抗体来源 Mouse
克隆类型 polyclonal
交叉反应 Human, Mouse, Rat, Chicken, Dog, Pig, Cow, Rabbit
产品类型 一抗
研究领域
蛋白分子量 predicted molecular weight: 4.4kDa
性 状 Lyophilized or Liquid
免 疫 原 KLH conjugated synthetic peptide of human beta-Amyloid(1-28)
亚 型 IgG
纯化方法 affinity purified by Protein A
储 存 液 0.01M PBS, pH 7.4 with 10 mg/ml BSA and 0.1% Sodium azide
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（1-28）抗体产品介绍 The cerebral and vascular plaques associated with Alzheimer's disease (AD) are mainly composed of amyloid beta peptides (Ab). Ab is derived from cleavage of the amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. Ab [1-40], Ab [1-42], and Ab [1-43] peptides result from cleavage of APP after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last APP processing step. Ab [1-40], [1-42] and [1-43] peptides are major constituents of the plaques and tangles that occur in AD. Ab antibodies and peptides have been developed as tools for elucidating the biology of AD.
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
纯度：在实验的任何阶段，确定抗体溶液纯度的最简单方法是取一部分样本进行SDS-PAGE电泳。凝胶可用考马斯亮蓝染色(灵敏度为0.1—0.5ug/带)或银染(灵敏度1～l0ug/带)。
定量：如果抗体还不纯，有一个快捷的定量方法，即通过SDS-PAGE电泳分离出轻、重链，然后和已知的标准染色带比较。如果需要分析许多样本，用免疫测定法对抗体定量较容易。如果抗体是经过纯化的，可通过测蛋白总量代替上述两种方法，有一简单的方法，即紫外吸收法。β淀粉样肽（1-28）抗体的量可通过测280nm处的吸收值来测(10D大致相当于0.75mg/m1的纯化抗体)。
抗原结合活性：一般说来，纯化方法不会引起抗原结合活性的改变。用蛋白G或蛋白A树脂很少导致抗体活性丧失。然而，如果最终抗体产物的作用不如原来所预料的好，检测抗体纯化过程所丢失的活性就极为重要。用一系列滴定法比较纯化的抗体和其原材料的活性，以标定每一步中的总抗体量，这将有助于较好的估计通过纯化所丢失的活性。
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