Anti-Supervillin抗体，监理蛋白抗体
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Anti-Supervillin抗体，监理蛋白抗体上海安研生物的理念是：为您提供性价比高的产品和全方位的服务。公司能够及时解决和满足客户的各方面的需求，与国内多家企业建立了良好的长期合作关系，在市场上树立了公司的良好信誉和形象。上海安研商贸有限公司，是专业经营生化试剂，抗体，细胞，培养基，试剂盒，染色液的公司，在广大用户的帮助和支持下，经过不懈的努力，已成为国内生命科学领域产品的主要供应商之一，代理许多国际先进水平的高科技产品，包括分子生物学、细胞生物学、免疫学、诊断等多个研究及应用领域。公司的服务和业务网络遍及全国，在同行获得一致好评。本公司备有上万种产品！所有生化试剂产品都具有类似以下产品价格绝对优势，质量保证!欢迎新老客户垂询！1.一抗及标记一抗抗体 &2.二抗及标记二抗抗体& 3.蛋白及抗原&&4.人Elisa试剂盒& 5.小鼠Elisa试剂盒&6.大鼠Elisa试剂盒& 7.豚鼠Elisa试剂盒 &8.猪Elisa试剂盒 &9.鸡Elisa试剂盒 &10.各种动物Elisa试剂盒& 11.植物Elisa试剂盒 &12.微生物Elisa试剂盒 &13.分离试剂& 14.酶与辅酶& 15.蛋白质 &16.抗生素& 17.放免试剂盒 &18.各种动物细胞株、细胞系..... &等等公司产品经无数次市场验证，若出现质量问题可无条件换货或退货。抗体中英文名称：Anti-Supervillin抗体，监理蛋白抗体抗体的相关标记：HRP,Biotin,Gold,RBITC,AP,FITC,Cy3,Cy5,Cy5.5,Cy7,PE,PE-Cy3,PE-Cy5,PE-Cy5.5,PE-Cy7,APC,Alexa&Fluor&350,Alexa&Fluor&488,Alexa&Fluor&555,Alexa&Fluor&647抗体种属有兔抗单克隆抗体，鼠抗单克隆抗体。抗体的浓度为1mg/ml。抗体可以与人，小鼠，大鼠，鸡&，狗，猪，羊，牛，兔等交叉反应。抗体可以用于做石蜡切片免疫组化，冰冻切片免疫组化，Elisa，WB，免疫荧光等实验。（公司备有抗体及以下抗体做免疫组化与WB所需的二抗）1、Western Blotting (starting dilution 1:200, dilution range1:100-1:1000)2、Immunoprecipitation [1-2 &g per 100-500 &g of total protein(1 ml ofcell lysate)]3、Immunofluorescence (starting dilution 1:50, dilution&range 1:50-1:500)4、ELISA (starting dilution 1:30, dilution&range 1:30-1:3000)5、Immunohistochemistry(including paraffin-embedded&sections) (starting dilution 1:50& & &dilution range 1:50-1:500)Anti-Supervillin抗体，监理蛋白抗体产品试验中的显色反应：免疫组化实验是利用抗原与抗体特异性结合的原理，通过化学反应使标记抗体的显色剂 (荧光素、酶、金属离子、同位素) 显色来确定组织细胞内抗原(多肽和蛋白质)，对其进行定位、定性及定量的研究。免疫组化实验中常用的抗体为单克隆抗体和多克隆抗体。单克隆抗体是一个B淋巴细胞克隆分泌的抗体，应用细胞融合杂交瘤技术免疫动物制备。多克隆抗体是将纯化后的抗原直接免疫动物后，从动物血中所获得的免疫血清，是多个B淋巴细胞克隆所产生的抗体混合物。显色反应（注：二抗一般有两种常用标记酶，HRP和AP，其相对应的显色底物试剂盒为DAB和BCIP/NBT，裂解液一般用发光法。）HRP标记二抗显色，&用DAB&KIT（KPL&LOT&NO&YM107&CAT：54-10-00）显色，按顺序依次加Tris&Buffer&3滴，DAB&Substrate&3滴,Peroxide&solution&2滴于5ml蒸馏水中，避光，混匀，将膜加入显色液中避光显色15&min左右终止反应，记录实验结果，将NC膜晾干扫描保存。AKP标记二抗显色，用AKP缓冲液洗膜5min，弃去AP缓冲液，加入显色液（66&lNBT溶液同10mlAKP缓冲液充分混合均匀后加入33&l&BCIP溶液1h内使用），室温下显色（37℃可加速反应），显色反应通常在30min内可完成。用20mM&EDTA/TBS洗膜终止反应,记录实验结果，将NC膜晾干扫描保存。反应溶液可预先配置，可在4℃储存一年以上。Anti-Supervillin抗体，监理蛋白抗体产品WB实验中的对照系统：Western&bloting首先是要将电泳后分离的蛋白从凝胶中转移到NC膜上，通常有两种方法：毛细管印迹法和电泳印迹法。&Western&bloting是用来对蛋白质进行检测的一种常用方法，通过抗原抗体的免疫反应可以定量测出抗体的相对分子量，以及抗体的相对丰度或与已知抗原的关系等等。目前它应用在多个领域,在临床上检测传染病和自身免疫病、过敏症等，在抗体生产领域它与ELISA、ICC、IHC、IFA等免疫技术相接合已成为单克隆抗体生产的主要筛选手段。毛细管印迹法是将凝胶放在缓冲液浸湿的滤纸上，在凝胶上放一片NC膜，再在上面放一层滤纸等吸水物质并用重物压好，缓冲液就会通过毛细作用流过凝胶。缓冲液通过凝胶时会将蛋白质带到NC膜上，NC膜可以与蛋白质通过疏水作用产生不可逆的结合。电泳印迹法是用有孔的塑料和有机玻璃板将凝胶和NC膜夹成&三明治&形状，而后浸入两个平行电极中间的缓冲液中进行电泳，选择适当的电泳方向就可以使蛋白质在电场力的作用下离开凝胶结合到NC膜上。常用的电泳转移方法有湿转和半干转。两者的原理完全相同，只是用于固定胶/膜叠层和施加电场的机械装置不同。WB对照系统阳性对照：最好有标准品，或阳性血清、阳性上清。阴性对照：测血时用相应小鼠未免疫血清，测培养上清，用无克隆培养上清。空白对照：不加一抗，用1%BSA代替。无关对照（替代对照）：用无关项目一抗，或无关项目的抗体。Anti-Supervillin抗体，监理蛋白抗体产品的相关产品：Anti-SALL4抗体，锌指转录蛋白Sall4抗体&Anti-SOX17抗体，转录因子SOX17抗体&Anti-SNX5抗体，分选连接蛋白5抗体&Anti-SNX2抗体，分选连接蛋白2抗体&Anti-SNX7抗体，分选连接蛋白7抗体&Anti-SOX1抗体，核转录因子抗体&Anti-SOX7抗体，转录因子SOX7抗体&Anti-Sohlh1抗体，精子卵子结合生成碱性螺旋蛋白抗体&Anti-SOHLH2抗体，精子卵子结合生成碱性螺旋蛋白2抗体&Anti-Stella抗体，发育多能性相关蛋白3抗体&Anti-Spectrin alpha chain, erythrocytic 1抗体，血影蛋白A链红细胞型抗体Anti-SPAG6抗体，精子相关抗原6抗体&Anti-SAP155抗体，剪接体相关蛋白155抗体&Anti-Sulfite oxidase抗体，亚硫酸盐氧化酶抗体&Anti-SCUBE3抗体，新型分泌细胞表面蛋白/成骨细胞相关蛋白SCUBE3抗体Anti-SCUBE2抗体，内皮分泌蛋白SCUBE2抗体&Anti-STRA6抗体，维甲酸诱导蛋白6抗体&Anti-SCXA抗体，碱性螺旋-环-螺旋转录因子SCXA抗体&Anti-SIX2抗体，转录因子同源框蛋白SIX2抗体&Anti-SUMF1抗体，硫酸酯酶修饰因子1抗体&Anti-STK33抗体，丝氨酸/苏氨酸激酶33抗体&Anti-phospho-STK39(Ser325)抗体，磷酸化丝氨酸/苏氨酸蛋白激酶39抗体Anti-Stanniocalcin 2抗体，斯钙素2抗体&Anti-SNX4抗体，分选连接蛋白4抗体&Anti-SH3PX1抗体，分选连接蛋白9抗体&Anti-SNX10抗体，分选连接蛋白10抗体&Anti-SNX11抗体，分选连接蛋白11抗体&Anti-SNX6抗体，分选连接蛋白6抗体&Anti-phospho-SP1 (Thr453)抗体，磷酸化转录生长因子SP1抗体&Anti-STOML2抗体，溴化丙胺太林相关蛋白2抗体&Anti-Alpha SNAP抗体，可溶性附着蛋白&-SNAP抗体&Anti-SECTM1抗体，分泌和跨膜蛋白1抗体&Anti-phospho-c-Abl (Ser569)抗体，磷酸化非受体酪氨酸激酶c-Abl抗体Anti-SPATA3抗体，精子生成相关蛋白3抗体&Anti-HADHSC抗体，短链L-3羟烷基辅酶A脱氢酶抗体&Anti-S100A6抗体，S100钙结合蛋白A6抗体&Anti-SLC7A9抗体，离子转运相关蛋白SLC7A9抗体&Anti-phospho-DOK1 (Ser450)抗体，磷酸化D酪氨酸激酶衰减蛋白1抗体Anti-STAT4抗体，信号转导和转录激活因子4抗体&Anti-FHOD3抗体，FHOD3蛋白抗体&Anti-Supervillin抗体，监理蛋白抗体&Anti-SP-A抗体，肺表面活性蛋白A抗体&Anti-SP-A抗体，肺表面活性蛋白A抗体&Anti-SLC20A2抗体，溶质载体蛋白家族20成员2抗体&Anti-Somatostatin抗体，生长抑素抗体&Anti-phospho-Syntaxin 1a(Ser188)抗体，磷酸化突触融合蛋白1抗体Anti-SCNN1D抗体，上皮钠离子通道蛋白D/&ENaC抗体&Anti-Sclerostin抗体，骨形态发生抑制蛋白SOST抗体&Anti-SLFNL1抗体，SLFNL1抗体&Anti-Sarcomeric Alpha Actinin抗体，&横纹肌辅肌动蛋白/&-SCA抗体
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感兴趣的其他供应Phosphotyrosine Antibody Review and FAQs
Phosphotyrosine Antibody Review and FAQs
Mary Johnson (mary at labome dot com)
Synatom Research, Princeton, New Jersey, United States
http://dx.doi.org/10.13070/mm.en.3.173
last modified : ; original version :
MATER METHODS
A comprehensive review of phosphotyrosine antibodies, FAQs and purchase guide.
Phosphotyrosine antibody
This is a review about phosphotyrosine antibodies (phospho-tyrosine antibodies), based on 83 published articles as of March 18, 2015, using phosphotyrosine antibodies in western blot, immunoprecipitation, immunocytochemistry, and other immunological technologies in
that Labome has been surveying systematically since 2006.
This review is aimed to facilitate the identification of the best-suited phosphotyrosine antibodies.
can be obtained from many suppliers. The article also addresses some of commonly asked questions about phosphotyrosine antibodies.
Figure 1. An example of phosphorylation studies before the usage of anti-phosphotyrosine antibodies (from [] ).
Tyrosine phosphorylation is one of the major means of cell signaling transduction and enzymatic activity regulation.
The advent of anti-phosphotyrosine antibodies is a significant event in signal transduction research.
Before the availability of anti-phosphotyrosine antibodies, tyrosyl phosphorylation of proteins and enzymes was investigated through hazardous and time-consuming radioactive experiments [] ; Figure 1 examplifies such an experiment.
Anti-phosphotyrosine antibodies are commonly used in western blots after a targeted protein has been immunoprecipitated to measure the tyrosyl phosphorylation of the protein. They are also used on cell lysates to examine the overall change of tyrosine phosphorylation level in response to various treatments.
Review of other general (nongene-specific) antibodies are available:
tag antibodies ( ,
); western blot loading controls ( ,
Figure 2. A composite figure derived from [] indicating the substrate selectivity of various anti-phosphotyrosine antibodies.
Upper table: sources and related information about the seven anti-phosphotyrosine antibodies. Middle panel left figure: substrate selectivity of
anti-phosphotyrosine antibodies in dot blots against synthetic phosphotyrosine peptides.
Middle panel right figure:
variations in bands and intensities of anti-phosphotyrosine antibodies in western blots against the equally-loaded samples.
Bottom table:
summary of substrate selectivity against phosphopeptides and phosphorylated CagA proteins by commercial α-phosphotyrosine antibodies.
Phosphotyrosine antibody clones
Three clones are commonly used: 4G10, PY20, and p-TYR-100.
PY20 clone of IgG2b isotype was first developed and described by Dr. John R. Glenney, Jr and his colleagues in 1988 [].
The other two clones were developed by commerical identities (Upstate/EMD Millipore 4G10 and New England Biolab/Cell Signaling Technology p-TYR-100).
Anti-phosphotyrosine antibodies binding to tyrosine-phosphorylated peptides exhibit substantial sequence selectivity. Michele Tinti et al. demonstrated that different phosphotyrosine antibody clones recognized their target sites in a sequence-specific manner and that this recognition differed from each other []. According to peptide microarray data, although different clones (i.e. 4G10, pY20 and p-TYR-100) showed a common enrichment of prolines at position +3 and leucine at position -1 with respect to the phosphorylated tyrosine in the peptides, differences between the sequence preferences were observed. For example, clone 4G10 displayed a sequence context preference for Pro, Thr, Val and Phe at position -3. Both 4G10 and p-TYR-100 bindings were likely to be hindered by a negative charge at position -1, while pY20 was more sensitive to a positive charge at the same position. Among phosphotyrosine peptides, a total of 10%-20% could be uniquely recognized by one antibody. These specificity differences were reflected in Western blots, where band intensities of 4G10 and p-TYR-100 differed and pY20 even stained an additional group of 95–34 kDa proteins [].
This substantial sequence selectivity is further evidenced by a direct comparison of seven commercial antibodies with regards to synthetic phospho-peptides in dot blots and phosphorylated CagA protein in Western blots (Figure 2) [].
SupplierNum 46 15BD Transduction Laboratories14Cell Signaling Technology6UBI3ICN Biomedicals2 Sigma2Molecular Probes / Invitrogen / LifeTech / Thermo Fisher1Amersham Biosciences1Biomol/Enzo Life Sciences1Table 1. Major suppliers of phosphotyrosine antibodies and the numbers of citations among the 83 publications surveyed by Labome. Phosphotyrosine antibody in literature
Table 1 lists the suppliers of phosphotyrosine antibodies among the 83 publications surveyed by Labome. Among the 23 articles that indicated clone names, 18 articles listed 4G10, and 6 articles listed PY20 clone (one article listed both clones [] ).
Table 2 lists the major applications of phosphotyrosine antibodies among the publications.
ApplicationnumTop supplierswestern blot64Upstate Biotechnology/EMD Millipore,
BD Transduction Laboratories,
Santa Cruzimmunoprecipitation16Upstate/EMD Millipore,
Santa Cruz Biotechnology,
BD Transduction Laboratoriesimmunocytochemistry7Upstate Biotechnology/EMD Millipore immunohistochemistry2Table 2. Applications of phosphotyrosine antibodies and their numbers of citations among the 83 publications surveyed by Labome.Upstate Biotechnology/EMD Millipore
Upstate Biotechnology is now part of EMD Millipore.
has provided some of most commonly used anti-phospho-tyrosine antibodies, including the most commonly used clone 4G10. More than half of the publications cited Upstate anti-phospho-tyrosine antibodies in western blot, immunoprecipitation, and immunocytochemistry.
Antibodies with clone 4G10 have been generated from both hybridoma and
Upstate anti-phosphotyrosine antibody was used to perform western blot and immunohistochemistry in order to study the function of sema3E-plexin D1 [], to perform immunoprecipitation in order to study the roles of LRP1 in the adult CNS [],
and western blot analysis (clone 4G10) in order to determine the receptor property of erythropoietin receptor during receptor signaling activation [] and to study the effect of the facilitation of AMPA receptor synaptic delivery on cognitive enhancement [].
Among papers published earlier in 2001, K Aoyama used 4G10 in western blot to study a novel dual specificity phosphatase, LMW-DSP2; K Sauer et al used 4G10 in western blot to examine the interaction of HPK1 with BLNK in B cells and with SLP-76 in T cells, A E Aplin et al used 4G10 in western blot to study the regulation of ERK nuclear translocation and Elk-1 phosphorylation by integrin- H Konishi et al used it in western blot to study the tyrosine phosphorylation sites of PKC delta in the H2O2- C C Chen used both clone PY-20 and clone 4G10 in western blot and immunocytochemistry to study the induction of adhesive signaling in primary hu C Gilbert used 4G10 in immunoprecipitation to evaluate the SAM68 roles in signal transduction during human neutrophil phagocytosis.
In 2002, clone 4G10 was used in western blots by Matthew N Poy to study the mitogenic action of insulin regulated by Shc and CEACAM1 interaction, by Kenneth L Byron to examine vasopressin signal transduction in A7r5 vascular smooth muscle cells, by Diane Lejeune et al to study STAT3 serine phosphorylation, and in immunocytochemistry by Ann L Moor to localize tyrosine-phosphorylated PLC (pY-PLC) in HTC cells.
In 2003, Yosuke Minami et al conducted western blot experiments with Upstate Biotechnology antiphosphotyrosine antibody to differentiate the antiapoptotic pathways between wild-type and mutated FLT3; K C Leung et al used 4G10 in western blot to study the inhibiting effects of estrogen on transcriptional action of GH through the SOCS-2 mediated JAK/STAT John H Griffin used 4G10 in western blot to study a fusion kinase in EOL-1 cells and the idiopathic hypereosinophilic syndrome.
Matthew L Jones in 2004 used 4G10 to immunoprecipitate phosphorylated SHP-1 Tod A Brown used anti-phosphotyrosine monoclonal antibody in western blot to elucidate the tyrosine phosphorylation of a novel membrane glycoprotein p80/gp140/CUB domain-containing protein 1 Charng-Jui Chen et al used 4G10 in western blot and immunocytochemistry to investigate the inhibition of IL-2 production and proliferation in human T cells by carcinoembryonic antigen-related cellular adhesion molecule 1.
In 2005, Upstate Biotechnology anti-phosphotyrosine antibodies were used in western blots to examine the Rac-MKK3/6-p38 pathway in breast epithelial cells by Ilchung Chin, the regulation of the endothelial cell response to Ang-1 through stable interaction between alpha5beta1 integrin and Tie2 tyrosine kinase receptor by Ilaria Cascone et al, the direct interaction between human CNK1 and Raf-1 by Algirdas Ziogas et al, and T-cell receptor-induced activation of phospholipase C-gamma1 by a sequence-independent function of the P-I region of SLP-76 by Ronnie Gonen et al. Upstate Biotech anti-phosphotyrosine antibody was used in immunoprecipitation to study the phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture by Dr. Amanchy in 2005.
Upstate Biotechnology anti-phosphotyrosine (1:3000) was used in western blot to demonstrate that lipid rafts sequester Ret away from the degradation machinery to sustain Ret signaling by Dr. Pierchala in 2006.
Upstate/Millipore 4G10 antibody was used in western blot to study the role of MNAR in 17beta-estradiol (E2)-induced activation of the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by Dr.Greger in 2007. Additional citations include [-]. Santa Cruz Biotechnology
Among the publications [,
antiphosphotyrosine (anti-pTyr) antibody was used in western blots to study the downregulation of the Ras-mitogen-activated protein kinase pathway by S Elowe in 2001, and to study the role of beta-arrestin in ubiquitination and
IGF-1 receptor down-regulation by Leonard Girnita in 2005; its PY20 anti-phosphotyrosine antibody was used in immunoprecipitation to study the IL-2 production and proliferation in human T cells inhibited by the cell-cell adhesion molecule carcinoembryonic antigen-related cellular adhesion molecule 1 by Charng-Jui Chen 2004;
Matthew N Poy in 2002 also used anti-phosphotyrosine antibody (PY20) in immunoprecipitation to study the regulation of insulin mitogenic action by Shc and CEACAM1 interaction, and Santa Cruz Biotechnology phosphotyrosine antibody was used in western blot to investigated the mechanism and function of ubiquitination of protease-activated receptor 2 (PAR2) by Dr. Jacob in 2005.
Santa Cruz Biotechnology mouse monoclonal anti-phosphotyrosine antibody was used to perform western blot to investigate the roles of Vav2 and Vav3 in skin cancer [].
Transduction Laboratories/BD Biosciences
Publications citing BD Biosciences anti-phosphotyrosine antibodies include [, , -], where Koichi Seta in 2003 used BD Biosciences horseradish peroxidase-conjugated anti-phosphotyrosine monoclonal antibody (RC20H) in western blot to study the angiotensin II-induced trans-activation of the EGF receptor and found that the transactivation was mediated by phosphorylation of tyrosine 319 of the angiotensin II type 1 the same clone was used by C Sweeney in 2001 in western blot to examine ErbB receptor-mediated signaling pathway stimulation Wen Hong Shen et al in 2004 used a different mouse anti-phosphotyrosine clone (PY20) in both western blot and immunoprecipitation to study cyclin A expression and retinoblastoma
polyclonal anti-phosphotyrosine antibody was used in immunoprecipitation to study vasopressin-induced signal transduction in A7r5 vascular smooth muscle cells by Kenneth L Byron in 2002; and peroxidase-conjugated anti-phosphotyrosine antibody was used in western blots to exploit EphA2 as a therapeutic target of cancer by Dr. Koolpe in 2002.
Cell Signaling Technology
Cell Signaling Technology phosphotyrosine antibody was used in western blot and immunoprecipitation to study the role of p68 RNA helicase [], in western blot to study cell adhesion molecule [] and vIL-6 ] and its monoclonal mouse anti-phosphotyrosine antibody was used in immunocytochemistry to study supervillin [].ICN Biomedicals/MPBIO
monoclonal anti-phosphotyrosine antibody PY20 in western blot to study the involvement of tumor necrosis factor receptor-associated protein 1 (TRAP1) in beta-hydroxyisovalerylshikon-induced apoptosis [] and the role of aldose reductase pathway during myocardial ischemic injury []. Sigma
In 2001, L You used Sigma monoclonal phosphotyrosine antibody in western blot to study migration and signal transduction induced by cell-derived neurotrophic factor (GDNF) in corneal epithelial cells []. Amersham Biosciences/GE Health Science
monoclonal anti-phosphotyrosine horseradish peroxidase-conjugated antibody was used in western blot to study insulin receptor catalytic activity inhibition by in 2002 [].Commonly asked questions about phosphotyrosine antibodies
Some of the commonly asked questions are answered here. How to detect tyrosine phosphorylation
of a specific protein?
There are several ways.
use a phosphorylation-specific
against the specific
use an antibody against the specific protein to
immunoprecipitate both
phosphorylated or non-phosphorylated forms
of the specific
then detect
phosphotyrosine antibodies in Western blot.
use phosphotyrosine antibodies
to immunoprecipitate
all tyrosine-phosphorylated proteins, and then detect with an antibody
against the specific protein.
mass spec.
For detailed discussion of the detection of
protein phosphorylation, see Labome
article about
. During Western blotting of phosphotyrosine antibodies,
should nonfat dry milk or BSA
be used as the blocking agent?
should be used, since nonfat dry milk contains proteins that are phosphorylated at tyrosine residues.
can the lysate samples
before detection of
phosphorylation?
The samples should generally be used fresh, since
the proteins
might be degraded, and dephosphorylation
due to phosphatases.Is there any anti-phosphotyrosine anybody
that can be used to neutralize or block the activities of
protein kinases
or phosphatases?
We do not know the answer to this question.
Anti-phosphotyrosine anybodies have been used for Western blot, immunoprecipitation,
immunocytochemistry, and immunohistochemistry.
References
Ushiro H, Cohen S. Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes. J Biol Chem. 3-5
Lind J, Backert S, Pfleiderer K, Berg D, Yamaoka Y, Sticht H, et al. Systematic analysis of phosphotyrosine antibodies recognizing single phosphorylated EPIYA-motifs in CagA of Western-type Helicobacter pylori strains. PLoS ONE. 488
Blaivas J, Scott R, Labib K. Urodynamic evaluation as neurologic test of sacral cord function. Urology. -7
Tinti M, Nardozza A, Ferrari E, Sacco F, Corallino S, Castagnoli L, et al. The 4G10, pY20 and p-TYR-100 antibody specificity: profiling by peptide microarrays. N Biotechnol. -7
Chen C, Chen N, Lau L. The angiogenic factors Cyr61 and connective tissue growth factor induce adhesive signaling in primary human skin fibroblasts. J Biol Chem. 43-52
Casazza A, Finisguerra V, Capparuccia L, Camperi A, Swiercz J, Rizzolio S, et al. Sema3E-Plexin D1 signaling drives human cancer cell invasiveness and metastatic spreading in mice. J Clin Invest. 4-98
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