Anti-Canine CD45 FITC 25 tests
- Known as:
- Antibody toCanine CD45 fluorecein 25 tests
- Catalog number:
- 11-5450-41
- Category:
- -
- Supplier:
- eBioscience
- Gene target:
- Anti-Canine CD45 FITC 25 tests
Related genes to: Anti-Canine CD45 FITC 25 tests
- Gene:
- PTPRC NIH gene
- Name:
- protein tyrosine phosphatase receptor type C
- Previous symbol:
- CD45
- Synonyms:
- LCA, T200, GP180
- Chromosome:
- 1q31.3-q32.1
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-04-23
- Gene:
- PTPRCAP NIH gene
- Name:
- protein tyrosine phosphatase receptor type C associated protein
- Previous symbol:
- -
- Synonyms:
- LPAP, CD45-AP
- Chromosome:
- 11q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1996-04-22
- Date modifiied:
- 2019-02-14
Related products to: Anti-Canine CD45 FITC 25 tests
Alkaline Phosphatase Conjugated Affinity Purified anti-Swine IgG (H&L) [Goat] Secondary_Antibodies(Deamino_Phe19,D_Ala24,D_Pro26_(®)_Phe27)_GRP (19_27) (human, porcine, canine) Salt Trifluoroacetate Binding _ Synonym BW_10 SumFormula C57H72N14O8(Deamino_Phe19,D_Ala24,D_Pro26_(®)_Phe27)_GRP (19_27) (human, porcine, canine) Salt Trifluoroacetate Binding _ Synonym BW_10 SumFormula C57H72N14O8(Draxin) C1ORf187 FITC-conjugates: Drax-FITC Host: Rabbit Affinity purifed(Draxin) C1ORf187, FITC conjugates(endo,anti)_((FITC-conjugates) Dopamine D2 Receptor Immunogen: peptide Host: Rabbit(FITC-conjugates) Glucose Transporter 1 Immunogen: peptide Host: Rabbit(FITC-conjugates) PDE3A(goat) Immunogen: peptide Host: Rabbit(FITC-conjugates) PDE7A(Goat) Immunogen: peptide (23mer) Host: Rabbit(FITC-conjugates) Phospho-calcium channel 2A subunit Immunogen: peptide Host: Rabbit(FITC-conjugates) Phospho-cyclic 5'-nucleotidase Immunogen: peptide Host: Rabbit(FITC-conjugates) Phospho-Erb 2 Immunogen: peptide Host: Rabbit(FITC-conjugates) Phospho-INAD antibody Immunogen: peptide Host: Rabbit(FITC-conjugates) Phospho-Kip Immunogen: peptide Host: Rabbit Related articles to: Anti-Canine CD45 FITC 25 tests
- Vulvar lichen planus (VLP) is a chronic inflammatory disease which adversely affects patients' quality of life. The pathogenesis of VLP is unknown although Th1 immune response has been implicated. We aimed to discover specific tissue-based protein biomarkers in VLP compared to normal vulvar tissue (NVT), vulvar lichen sclerosus (VLS) and oral lichen planus (OLP). We used laser capture microdissection-liquid chromatography- tandem mass spectrometry to assess protein expression in fixed lesional mucosal specimens from patients with VLP (n = 5). We then compared proteomic profiles against those of NVT (n = 4), VLS (n = 5), OLP (n = 6) and normal oral mucosa (n = 5), previously published by our group. IL16, PTPRC, PTPRCAP, TAP1 and ITGB2 and were significantly overexpressed in VLP compared to NVT. Ingenuity pathway analysis identified antigen presentation and integrin signalling pathways. Proteins overexpressed in both VLP versus NVT and OLP versus NOM included IL16, PTPRC, PTPRCAP, TAP1, HLA-DPB1, HLA-B and HLA-DRA. This proteomic analysis revealed several overexpressed proteins in VLP that relate to Th1 autoimmunity, including IL16. Overlapping pathways, including those involving IFNγ and Th1 signalling, were observed between VLP, VLS, and OLP. - Source: PubMed
Publication date: 2023/06/15
Xie FangyiDasari SurendraDeschaine MariaGleue Casey ASartori-Valinotti Julio CTorgerson Rochelle RDavis Mark D PCharlesworth M CristineMeves AlexanderLehman Julia S - Lymphocyte phosphatase-associated phosphoprotein (LPAP) is a small transmembrane protein that is found in lymphocytes and is tightly associated with the phosphatase CD45. The function of LPAP is still unknown. Studies of the LPAP interactome may reveal new details of how C45 and lymphocyte signaling in general are regulated. LPAP binding partners were sought using coimmunoprecipitation coupled with mass spectrometry, stabilization of protein complexes with chemical crosslinkers, and Blue Native electrophoresis. In addition to CD45, several proteins were identified as LPAP partners, including CD71, CD98, cytoskeletal proteins, the amino acid transporter SLC1A4, and the cell signaling component HS1. It was confirmed that more than 70% of LPAP molecules were bound with CD45 in a 1 : 1 complex. The effect of CD45 on LPAP was studied in CEM and Jurkat cells with a CD45 knockout. The LPAP levels in the cells were 10% of the level in wild-type cells. In the absence of CD45, LPAP phosphorylation at Ser-153 and Ser-163 was not affected, whereas phosphorylation at Ser-99 and Ser-172 decreased significantly. Based on the results, CD45 was assumed to play a role in regulating LPAP expression and phosphorylation status. - Source: PubMed
Kruglova N AKopylov A TFilatov A V - Lymphocyte phosphatase-associated phosphoprotein (LPAP) is a molecular partner of CD45 phosphatase that plays a key role in the regulation of antigen-specific activation of lymphocytes. The functions of LPAP still remain unknown. We believe that studying LPAP phosphorylation pathways could shed light on its functions. In this work, we studied the phosphorylation of LPAP ectopically expressed in non-lymphoid cells in order to determine the effect of LPAP interaction partners on its phosphorylation. We found that phosphorylation at Ser153 and Ser163 in non-hematopoietic HEK293 cells was conserved, while phosphorylation at Ser99 and Ser172 was almost absent. The pattern of LPAP phosphorylation in K562 erythroid and U937 myeloid cells expressing endogenous CD45 protein was similar to that observed in T and B lymphocytes. We demonstrated for the first time that LPAP is a substrate for protein kinase CK2 that phosphorylates it at Ser153, presumably ensuring LPAP resistance to degradation. - Source: PubMed
Tsoy T DKruglova N AFilatov A V - PTPRCAP (CD45-AP) is a positive regulator of protein tyrosine phosphatase PTPRC (CD45), which activates Src family kinases implicated in tumorigenesis. Single-nucleotide polymorphism (SNP) rs869736 located at position -309 of the PTPRCAP promoter was associated with susceptibility to diffuse-type gastric cancer in the current case-control study. The minor-allele homozygote was significantly associated with a 2.5-fold increased susceptibility to diffuse-type gastric cancer (P = .0021, n = 252), but not to intestinal-type (P = .30, n = 178), versus the major-allele homozygote, when comparing unrelated Korean patients with healthy controls (n = 406). Nine other SNPs were in nearly perfect linkage disequilibrium (r(2) >or= 0.97) with this SNP, exhibiting the same association, and spread out for 26 kb on chromosome 11q13.1 covering RPS6KB2, PTPRCAP, CORO1B, and GPR152. Among the four genes, however, only PTPRCAP expression was affected by haplotypes of the 10 SNPs. Endogenous transcript levels of PTPRCAP were linearly correlated with copy numbers (0, 1, and 2) of the risk-haplotype (P = .0060) in 12 lymphoblastoid cells derived from blood samples, but those of the other three genes were not. Furthermore, the cancer-risk, minor-allele T of rs869736 increased both promoter activity and specific nuclear protein-binding affinity than the nonrisk, major-allele G in luciferase reporter and electrophoretic mobility shift assays, respectively. Accordingly, the minor allele of rs869736 in the PTPRCAP promoter is associated with increased susceptibility to diffuse-type gastric cancer by increasing PTPRCAP expression, possibly leading to activation of the oncogenic Src family kinases. - Source: PubMed
Ju HyoungseokLim ByunghoKim MinjinKim Yong SungKim Woo HoIhm ChunhwaNoh Seung-MooHan Dong SooYu Hang-JongChoi Bo YoulKang Changwon - Intermolecular complexes produced by the CD4 molecule were studied. To preserve the integrity of weak protein-protein interactions of the CD4 antigen, cells were lysed in a mild nonionic detergent Brij97. Protein constituents of the complex were identified by our previously proposed fluorescence immunoprecipitation assay with subsequent mass spectrometry. In total, 26 proteins associated with CD4 were identified on CEM cells. The CD4 complex included the following major components: tyrosine phosphatase CD45, transferrin receptor CD71, tyrosine kinase Lck, and a lymphocyte phosphatase-associated phosphoprotein LPAP. The CD4 complex also contained some components of cytoskeleton and heat shock proteins. The association between CD4, CD71, and CD45 molecules was confirmed by immunoblotting. The CD4 complexes were not detected on the U937 myeloid cells lacking Lck and LPAP. We attempted to quantitatively characterize the CD4 complex composition. - Source: PubMed
Krotov G IKrutikova M PZgoda V GFilatov A V