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3,3'5,5'-四甲基聯苯胺丙磺酸鈉號：102062-36-2   
英文名稱：TMB-PS；TMB-N-Propane sulfonic acid sodium Salt；N-(3-Sulfopropyl)-3,3',5,5'-tetramethylbenzidine sodium salt   
其他名稱：N-(3-磺丙基)-3,3',5,5'-四甲基聯苯胺鈉鹽；TMB丙磺酸鈉   
號：102062-36-2   
C19H25N2NaO3S=384.47   
級別：BR   
純度：≥98%   
熔點：220～251℃   
摩爾吸收系數：≥43000(λmax213nm)   
性狀(以下信息僅供參考)：白色或淡黃色結晶。溶于水。一種水溶性的TMB類似物，無色水溶液在過氧化輕或過氧化物酶存在時變成藍綠色。Z大吸收波長:655nm   
用途：本品僅供科研，不得用于其它用途。(以下用途僅供參考)用于檢測過氧化輕或過氧化物酶活性   
保存：2～8℃，避光3,3'5,5'-四甲基聯苯胺丙磺酸鈉號：102062-36-2儲存條件：
避光、干燥陰涼處封閉貯存,嚴禁與有毒、有害物品混放、混運。本品為非危險 產品可按一般化學品運輸,輕搬動輕放,防止日曬、雨淋！受熱、受潮、受光后易喪失活力,保存期短,因此貯存和運輸條件比較苛刻。
運輸：汽車運輸、EMS郵政快遞，申通快遞等， 款到上海3天內發(fā)貨；
售后：如您對我們的產品服務及技術指標有特殊要求，請及時通知我方。
存儲：應貯存在干燥清潔避光的環(huán)境中，嚴禁與有毒物質混放，以免污染（保質期為兩年）。
3,3'5,5'-四甲基聯苯胺丙磺酸鈉號：102062-36-2主要優(yōu)級純、分級純和化學純3種：
（1）優(yōu)級純（GR：Guaranteed reagent），又稱一級品或保證試劑，99.8%，這種試劑純度Z高，雜質含量Z低，適合于重要精密的分析工作和科學研究工作，使用綠色瓶簽。
（2）分析純（AR），又稱二級試劑，純度很高，99.7%，略次于優(yōu)級純，適合于重要分析及一般研究工作，使用紅色瓶簽。
（3）化學純（CP），又稱三級試劑，≥ 99.5%，純度與分析純相差較大，適用于工礦、學校一般分析工作。使用藍色（深藍色）標簽。
（4）實驗試劑（LR：Laboratory reagent），又稱四級試劑。

 optimal dilutions/concentrations should be determined by the end user. 
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.
Important Note  This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
產品介紹 SHIP1 is a member of the inositol polyphosphate-5-phosphatase (INPP5) family and contains an N-terminal SH2 domain, an inositol phosphatase domain, and two C-terminal protein interaction domains. Expression of this protein is restricted to hematopoietic cells where its movement from the cytosol to the plasma membrane is mediated by tyrosine phosphorylation in response to multiple cytokine and B and T cell receptor activation. At the plasma membrane, the protein hydrolyzes the 5' phosphate from phosphatidylinositol (3,4,5)-trisphosphate and inositol-1,3,4,5-tetrakisphosphate, thereby affecting multiple signaling pathways. Overall the protein functions as a negative regulator of myeliod cell proliferation and survival.
Function : Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in plaets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6.
Subunit : Interacts with tyrosine phosphorylated forms of SHC1, DOK1, DOK3, PTPN11/SHP-2, SLAMF1/CD150. Interacts with PTPN11 in response to IL-3. Interacts with receptors EPOR, MS4A2/FCER1B and FCER1G, FCGR2A, FCGR2B and FCGR3. Interacts with GRB2 and PLCG1. Interacts with tyrosine kinases SRC and TEC. Interacts with FCGR2A, leading to regulate gene expression during the phagocytic process. Interacts with c-Met/MET (By similarity). Interacts with MILR1 (tyrosine-phosphorylated). Can weakly interact (via NPXY motif 2) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif (By similarity).
Subcellular Location : Cytoplasm. Membrane; Peripheral membrane protein. Note=Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B) or CD16/FCGR3. Tyrosine phosphorylation may also participate in membrane localization (By similarity).
Tissue Specificity : Specifically expressed in immune and hematopoietic cells. Expressed in bone marrow and blood cells. Levels vary considerably within this compartment. Present in at least 74% of immature CD34+ cells, whereas within the more mature population of CD33+ cells, it is present in only 10% of cells. Present in the majority of T-cells, while it is present in a minority of B-cells (at protein level).
Post-translational modifications : Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as cytokines, growth factors, antibodies, chemokines, integrin ligands and hypertonic and oxidative stress. Phosphorylated upon IgG receptor FCGR2B-binding.
Similarity : Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase family.
Contains 1 SH2 domain.
Database links : UniProtKB/Swiss-Prot: Q92835.2
英文名稱  Anti-phospho-Src(Tyr529)
中文名稱  磷酸化Src原癌基因抗體
別    名  Src(Phospho-Tyr529); ASV; Avian sarcoma virus; c SRC; CDNA FLJ14219 fis clone NT2RP3003800 highly similar to Rattus norvegicus tyrosine protein kinase pp60 c src mRNA; cSrc; EC 2.7.10.2; Neuronal CSRC tyrosine specific protein kinase; Neuronal SRC; Oncogene SRC; OTTHUMP00000030931; OTTHUMP00000174476; OTTHUMP00000174477; p60 Src; p60-Src; p60Src; pp60c src; pp60c-src; pp60csrc; Proto oncogene tyrosine protein kinase Src; Proto-oncogene c-Src; Proto-oncogene tyrosine-protein kinase Src; Protooncogene SRC; protooncogene SRC Rous sarcoma; Src; SRC Oncogene; SRC_MOUSE; SRC1; Tyrosine kinase pp60c src; Tyrosine protein kinase SRC 1; Tyrosine protein kinase SRC1; v src avian sarcoma (Schmidt Ruppin A2) viral oncogene homolog; V src sarcoma (Schmidt Ruppin A 2) viral oncogene homolog (avian); v src sarcoma (Schmidt Ruppin A 2) viral oncogene homolog avian; vsrc avian sarcoma (Schmidt Ruppin A2) viral oncogene homolog.
濃    度  1mg/1ml
規(guī) 格  0.1ml/100μg
抗體來源  Rabbit 
克隆類型  polyclonal
交叉反應  Human, Mouse, Rat, Chicken, Dog, Pig, Horse, Rabbit
產品類型  一抗  磷酸化抗體  
研究領域  腫瘤 細胞生物 染色質和核信號 神經生物學 信號轉導 激酶和磷酸酶 表觀遺傳學 
蛋白分子量  predicted molecular weight: 61kDa
性    狀  Lyophilized or Liquid
免 疫 原  KLH conjugated Synthesised phosphopeptide derived from mose Src around the phosphorylation site of tyrosine 529
亞    型  IgG
純化方法  affinity purified by Protein A
儲 存 液  0.01M PBS, pH 7.4 with 10 mg/ml BSA and 0.1% Sodium azide
產品應用   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
（石蠟切片需做抗原修復）
 not yet tested in other applications.
 optimal dilutions/concentrations should be determined by the end user. 
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.
Important Note  This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
產品介紹 Src (also known as pp60src) is a non receptor Tyrosine Kinase involved in signal transduction in many biological systems and implicated in the development of human tumors. There are two critical phosphorylation sites of tyrosine on Src, tyrosine 418 and tyrosine 529 (referring to human Src sequence). The tyrosine 418 is located in the catalytic domain and is one of the autophosphorylation sites. Full catalytic activity of Src requires phosphorylation of tyrosine 418. The tyrosine 529 is located near the carboxyl terminus of Src and acts as a negative regulator, in that Src is held in the inactive form through an intramolecular interaction between the SH2 domain and the carboxyl terminus when tyrosine 529 is phosphorylated by Csk. This conformation blocks phosphorylation of tyrosine 418 at the catalytic domain, thereby preventing Src activation. When tyrosine 529 is dephosphorylated, tyrosine 418 can be maximally phosphorylated and Src becomes active. Src is a proto oncogene that may play a role in the regulation of embryonic development and cell growth. Mutations in this gene could be involved in the malignant progression of colon cancer.
Immunogen: Synthetic peptide (Human) derived from the region of Src that contains tyrosine 529, based on the human sequence. The sequence is conserved in mouse (tyrosine 534), chicken (tyrosine 527) and frog (tyrosine 525).
Function : Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of ADRBK1, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (By similarity). Phosphorylates BCAR1 at 'Tyr-132' (By similarity).
Subunit : Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2 (By similarity). Interacts with DDEF1/ASAP1 via its SH3 domain. Interacts with CCPG1. Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin. Interacts with RALGPS1 via its SH3 domain. Interacts with CAV2 (tyrosine phosphorylated form). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with FCAMR and PXN. Interacts with ARRB2. Interacts with ARRB1. Interacts with SRCIN1 (By similarity). Interacts with SRCIN1. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1, ESR1 (dimethylated on arginine) and FAK. Interacts (via SH2 and SH3 domain) with TNK2. Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain). Interacts with TRAF3 (via RING-type zinc finger domain). Interacts with DDX58, MAVS and TBK1. Interacts (via SH2 domain) with GNB2L1/RACK1; the interaction is enhanced by tyrosine phosphorylation of GNB2L1 and inhibits SRC activity (By similarity). Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration. Interacts with ERBB2 and STAT1. Interacts with PDGFRA (tyrosine phosphorylated). Interacts with CSF1R. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with DDR2. Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Interacts with DDR1 and DAB2. [INTERACTION] Q63767:Bcar1 (xeno); NbExp=2; IntAct=EBI-298680, EBI-1176801; P07141:Csf1; NbExp=2; IntAct=EBI-298680, EBI-777188; Q8T4F7:ena (xeno); NbExp=2; IntAct=EBI-298680, EBI-466810; P54763:Ephb2; NbExp=3; IntAct=EBI-298680, EBI-537711; P05106:ITGB3 (xeno); NbExp=5; IntAct=EBI-298680, EBI-702847; P49023:PXN (xeno); NbExp=2; IntAct=EBI-298680, EBI-702209; Q01973:ROR1 (xeno); NbExp=3; IntAct=EBI-298680, EBI-6082337; P70315:Was; NbExp=2; IntAct=EBI-298680, EBI-644195.
Subcellular Location : Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasm, cytoskeleton. Note=Localizes to focal adhesion sites after integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain.
Tissue Specificity : Expressed ubiquitously. Plaets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues.
Post-translational modifications : Myristoylated at Gly-2, and this is essential for targeting to membranes (By similarity).
Dephosphorylated at Tyr-535 by PTPRJ (By similarity). Phosphorylated on Tyr-535 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-424. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-535, the SH3 domain engaged with the SH2-kinase linker, and Tyr-424 dephosphorylated. Dephosphorylation of Tyr-535 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-535, Tyr-424 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-535 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-74 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity (By similarity).
S-nitrosylation is important for activation of its kinase activity (By similarity).
Ubiquitinated in response to CDK5-mediated phosphorylation.