Effects of miR-34a on cellular phosphoprotein activation in NB1691luc cells. NB1691luc (1 × 106) cells were reverse transfected with premiR-34a (30 μM) or a p

A 47 kDa phosphoprotein is involved in the respiratory-burst oxidase of phagocytic cells. After stimulation of neutrophils with phorbol myristate acetate, this phosphoprotein was identified in both the cytosol and membranes. Peptide mapping of the two forms resulted in identical patterns of phosphopeptides. Dose-response curves for accumulation of phosphoprotein in the two sites were very similar, whereas the detection of the phosphoprotein in the cytosol preceded that in the membranes. The membrane-associated 47 kDa phosphoprotein was absent from the neutrophils of patients with X-chromosome-linked chronic granulomatous disease, which lack cytochrome b-245, and intermediate levels were detected in the membranes of their heterozygote carrier mothers. Activation of the neutrophil oxidase system appears to be dependent upon phosphorylation of the cytosolic 47 kDa protein and its association with cytochrome b-245 in the membranes. It is probably the cytosolic factor required for reconstitution of ...

TY - JOUR. T1 - Cloning of a novel phosphoprotein regulated by colony-stimulating factor 1 shares a domain with the Drosophila disabled gene product. AU - Xu, Xiangxi. AU - Yang, W.. AU - Jackowski, S.. AU - Rock, C. O.. PY - 1995/1/1. Y1 - 1995/1/1. N2 - A unique protein with an apparent molecular mass of 96 kilodaltons (p96) was detected in the routine macrophage cell line, BAC1.2F5. The murine cDNA encoding p96 was cloned and sequenced, along with cDNAs representing two alternatively spliced forms of the protein. All three proteins possessed identical amino-terminal domains with significant similarity to the amino- terminal domain of the Drosophila disabled gene product and carboxyl-terminal domains containing proline-rich sequences characteristic of src homology region (domain 3) binding regions. BAC1.2F5 cells predominately expressed the p96 protein, although mRNA and protein corresponding to the p67 splice variant were also detected. Electrophoretic gel retardation of p96 in response to ...

The Phosphoprotein Enrichment Kit provides a rapid and specific IMAC-based procedure for isolating phosphorylated proteins from mammalian cells and tissues. The Phosphoprotein Enrichment Kit Procedure is fast, with an average cell-to-sample purification time of less than 2 hours. It is also straightforward, consisting of four main steps (Figure 1): adding Extraction/Loading Buffer to the cell or tissue pellet to extract total cellular protein, loading the extract on an affinity column, washing, and, finally, eluting the bound phosphoprotein with the detergent-free Elution Buffer. A single buffer-Extraction/Loading Buffer-is used for both the protein extraction and affinity column steps, making buffer exchange unnecessary. This saves time and prevents sample loss. The procedure is non-denaturing, so phosphoproteins remain folded throughout the process, even during the extraction and elution steps.. The Phosphoprotein Enrichment Kit may be used with any mammalian cell type. Cell lines tested ...

The two proteins with different electrophoretic mobilities that were immunodetected by using the anti-FUS5 antibody in both the wild type and cop1-6 are products of the same gene. If these two proteins were the products of two different genes, we would expect that only one of them would be missing in the fus5 mutant strains, but this is not the case. Both proteins are absent in all fus5 mutant strains, although both are present in strains known to have an intact COP9 complex, such as wild type and cop1-6. In our gel filtration analysis, the FUS5 doublet was also detected in fractions corresponding to the COP9 complex. However, we do not know whether these two proteins represent different functional forms of FUS5, or whether they are simply an artifact of SDS-PAGE. It should be noted that both FUS6 and COP9 sometimes appear as a doublet after SDS-PAGE (Chamovitz et al., 1996; Chamovitz and Deng, 1998).. The mobility shift of FUS5 between that of the wild type and the cop9 and fus6 mutants is most ...

Intracellular protein levels, subcellular localization, or activation state are reflective of a cells functions. Some relevant cell populations are so rare as...

The KOMP Repository is located at the University of California Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...

Homo sapiens acidic (leucine-rich) nuclear phosphoprotein 32 family, member A (ANP32A), mRNA. (H00008125-R01) - Products - Abnova

Activation of cytoplasmic tyrosine kinase activity is required for T cell receptor (TCR)-dependent lymphocyte activation (1). Adapter proteins serve as substrates for these kinases and as such may function to couple the TCR with downstream signaling events (2-6). SLP-76 is a hematopoietic cell-specific adapter protein that is phosphorylated rapidly on NH2-terminal tyrosine residues after TCR ligation (3), providing a binding site for the Src homology 2 (SH2) domain of Vav (7). SLP-76 also contains a central proline-rich region that associates constitutively with the SH3 domains of Grb2 (8). In addition, SLP-76 has a COOH-terminal SH2 domain that inducibly associates with SLAP-130 (SLP-76-associated phosphoprotein of 130 kD) and an unidentified 62-kD tyrosine phosphoprotein (5, 8, 9). The ability of SLP-76 to augment TCR-dependent nuclear factor of activated T cells (NFAT) activation when transiently overexpressed in a T cell line is dependent on the presence of each of these domains, suggesting ...

Shop Steroidogenic acute regulatory protein ELISA Kit, Recombinant Protein and Steroidogenic acute regulatory protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.

Cytokine signal transduction is essential for normal immune function and controls the quality of responses to a wide variety of microbial infections. Innate and adaptive host responses to virus infections are regulated by autocrine and paracrine cytokine signaling systems. For most cytokines, receptor binding triggers an intracellular signaling cascade involving one or more signal transducer and activator of transcription (STAT) proteins. Diverse cytokine and growth factor signaling pathways produce active STAT transcription factors that specify mRNA induction profiles (26). For example, the alpha and beta interferon (IFN-α/β) family is of primary importance for both innate and adaptive antiviral immunity (reviewed in references 1, 49, and 53). In the innate antiviral system, IFN-α/β initiates a receptor-mediated signaling system that produces an activated STAT1-STAT2-IRF9 heterotrimeric transcription complex known as ISGF3 (27). The ISGF3 complex translocates to the nucleus, where it can ...

Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.. The complexity of canonical Wnt signaling comes not only from the numerous components but also from multiple post-translational modifications. Protein phosphorylation is one of the most common modifications that propagates signals from extracellular stimuli to downstream effectors. To investigate the global phosphorylation regulation and uncover novel phosphoproteins at the early stages of canonical Wnt signaling, HEK293 cells were metabolically labeled with two stable isotopic forms of lysine and were stimulated for 0, 1, or 30 min with purified Wnt3a. After phosphoprotein enrichment and LC-MS/MS analysis, 1057 proteins were identified in all three time points. In total 287 proteins showed a 1.5-fold or greater change in at least one time point. In addition to many known Wnt signaling transducers, other phosphoproteins were identified and quantitated, implicating their ...

ARPP21 overexpression lysate, 0.1 mg. Transient overexpression lysate of cyclic AMP-regulated phosphoprotein, 21 kD (ARPP-21), transcript variant 4

Procaspase-8, the zymogen type of the apoptosis-initiator caspase-8, undergoes phosphorylation following integrin-mediated cell connection to an extracellular matrix base. CrkII and Crk, each bearing an Src-homology 2 domains (SH2) and one or two Src homology 3 (SH3) websites, respectively. CrkL (and knockouts display cardiac and sensory crest flaws, ending in embryonic lethality.17,18 Here, we offer proof that caspase-8 interacts with the You will need2 domains of CrkL in a Src- and adhesion-dependent way, and that this connections stimulates cellular migration. Outcomes Caspase-8 interacts with CrkL SH2 domains We observed the de novo phosphorylation of many protein, in caspase-8 showing cells selectively, pursuing cell adhesion to fibronectin substrates. These included a phosphoprotein at ~37 kDa (Fig.?1A). To determine whether the phosphoprotein may end up being component of a complicated linked with the caspase, caspase-8 immunoprecipitations had been performed by us, solved the necessary ...

SLP76 (SH2 domain-containing leukocyte protein of 76 kDa) is a cytosolic adaptor protein which translocates to the plasma mambrane and is involved in multiple signaling pathways in T cells, mast cells, neutrophils and platelets; B cells express its analog SLP65/BLNK (B cell linker protein). SLP76 is phosphorylated by Syk-family and Tec-family tyrosine kinases and couples them to the phosphorylation and activation of PLC-gamma. Via Gads or Grb2, SLP76 also associates with LAT adaptor by involvement of SLP76 proline-rich region. The SH2 domain of SLP76 has been identified as the region involved in binding the serine/threonine kinase HPK1. HPK1 may act as both a positive and a negative regulator by promoting the Jnk-mitogen activated protein kinase (MAPK) pathway and inhibiting the pathway leading to AP-1 activation ...

RecName: Full=Ezrin-radixin-moesin-binding phosphoprotein 50; Short=EBP50; AltName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF; AltName: Full=NHERF-1; AltName: Full=Regulatory cofactor of Na(+)/H(+) exchanger; AltName: Full=Sodium-hydrogen exchanger regulatory factor 1; AltName: Full=Solute carrier family 9 isoform A3 regulatory factor 1 ...

The adaptor protein Src homology 2 domain-containing leukocyte phosphoprotein of 76 kDa (SLP-76) plays a crucial role in T cell activation by linking antigen receptor (T cell receptor, TCR) signals to downstream pathways ...

Protein phosphorylation affects most, if not all, cellular activities in eukaryotes and is essential for cell proliferation and development. An estimated 30% of cellular proteins are phosphorylated, representing the phosphoproteome, and phosphorylation can alter a proteins function, activity, local …

TP53 / p53 (C-Terminus) antibody | P04637 | Cellular tumor antigen p53, Antigen NY-CO-13, Phosphoprotein p53, Tumor suppressor p53, TP53, P53

Stimulation of beta2-adrenergic receptors on the cell surface by adrenaline or noradrenaline leads to alterations in the metabolism, excitability, differentiation and growth of many cell types. These effects have traditionally been thought to be mediated exclusively by receptor activation of intrace …

VASP - VASP (untagged)-Human vasodilator-stimulated phosphoprotein (VASP) available for purchase from OriGene - Your Gene Company.

This gene encodes a member of the paralemmin protein family. The product of this gene is a prenylated and palmitoylated phosphoprotein that associates with the cytoplasmic face of plasma membranes and is implicated in plasma membrane dynamics in neurons and other cell types. Several alternatively spliced transcript variants have been identified, but the full-length nature of only two transcript variants has been determined. [provided by RefSeq, Jul 2008 ...

VASP (phospho Ser239) antibody (vasodilator-stimulated phosphoprotein) for IHC-P, WB. Anti-VASP (phospho Ser239) pAb (GTX38661) is tested in Human, Mouse samples. 100% Ab-Assurance.

Protein phosphorylation significantly impacts protein function. Find products, protocols, articles and pathways for protein phosphorylation research.

The Vasp Tetramerization Domain is a Right-Handed Coiled Coil Based on a 15-Residue Repeat.. PubMed ID: 15-569-942. From NIHs 3D Print Exchange. ...

GO:0072332. A series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, and ends when the execution phase of apoptosis is triggered. ...

This overview provides a history of protein phosphorylation research and provides the reader with an understanding of how and why labeling studies are performed

Phosphoflow analysis of phosphorylated proteins allows researchers a quick and effective way to measure signalling cascades in individual cells.

Fertilizer is a cost-effective solution to save you money, and Birchs Lawn Care is the premium fertilizer expert in the Tri-Cities, WA.

Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) is a prominent substrate for activated tyrosine kinase receptors that has been proposed to play a role in endosomal membrane trafficking. The protein contains a FYVE domain, which specifically binds to the lipid phosphatidylinositol (PI) 3-phosphate (PI 3-P). We show that this interaction is required both for correct localization of the protein to endosomes that only partially coincides with early endosomal autoantigen 1 and for efficient tyrosine phosphorylation of the protein in response to epidermal growth factor stimulation. Treatment with wortmannin reveals that Hrs phosphorylation also requires PI 3-kinase activity, which is necessary to generate the PI 3-P required for localization. We have used both hypertonic media and expression of a dominant-negative form of dynamin (K44A) to inhibit endocytosis; under which conditions, receptor stimulation fails to elicit phosphorylation of Hrs. Our results provide a clear example of the

Immune responses are initiated when molecules of microbial origin are sensed by the Toll-like receptors (TLRs). We now report the identification of essential molecular components for the trafficking of the lipopolysaccharide (LPS) receptor complex. LPS was endocytosed by a receptor-mediated mechanism dependent on dynamin and clathrin and colocalized with TLR4 on early/sorting endosomes. TLR4 was ubiquitinated and associated with the ubiquitin-binding endosomal sorting protein hepatocyte growth factor-regulated tyrosine kinase substrate, Hrs. Inhibition of endocytosis and endosomal sorting increased LPS signaling. Finally, the LPS receptor complex was sorted to late endosomes/lysosomes for degradation and loading of associated antigens onto HLA class II molecules for presentation to CD4+ T cells. Our results show that endosomal trafficking of the LPS receptor complex is essential for signal termination and LPS-associated antigen presentation, thus controlling both innate and adaptive immunity through

The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.

Abstract. RPLP1 is one of acidic ribosomal phosphoproteins encoded by RPLP1 gene, which plays an important role in the elongation step of protein synthesis. The cDNA of RPLP1 was cloned successfully for the first time from the Giant Panda (Ailuropoda melanoleuca) using RT-PCR technology, which was also sequenced, analyzed preliminarily and expressed in E.coli. The cDNA fragment cloned is 449bp in size, containing an open reading frame of 344bp encoding 114 amino acids. Alignment analysis indicated that the nucleotide sequence and the deduced amino acid sequence are highly conserved to other five species studied, including Homo sapiens, Mus musculus, Rattus norvegicus, Bos Taurus and Sus scrofa. The homologies for nucleotide sequences of Giant Panda PPLP1 to that of these species are 92.4%, 89.8%, 89.0%, 91.3% and 87.5%, while the homologies for amino acid sequences are 96.5%, 94.7%, 95.6%, 96.5% and 88.6%. Topology prediction showed there are three Casein kinase II phosphorylation sites and two ...

ABSTRACT: The Insulin Receptor Substrate (IRS) proteins are cytoplasmic adaptor proteins that function as essential signaling intermediates downstream of activated cell surface receptors, many of which have been implicated in cancer. The IRS proteins do not contain any intrinsic kinase activity, but rather serve as scaffolds to organize signaling complexes and initiate intracellular signaling pathways. As common intermediates of multiple receptors that can influence tumor progression, the IRS proteins are positioned to play a pivotal role in regulating the response of tumor cells to many different microenvironmental stimuli. Limited studies on IRS expression in human tumors and studies on IRS function in human tumor cell lines and in mouse models have provided clues to the potential function of these adaptor proteins in human cancer. A general theme arises from these studies; IRS-1 and IRS-4 are most often associated with tumor growth and proliferation and IRS-2 is most often associated with tumor

This protein, p55 , of a 55-kD erythrocyte membrane protein locus Xq28: [§§]; exon sizes range from 69 (exon 5) to 203 (exon 10) bp, is the prototype of a family of membrane-associated proteins that contains three distinct domains in its primary structure: estimates relative utilization of the three sites the binding sites for band 3. The interactions involving protein 4.1 with p55 and p55 with GPC/D that migrate in the region of band 4.9 in a directional fashion are of high affinity*(nM) termed MAGUKs (membrane-associated guanylate kinase homologs) with the FERM domain of protein 4.1R is the most extensively palmitoylated protein of the erythrocyte membrane a classical PDZ domain-to-PDZ binding motif (PBM) mechanism also designated as MPP1 FERM domain of NF2 protein. Human erythroid p55, a palmitoylated peripheral membrane phosphoprotein were used to map the protein 4.1 binding site on human erythroid glycophorin C, a transmembrane protein of red blood cells phosphorylation to the cell ...

Cloning, Expression and Hormonal Regulation of Steroidogenic Acute Regulatory Protein Gene in Buffalo Ovary - StAR Gene;StAR mRNA;Semi-quantitative RT-PCR;Granulosa Cells;Ovary;Buffalo;

Protein target information for Dentin matrix acidic phosphoprotein 1 (pig). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.

In eukaryotes, hundreds of protein kinases (PKs) specifically and precisely modify thousands of substrates at specific amino acid residues to faithfully orchestrate numerous biological processes, and reversibly determine the cellular dynamics and plasticity. Although over 100,000 phosphorylation sites (p-sites) have been experimentally identified from phosphoproteomic studies, the regulatory PKs for most of these sites still remain to be characterized. Here, we present a novel software package of iGPS for the prediction of in vivo site-specific kinase-substrate relations mainly from the phosphoproteomic data. By critical evaluations and comparisons, the performance of iGPS is satisfying and better than other existed tools. Based on the prediction results, we modeled protein phosphorylation networks and observed that the eukaryotic phospho-regulation is poorly conserved at the site and substrate levels. With an integrative procedure, we conducted a large-scale phosphorylation analysis of human ...

Characterization of the Borna disease virus phosphoprotein, p23.: Borna disease virus infection is diagnosed by the presence of serum antibodies reactive with t

The polymerization-inducing activity of the p48 integral membrane protein does not require an intact bilayer, and so we were able to harvest vesicles from S100, solubilize the membrane proteins with detergents, separate them by size exclusion chromatography and recombine fractions at each step with cytosol to assay for filament formation. The requirement for tyrosine phosphorylation provided a convenient, complementary biochemical assay. At each step in fractionation, we found that fractions that induced MSP polymerization in cytosol also contained phosphorylated p48 on western blots. In most preparations of vesicles, p48 was the only protein that labeled with antiphosphotyrosine. Some preparations also contained a minor reactive band at Mr ∼68 kDa. The sequence of a 20 amino acid peptide fragment of this protein matched that of flavoprotein subunit II of fumarate reductase, a 67.9 kDa mitochondrial enzyme from Ascaris that contains phosphotyrosine residues (Kuramochi et al., 1994). Thus, the ...

Complex brain functions, such as learning and memory, are believed to involve changes in the efficiency of communication between nerve cells. Therefore, the elucidation of the molecular mechanisms that regulate synaptic transmission, the process of intercellular communication, is an essential step toward understanding nervous system function. Several proteins associated with synaptic vesicles, the organelles that store neurotransmitters, are targets for protein phosphorylation and dephosphorylation. One of these phosphoproteins, synapsin I, by means of changes in its state of phosphorylation, appears to control the fraction of synaptic vesicles available for release and thereby to regulate the efficiency of neurotransmitter release. This article describes current understanding of the mechanism by which synapsin I modulates communication between nerve cells and reviews the properties and putative functions of other phosphoproteins associated with synaptic vesicles. ...

Primary Objective 1: Determine changes in tumor EGFR, pEGFR, downstream signaling and novel phosphoproteins following a loading dose of cetuximab in patients who are poor candidates for chemoradiation (age =70 years or with significant co-morbidities) and are therefore treated with cetuximab with radiation.. Primary Objective 2: Characterize clinical outcomes, including local recurrence, progression-free survival and overall survival in these patients, and correlate these clinical outcomes with the changes in tumor EGFR, pEGFR, downstream signaling, and novel phosphoproteins.. Primary Objective 3: Describe the toxicity, in particular mucositis/dysphagia, of this regimen.. Secondary Objective 1: Conduct normal mucosa EGFR assessment for comparison with tumor sample.. Secondary Objective 2: Correlate HPV presence and titer with p53 status and clinical outcome. ...

Two-dimensional gel electrophoresis of nuclear phosphoproteins of Novikoff hepatoma and regenerating liver.: Two-dimensional polyacrylamide gel electrophoresis

Integrins interact with extracellular matrix (ECM) and deliver intracellular signaling for cell proliferation, survival, and motility. During tumor metastasis, integrin-mediated cell adhesion to and migration on the ECM proteins are required for cancer cell survival and adaptation to the new microenvironment. Using stable isotope labeling by amino acids in cell culture-mass spectrometry, we profiled the phosphoproteomic changes induced by the interactions of cell integrins with type I collagen, the most common ECM substratum. Integrin-ECM interactions modulate phosphorylation of 517 serine, threonine, or tyrosine residues in 513 peptides, corresponding to 357 proteins. Among these proteins, 33 key signaling mediators with kinase or phosphatase activity were subjected to small interfering RNA-based functional screening. Three integrin-regulated kinases, DBF4, PAK2, and GRK6, were identified for their critical role in cell adhesion and migration possibly through their regulation of actin ...

T cells play a central role in immune responses mounted against pathogens and cancer. Dramatic cytoskeletal reorganization during T cell activation is a prerequisite for a specific immune response (for references see Penninger and Crabtree 1999). Upon binding to an antigen-presenting cell (APC), the cytoskeleton of a T cell rapidly polarizes. The accumulation of actin in a tight collar at the T cell-APC interface is thought to stabilize a continuous contact between T cells and APCs (Ryser et al. 1982; Valitutti et al. 1995). The formation of this tight contact is accompanied by the reorientation of the microtubule-organizing center towards the contact site to ensure a polarized release of cytokines or cytotoxic factors (Geiger et al. 1982; Kupfer et al. 1987, Kupfer et al. 1991). Although actin remodeling is thought to be essential for T cell activation (see Penninger and Crabtree 1999), it is not known how T cell receptor (TCR) signaling is linked to the rearrangement of the actin ...

FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a protein with a C-terminal Sprouty-like cysteine-rich domain (SRY) and an N-terminal Ena/Vasodilator-stimulated phosphoprotein (VASP) homology-1 (EVH-1) domain. The encoded protein is a member of a family of proteins that negatively regulates mitogen-activated protein (MAP) kinase signaling, particularly during organogenesis. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2012 ...

The KOMP Repository is located at the University of California Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...

Kettenbach AN, et al. (2011) Quantitative phosphoproteomics identifies substrates and functional modules of aurora and polo-like kinase activities in mitotic cells. Sci Signal 4, rs5 ...

Kettenbach AN, et al. (2011) Quantitative phosphoproteomics identifies substrates and functional modules of aurora and polo-like kinase activities in mitotic cells. Sci Signal 4, rs5 ...

(2013) Schokoroy et al. PLoS ONE. Background:The ErbB receptors, Ras proteins and nucleolin are major contributors to malignant transformation. The pleiotropic protein nucleolin can bind to both Ras protein and ErbB receptors. Previously, we have demonstrated a crosstalk between Ras, nucleolin an...

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

c-Myc, 0.1 ml. c-Myc is a multifunctiol, nuclear phosphoprotein that plays a role in cell cycle progression, apoptosis and cellular transformation.

The BRCA-1 antibody gene codes for a nuclear phosphoprotein that plays a role in maintaining genomic stability and acts as a tumor suppressor.

Tyrosine, 3-isobutyl-1-methylxanthine, Antibodies, Cells, Dbcamp, Ibmx, Immunoblotting, Kinase, Phosphoproteins, Phosphorylation, Proteins, Serine, Sperm, Threonine, Time

购买我们的小鼠Paxillin (phospho S83)肽。ab42724可作为ab31833的封闭肽并经过Blocking, ELISA实验验证。Abcam提供免费的实验方案，操作技巧及专业的支持。