protein (APP) and hence formation of β-APP.
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TMPJ-00851 | IDE Protein, Human, Recombinant (His) | Human | Human Cells | ||
Insulin-Degrading Enzyme (IDE) is a secreted enzyme that belongs to the peptidase M16 family. IDE is a large zinc-binding protease and cleaves multiple short polypeptides that vary considerably in sequence. IDE plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling. IDE degrades amyloid formed by APP and IAPP. IDE may participate in the degradation and clearance of naturally secreted amyloid β-protein by neurons and microglia. IDE, which migrates at 110 kDa during gel electrophoresis under denaturing conditions, has since been shown to have additional substrates, including the signaling peptides glucagon, TGF α and β-endorphin.
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TMPK-00935 | APLP2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Amyloid β precursor-like protein 2 (APLP2) has been determined to serve an important role in the progression of a number of cancer types. APLP2 expression was significantly associated with disease-specific survival (P<0.001). APLP2 may be used to potentially predict patient prognosis, and to guide clinical diagnosis and treatment in CCRCC.
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TMPK-00998 | SEZ6 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface.
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TMPK-01065 | SEZ6 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface.
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TMPK-00997 | SEZ6 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface.
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TMPK-00996 | SEZ6 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface.
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TMPK-00541 | SEZ6 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Seizure-related protein 6 (Sez6) contributes to chronic pain development as sez6 knockout mice show attenuated pain behaviours after peripheral nerve injury, compared with control mice. The type I transmembrane isoform of Sez6 is cleaved by the β-amyloid precursor protein cleavage enzyme 1 (BACE1), resulting in Sez6 extracellular domain shedding from the neuron surface.
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TMPK-01146 | LGMN Protein, Human, Recombinant (His) | Human | HEK293 | ||
Recently, functional studies have demonstrated that legumain (LGMN) cleaves both amyloid β-protein precursor and tau, promoting senile plaques and formation of neurofibrillary tangles, which may play a crucial role in the pathogenesis of Alzheimer's disease (AD). In single-variant association analysis, none of the common variants in LGMN were statistically significant. In gene-based analysis, the LGMN gene also showed no association with AD.
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TMPY-03065 | BACE2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
BACE2, also known as beta secretase 2, belongs to the peptidase A1 family. It is a protease known to be an important enzyme involved in the cellular pathways. BACE2 has been shown to interact with GGA1 and GGA2. It is the major β-secretase in vivo. BACE2 is located on chromosome 21 and may play a role in alzheimer's disease pathogenesis in down syndrome(DS). Overexpression of BACE2 by lentivirus markedly reduced amyloid β protein production in primary neurons. Despite an extra copy of the BACE2 gene in DS and the increase of its transcription, BACE2 protein levels are unchanged.
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TMPJ-01235 | B2M/beta 2-Microglobulin Protein, Cynomolgus, Recombinant (hFc) | Cynomolgus | Human Cells | ||
β-2-Microglobulin (B2M) is a secreted protein with 1 Ig-like C1-type (immunoglobulin-like) domain which belongs to the beta-2-microglobulin family. B2M component of major histocompatibility complex (MHC) class I molecules, involved in the presentation of peptide antigens to the immune system. Polymers of beta 2-microglobulin can be found in tissues from patients on long-term hemodialysis. B2M is a protein found on the surface of many cells and plentiful on the surface of white blood cells. Serum B2M concentration is increased in renal diseases, various malignant diseases and some inflammatory and autoimmune disorders. B2M may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. B2M has been shown as a marker for monitoring inflammatory disease activity and it appears likely to have a destructive role in amyloidosis-related arthritis. B2M might be involved in the OA (osteoarthritis) pathogenesis. Defects in B2M are the cause of hypercatabolic hypoproteinemia. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation. B2M could be a potential therapeutic target in ovarian cancer.
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TMPJ-01236 | B2M/beta 2-Microglobulin Protein, Cynomolgus, Recombinant (aa 21-119, His) | Cynomolgus | Human Cells | ||
β-2-Microglobulin (B2M) is a secreted protein with 1 Ig-like C1-type (immunoglobulin-like) domain which belongs to the beta-2-microglobulin family. B2M component of major histocompatibility complex (MHC) class I molecules, involved in the presentation of peptide antigens to the immune system. Polymers of beta 2-microglobulin can be found in tissues from patients on long-term hemodialysis. B2M is a protein found on the surface of many cells and plentiful on the surface of white blood cells. Serum B2M concentration is increased in renal diseases, various malignant diseases and some inflammatory and autoimmune disorders. B2M may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. B2M has been shown as a marker for monitoring inflammatory disease activity and it appears likely to have a destructive role in amyloidosis-related arthritis. B2M might be involved in the OA (osteoarthritis) pathogenesis. Defects in B2M are the cause of hypercatabolic hypoproteinemia. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation. B2M could be a potential therapeutic target in ovarian cancer.
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TMPJ-00292 | CD36 Protein, Human, Recombinant (hFc) | Human | Human Cells | ||
Platelet Glycoprotein 4 (CD36) is an integral membrane glycoprotein that has multiple physiological functions. It is broadly expressed on a variety of cell types including microvascular endothelium, adipocytes, skeletal muscle, epithelial cells of the retina, breast, and intestine, smooth muscle cells, erythroid precursors, platelets, megakaryocytes, dendritic cells, monocytes/macrophages, and microglia. As a member of the scavenger receptor family, CD36 is a multiligand pattern recognition receptor that interacts with a large number of structurally dissimilar ligands, including long chain fatty acid (LCFA), advanced glycation end products (AGE), thrombospondin-1,oxidized lowdensity lipoproteins (oxLDLs), high density lipoprotein (HDL), phosphatidylserine, apoptotic cells, β amyloid fibrils (fAβ), collagens I and IV, and Plasmodium falciparuminfected erythrocytes. CD36 is required for the antiangiogenic effects of thrombospondin-1 in the corneal neovascularization assay. It plays a role in lipid metabolism and has been identified as a fatty acid translocase necessary for the binding and transport of LCFA in cells and tissues.
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