Lymphocyte-Specific Protein 1 (LSP1) ELISA Kits

Mouse (Murine) Lymphocyte-Specific Protein 1 (LSP1) interaction partners

1. Regulation of O-GlcNAcylation and phosphorylation of lymphocyte-specific protein-1 (Lsp1) is a key switch that triggers apoptosis in activated B cells. O-GlcNAcylation at S209 of Lsp1 is a prerequisite for the recruitment of its kinase, PKC-beta1, to induce S243 phosphorylation.

2. the LSP1-myosin1e bimolecular complex plays a pivotal role in the regulation of actin cytoskeleton remodeling during Fc gamma receptor-driven phagocytosis.

3. the importance of LSP1 Copy number variations and LSP1 insufficiency in the pathogenesis of rheumatoid arthritis, is reported.

4. Data indicate that in lymphocyte specific 1 protein (LSP1)-deficient mice, PECAM-1 expression was reduced in endothelial cells, but not in neutrophils.

5. functions as a negative regulator of proliferation and migration in liver

6. TRAF1 and LSP1 cooperate downstream of 4-1BB to activate ERK signaling and down-modulate the levels of Bim leading to enhanced T cell survival.

7. Endothelial LSP1 participates in leukocyte adhesion in vitro, and leukocyte adhesion, through ICAM-1, fosters the activation of endothelial LSP1.

8. LSP1 plays an important role in leukocyte recruitment induced by both KC and MIP-2.

9. Data demonstrate that endothelial LSP1 is recruited to the cytoskeleton in inflammation and plays an important role in forming endothelial domes thereby regulating neutrophil transendothelial migration.

10. Lsp1 negatively regulates fMLP-induced polarization and chemotaxis of neutrophils during inflammation through its function on adhesion via specific integrins, such as Mac-1 (CD11b/CD18).

11. The results show a complex function of LSP1 in regulating leukocyte recruitment to inflamed sites.

12. MK2-regulated LSP1 phosphorylation is involved in stabilization of F-actin polarization during neutrophil chemotaxis.

13. These results demonstrate that the absence of LSP1 promotes healing of skin wounds.

14. the absence of LSP1 promotes fibrosis in the skin

Human Lymphocyte-Specific Protein 1 (LSP1) interaction partners

1. Differential gene expression by SFRP2(+), FMO1(+), and COL11A1(+) fibroblasts suggests roles in matrix deposition, inflammatory cell retention, and connective tissue cell differentiation, respectively.

2. LSP1 rs3817198 T > C polymorphism is associated with increased risk of breast cancer, especially in Caucasian and Asian populations [meta-analysis]

3. These results show that LSP1 is critical regulator of actomyosin contractility in primary macrophages.

4. Underexpression of LSP1 is associated with Breast Cancer Recurrence.

5. LSP1 rs569550 and rs592373 polymorphisms are both risk factors for breast cancer.

6. the importance of LSP1 Copy number variations and LSP1 insufficiency in the pathogenesis of rheumatoid arthritis, is reported.

7. The breast cancer SNP LSP1 rs3817198 was associated with an increased risk of lung cancer (odds ratio: 1.10) This association was strongest for women with adenocarcinoma (P = 1.2x10(-4)).

8. Data indicate that slit2N alters the localization and binding of Robo1 to WASp and LSP1 in HIV-1-gp120-treated immature dendritic cells (iDCs).

9. Single nucleotide polymorphism in LSP1 is associated with breast cancer.

10. The LSP1 rs3817198T>C polymorphism is a low-penetrant risk factor for developing breast cancer but may not be in Africans.

11. Low-risk variants of LSP1 is associated with familial breast cancer.

12. The LSP1 and 2q35 SNPs appear to interact multiplicatively on breast cancer risk for BRCA2 mutation carriers.

13. LSP1 interacts with F-actin and the cytoskeleton through residues downstream of amino acid residue 230. The cytoskeleton binding site of mouse LSP1 maps to the 300-330 interval.

14. Leukocyte-specific protein 1 is a cytoskeletal targeting protein for the ERK/MAP kinase pathway

15. LSP1 protein facilitates virus transport into the proteasome after its interaction with DC-SIGN through its interaction with cytoskeletal proteins.

16. MK2-regulated LSP1 phosphorylation is involved in stabilization of F-actin polarization during neutrophil chemotaxis.

17. DC-SIGN was constitutively associated with a signalosome complex consisting of the scaffold proteins LSP1, KSR1 and CNK and the kinase Raf-1