您好,欢迎访问仪器信息网
注册
上海基免实业有限公司

关注

已关注

已认证

粉丝量 0

当前位置: 上海基免 > 抗体/抗原 > β淀粉样肽/Aβ42抗体

β淀粉样肽/Aβ42抗体

供货周期: 7天
品牌:
型号: 0.2ml/200μg
货号:
报价: ¥1
留言咨询
产品介绍
β淀粉样肽/Aβ42抗体勿使用无霜冷冻箱,因为会冷冻循环,这样会损伤抗体。
英文名称  Anti-beta-Amyloid 1-42(CT) 
中文名称  β淀粉样肽/Aβ42抗体  
别    名  beta Amyloid(1-42); beta Amyloid 1-42; beta-Amyloid 1-42; Amyloid 1-42; beta-Amyloid 42; A4; AAA; ABETA; ABPP; AD1; Alzheimers Disease Amyloid Protein; Amyloid B; Amyloid Beta A4 Protein Precursor; Amyloid Beta; Amyloid of Aging and Alzheimer Disease; APP; APPI; B Amyloid; Beta APP; Cerebral Vascular Amyloid Peptide; CTFgamma; CVAP; PN II; PN2; PreA4; Protease nexin II; A beta; A4_HUMAN. 
浓    度  1mg/1ml 
规 格  0.1ml/100μg  0.2ml/200μg 
抗体来源  Rabbit  
β淀粉样肽/Aβ42抗体克隆类型  polyclonal 
交叉反应  Human, Mouse, Rat, Dog, Pig, Cow, Horse, Rabbit  
产品类型  一抗    
研究领域  细胞生物 免疫学 神经生物学  
蛋白分子量  predicted molecular weight: 4.3kDa 
性    状  Lyophilized or Liquid 
免 疫 原  KLH conjugated synthetic peptide derived from human beta-Amyloid(35-42) 
亚    型  IgG 
纯化方法  affinity purified by Protein A 
储 存 液  Preservative: 15mM Sodium Azide, Constituents: 1% BSA, 0.01M PBS, pH 7.4 
产品应用   WB=1:100-500  ELISA=1:500-1000  IP=1:20-100  IHC-P=1:100-500  IHC-F=1:100-500  IF=1:100-500 
(石蜡切片需做抗原修复) 
 not yet tested in other applications.
 optimal dilutions/concentrations should be determined by the end user.  
保存条件  Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. 
Important Note  This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. 
β淀粉样肽/Aβ42抗体产品介绍 The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid antibodies and peptides have been developed as tools for elucidating the biology of Alzheimer's disease. 
Function : Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. 
Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity. 
Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brai. 
The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. 
N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).
Subunit : Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and, NUMB and DAB. Binding to DAB1 inhibits its serine phosphorylation (By similarity). Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. Soluble APP binds, via its N-terminal head, to FBLN1. Interacts with CPEB1 and AGER. Interacts with ANKS1B and TNFRSF21. Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; this is promoted by heparin binding.
Subcellular Location : Membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit. Note=Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Gamma-CTF(59) peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Beta-APP42 associates with FRPL1 at the cell surface and the complex is then rapidly internalized. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment.
Tissue Specificity : Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex-opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression found in the striate, extra-striate and motor cortices. Expressed in cerebrospinal fluid, and plasma. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Appican is expressed in astrocytes.
Post-translational modifications : Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). 
Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-6, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of beta-amyloid peptides. 
N- and O-glycosylated. O-linkage of chondroitin sulfate to the L-APP isoforms produces the APP proteoglycan core proteins, the appicans. The chondroitin sulfate chain of appicans contains 4-O-sulfated galactose in the linkage region and chondroitin sulfate E in the repeated disaccharide region. 
Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin. 
Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. In vitro, the APP-Cu(+) complex in the presence of hydrogen peroxide results in an increased production of beta-amyloid-containing peptides. 
Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). 
Beta-amyloid peptides are degraded by IDE.
DISEASE : Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:104300]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. 
Defects in APP are the cause of amyloidosis cerebroarterial Dutch type (AMYLCAD) [MIM:605714]; also known as hereditary cerebral hemorrhage with amyloidosis Dutch type (HCHWAD). AMYLCAD is a hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. Beta-APP40 is the predominant form of cerebrovascular amyloid. Amyloid is not found outside the nervous system. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Onset of the disease is in middle age (44 to 60 years). Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease. 
Defects in APP are the cause of amyloidosis cerebroarterial Italian type (AMYLCAIT) [MIM:605714]. AMYLCAIT is a hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels, resulting in cerebral amyloid angiopathy. Amyloid is not found outside the nervous system. It is a condition very similar to AMYLCAD, but the clinical course is less severe. Patients manifest mild cognitive decline, recurrent strokes, and epilepsy in some cases. There are extensive amyloid deposits in leptomeningeal and cortical vessels and, to a lesser extent, in the neuropil of the cerebral cortex, in the absence of neurofibrillary tangles. 
Defects in APP are the cause of amyloidosis cerebroarterial Iowa type (AMYLCAIW) [MIM:605714]. AMYLCAIW is a hereditary amyloidosis due to amyloid-beta A4 peptide(s) deposition. Patients have progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.
Similarity : Belongs to the APP family. 
Contains 1 BPTI/Kunitz inhibitor domain.
Database links : UniProtKB/Swiss-Prot: P05067.3
Entrez Gene: 351 Human 
Entrez Gene: 11820 Mouse
Entrez Gene: 54226 Rat
Omim: 104760 Human
我们应该如何储存抗体且最大限度地提高保质期,简单地说:
抗体应在(-20℃)中冷冻干燥或浓缩的液体形式,直到需要,避免反复冷冻/解冻周期,降低抗体含量和浓度。相反,冻结在单次使用的等分试样重组抗体或添加防冻剂(甘油或乙二醇),从而使料液可以保持在-20℃下为液体形式,以使移液没有“解冻”。
在4℃下存放,避免抗体(或其他蛋白质溶液)超过几天浓缩存量(> 0.5毫克)通常是稳定的,β淀粉样肽/Aβ42抗体微生物添加剂,如叠氮化钠。不要试图保存稀释(<0.1mg/ml时)抗体溶液稳定,除非通过添加“载体”蛋白质或特殊添加剂。
工商信息

企业名称

上海基免实业有限公司

企业信息已认证

企业类型

信用代码

310116002801941

成立日期

2013-03-11

注册资本

10

经营范围

联系方式
β淀粉样肽/Aβ42抗体由上海基免实业有限公司为您提供,货号,规格:0.2ml/200μg ,CAS号:,如您想了解更多关于β淀粉样肽/Aβ42抗体价格、β淀粉样肽/Aβ42抗体结构式、批发、用途等信息,欢迎咨询。除供应β淀粉样肽/Aβ42抗体外,还可为您提供昆虫蜕皮激素(Ecdysone)检测试剂盒、T-2毒素(T-2toxin)检测试剂盒、植物N-甲基腐胺氧化酶(MPO)检测试剂盒等试剂,公司有专业的客户服务团队,是您值得信赖的合作伙伴,上海基免客户服务电话,售前、售后均可联系。
推荐产品
供应产品
相关品类

上海基免实业有限公司

沟通底价

提交后,商家将派代表为您专人服务

获取验证码

{{maxedution}}s后重新发送

获取多家报价,选型效率提升30%
提交留言
点击提交代表您同意 《用户服务协议》 《隐私政策》 且同意关注厂商展位
联系方式:

公司名称: 上海基免实业有限公司

公司地址: 上海市金山工业区亭卫公路6558号9幢2441室 联系人: 肖菊芳 邮编: 201507

仪器信息网APP

展位手机站