| 產(chǎn)品編號(hào) | bs-3465R-Cy3 |
| 英文名稱(chēng) | Rabbit Anti-Phospho-VASP(Ser157)/Cy3 Conjugated antibody |
| 中文名稱(chēng) | Cy3標(biāo)記的磷酸化血管擴(kuò)張刺激磷蛋白抗體 |
| 別 名 | VASP(phospho S157); Vasodilator-stimulated phosphoprotein; Vasodilator-stimulated phosphoprotein； VASP； VASP_HUMAN. |
| 規(guī)格價(jià)格 | 100ul/2980元 購(gòu)買(mǎi) 大包裝/詢(xún)價(jià) |
| 說(shuō) 明 書(shū) | 100ul |
| 產(chǎn)品類(lèi)型 | 磷酸化抗體 |
| 研究領(lǐng)域 | 腫瘤 細(xì)胞生物 免疫學(xué) 神經(jīng)生物學(xué) 信號(hào)轉(zhuǎn)導(dǎo) 細(xì)胞凋亡 轉(zhuǎn)錄調(diào)節(jié)因子 激酶和磷酸酶 |
| 抗體來(lái)源 | Rabbit |
| 克隆類(lèi)型 | Polyclonal |
| 交叉反應(yīng) | Human, Mouse, (predicted: Rat, Dog, ) |
| 產(chǎn)品應(yīng)用 | IF=1:50-200
not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user. |
| 分 子 量 | 40kDa |
| 性 狀 | Lyophilized or Liquid |
| 濃 度 | 1mg/ml |
| 免 疫 原 | KLH conjugated Synthesised phosphopeptide derived from human VASP around the phosphorylation site of Ser157 |
| 亞 型 | IgG |
| 純化方法 | affinity purified by Protein A |
| 儲(chǔ) 存 液 | 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. |
| 保存條件 | 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. |
| 產(chǎn)品介紹 |
background: Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG. [provided by RefSeq]. Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. Subunit: Homotetramer. Interacts with PFN1, PFN2, LPP, ACTN1 and ACTG1. Interacts, via the EVH1 domain, with the Pro-rich regions of ZYX. This interaction is important for targeting to focal adhesions and the formation of actin-rich structures at the apical surface of cells. Interacts, via the EVH1 domain, with the Pro-rich domain of Listeria monocytogenes actA. Interacts with APBB1IP. Interacts, via the Pro-rich domain, with the C-terminal SH3 domain of DNMBP (By similarity). Subcellular Location: Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell projection, lamellipodium membrane. Cell projection, filopodium membrane. Note=Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions. Tissue Specificity: Highly expressed in platelets. Post-translational modifications: Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-157, the preferred site for PKG/PRKG1, Ser-239. In ADP-activated platelets, phosphorylation by PKA or PKG on Ser-157 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-278 requires prior phosphorylation on Ser-157 and Ser-239. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-278 by AMPK does not require prior phosphorylation at Ser-157 or Ser-239. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Phosphorylation at Ser-322 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-157, while nitric oxide (NO) promotes phosphorylation at Ser-157, but also at Ser-239. Response to NO and CO is blunted in platelets from diabetic patients, and VASP is not phosphorylated efficiently at Ser-157 and Ser-239. Similarity: Belongs to the Ena/VASP family. Contains 1 WH1 domain. Database links: Entrez Gene: 7408 Human Entrez Gene: 22323 Mouse Omim: 601703 Human SwissProt: P50552 Human SwissProt: P70460 Mouse Unigene: 515469 Human Unigene: 9684 Mouse Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. ????VASP屬于Ena-VASP蛋白家族，是一種肌動(dòng)蛋白結(jié)合蛋白。細(xì)胞骨架動(dòng)力學(xué)的調(diào)節(jié)在細(xì)胞粘附、細(xì)胞變形、細(xì)胞移動(dòng)等生理過(guò)程中是必需的。VASP可能也參與細(xì)胞內(nèi)信號(hào)通道，該通道調(diào)節(jié)整聯(lián)蛋白與細(xì)胞外基質(zhì)間的相互作用。VASP被周期核苷酸依賴(lài)型激酶PKA與PKG所調(diào)節(jié),在一些腫瘤的分化、增值、轉(zhuǎn)移中起到一定的作用，在腫瘤中有較高的表達(dá)。 ????近年來(lái)的研究發(fā)現(xiàn)VASP在與細(xì)胞骨架調(diào)節(jié)有關(guān)的各種細(xì)胞行為中起著重要作用，如神經(jīng)細(xì)胞軸索的延伸、T細(xì)胞的移動(dòng)、成纖維細(xì)胞的遷移等。 ????VASP的磷酸化受PKG（cGMP-dependent protein kinase）和PKA（cAMP—dependent protein kinase）的調(diào)控。在粘附斑的形成與脫落過(guò)程中，該磷酸化起著一個(gè)“開(kāi)關(guān)”的作用。 |
