世界*实验材料供应商phosphosolutions正式上海金畔为其中国代理，phosphosolutions在一直是行业的*,一直为广大科研客户提供zui为的产品和服务,上海金畔一直秉承为中国科研客户带来的产品，的服务， phosphosolutions就是为了给广大科研客户带来更加完善的产品和服务,您的满意将是我们zui大的收获

phosphosolutions中国代理，phosphosolutions上海代理，phosphosolutions北京代理，phosphosolutions广东代理，phosphosolutions江苏代理 phosphosolutions湖北代理, phosphosolutions天津, phosphosolutions黑龙江代理, phosphosolutions内蒙古代理, phosphosolutions吉林代理, phosphosolutions福建代理, phosphosolutions江苏代理, phosphosolutions浙江代理, phosphosolutions四川代理,

我们公司zui大优势是强大的采购，

1：基本什么都能进口，血清，抗体，耗材，还有部分限制进口的，

2： 货品全，现经营过700多个品牌，基本所有生物试剂耗材都可以进口，特别是冷偏的产品那就更有优势，

3：提供加急服务，一般1-2周到货，超过时限加急费全免

4：价格公道，绝大部分价格有优势，当然不能保证100%产品都是,因为意味着没有服务.

5：良好的信誉，大部分客户我们提供货到付款服务，客户包括清华，北大 交大 复旦，中山等100多所大学，ROCHE，阿斯利康，国药 ，fisher等500多家公司

6：我们还是santa,Advanced Biotechnologies Inc;Athens Research & Technology, bangs, BBInternational, crystalchem, dianova, FD Neurotechnologies, Inc. FormuMax Scientific, Inc; Genebridege; Glycotope Biotechnology GmbH; iduron; Innovative Research of America； Ludger ； neuroprobe; omicronbio; Polysciences; prospecbi; QA-BIO；quickzyme；RESEARCH DIETS, INC；sterlitech；sysy；TriLink BioTechnologies, Inc；worthington-biochem;zyagen;……几十家国外公司代理

7：我们还从事invitrogen，qiagen; abcam ;sigma;neb; roche;merck; rnd; BD; GE; pierce; BioLegend….等*批发

PhosphoSolutions 是您在科罗拉多州丹佛市制造和测试的 Work™ 神经科学抗体的来源。我们是一支敬业、友好、勤奋的科学家团队，致力于为您提供业内最高质量的抗体和客户支持。

phosphosolutions 125-ACT说明书

抗肌动蛋白抗体

SKU：125-ACT

Anti-Actin Antibody (C4)

 PhosphoSolutions 的抗肌动蛋白一抗是小鼠单克隆抗体。它检测所有已知物种的肌动蛋白并且是腹水。它非常适合用于 WB、IHC、ICC。

产品详情

Phosphosolutions产品代理信息

详细介绍

产品咨询

 公司概况

背景

基因工程– Phosphosolutions是*代可以完整描绘人体的遗传物质序列的企业。

蛋白质体学项目：Phosphosolutions是第二代试图将所有体内蛋白质表达出来的企业。

PhosphoSolutions公司—第三步我们将超越蛋白质体学 进而 专注于磷蛋白质。

our focus 专业特色

PhosphoSolutions公司专注于蛋白质组学中的一个（10-20%）含量的小部分磷蛋白质。磷蛋白是监管控制组蛋白质的关键,这一部分是被称为phosphosome蛋白质。磷蛋白被认为是在神经系统疾病如老年痴呆症和癌症方面的关键元素，实质上,phosphosome是蛋白质组学作物的精华。

公司目标

简明概述：我们要成为世界上的磷蛋白组的提供者。

方案#1， 特异性磷抗体：首先我们要准备磷蛋白组。在激活或磷酸化状态下磷蛋白组是蛋白质识别研究中的*关键工具。

Antibodies 抗体

特异性磷抗体：Detection and quantitation of changes in the state of phosphorylation of specific proteins is of great utility in the quest to establish the function of a given protein and the consequences of its reversible phosphorylation. Two methods commonly used to measure protein phosphorylation and dephosphorylation in cell preparations employ prelabeling with 32Pi or back phosphorylation. These methods continue to be very effective and have advantages for many test systems, but they do have several practical and theoretical limitations （Nestler and Greengard, 1984）. Based in large part on the successful use of short synthetic peptides to produce epitope-targeted antibodies （Lerner, 1982;Sutcliffe et al., 1983）, an immunochemical approach became an attractive alternative for detecting changes in the state of phosphorylation of specific proteins at a specific site. The use of phosphorylation state-specific antibodies takes advantage of the sensitivity and selectivity afforded by immunochemical methodology, combined with relatively simple preparation and potentially broad applications.

The first report of phosphorylation-dependent antibodies appeared in 1981, when polyclonal antibodies that could detect phosphotyrosine-containing proteins were produced by immunization with benzyl phosphonate conjugated to keyhole limpet hemocyanin （KLH） （Ross et al., 1981）. Shortly thereafter, Nairn and colleagues reported the production of serum antibodies that distinguished between the phospho- and dephospho-forms of G-substrate, a protein localized to cerebellar Purkinje cells and phosphorylated by cGMP-dependent protein kinase （Nairn et al., 1982）. A synthetic heptapeptide, Arg-Lys-Asp-Thr-Pro-Ala-Leu, corresponding to a repeated sequence surrounding two phosphorylated threonyl residues in the intact protein, served as antigen. Rabbit antisera against a peptide-KLH conjugate were specific for the dephospho-form of G-substrate. Phospho-specific antibodies were prepared by immunization of rabbits with the purified phosphoprotein, phosphorylated in vitro to a stoichiometry of 2 mol/mol with cGMP-dependent protein kinase. Despite this initial success, other attempts in our laboratory to produce phospho-specific polyclonal antisera by immunization with the phospho-form of intact proteins were not very successful, probably because of two significant factors. First, many phosphorylated proteins are believed to undergo rapid dephosphorylation during immunization, regardless of the route of injection, leading to the loss of the desired phospho-epitope. Second, holoproteins generally contain multiple immunogenic epitopes; this decreases the probability that colonal dominance for a phospho-specific epitope will be obtained.

Taking a more direct approach utilizing phosphorylated and unphosphorylated forms of synthetic phosphopeptides, we developed a general protocol for the production of phosphorylation state-specific antibodies for substrates with established site（s） of phosphorylation （Czernik et al., 1991））. In early stages of our development of this methodology, phosphopeptides were routinely prepared by enzymatic phosphorylation （Czernik et al., 1991）. Although this approach remains perfectly valid today, the preparation of synthetic phosphopeptides using Fmoc derivatives of phosphoamino acids has become the state-of-the-art （Czernik et al., 1995;Czernik et al., 1996）. Likewise, we have examined the use of both polyclonal and monoclonal techniques for antibody production. Given the high success rate that we and others have obtained with the polyclonal technique, it has become the method of choice, because it is an easier and less costly method for the average laboratory. However, when appropriate, this approach can be readily adapted for monoclonal antibody production.

参考文献

1. Czernik AJ, Girault J-A, Nairn AC, Chen J, Snyder G, Kebabian J, Greengard P （1991） Production of phosphorylation state-specific antibodies. Methods Enzymol 201: 264-283.

2. Czernik AJ, Mathers J, Mische SM （1997） Phosphorylation state-specific antibodies. Neuromethods: Regulatory Protein Modification: Techniques & Protocols 30: 219-250.

3. Czernik AJ, Mathers J, Tsou K, Greengard P, Mische SM （1995） Phosphorylation state-specific antibodies: preparation and applications. Neuroprotocols 6: 56-61.

4. Lerner, R. A. Tapping the immunological repertoire to produce antibodies of predetermined specificity. Nature 299, 593-596. 1982.

5. Nairn AC, Detre JA, Casnellie JE, Greengard P （1982） Serum antibodies that distinguish between the phospho- and dephospho-forms of a phosphoprotein. Nature （Lond ） 299: 734-736.

6. Nestler, E. J. and Greengard, P. Protein Phosphorylation in the Nervous System. Nestler and Greengard. Protein Phosphorylation in the Nervous System. [8], 255-299. 1984. New York, Wiley. 

8. Sutcliffe JG, Shinnick TM, Green N, Lerner RA （1983） Antibodies that react with predetermined sites on proteins. Science 219: 660-666.

主营产品清单如下：