Anti-Mouse CD105 (Endoglin) - Purified in vivo PLATINUMTM Functional Grade

Leinco Technologies
Product Code: LEI-C912
Product Group: Primary Antibodies
CodeSizePrice
LEI-C912-1.0mg1.0 mg£283.00
Quantity:
LEI-C912-5.0mg5.0 mg£456.00
Quantity:
LEI-C912-25mg25 mg£1,335.00
Quantity:
LEI-C912-50mg50 mg£1,938.00
Quantity:
LEI-C912-100mg100 mg£2,741.00
Quantity:
Prices exclude any Taxes / VAT

Overview

Host Type: Rat
Antibody Isotype: IgG2a κ
Antibody Clonality: Monoclonal
Antibody Clone: MJ7/18
Regulatory Status: RUO
Target Species: Mouse
Applications:
  • Agonism
  • Enzyme-Linked Immunosorbent Assay (ELISA)
  • Flow Cytometry
  • Immunofluorescence (IF)
  • Immunohistochemistry (IHC)
  • Immunohistochemistry- Frozen Section (IHC-F)
  • Immunoprecipitation (IP)
  • In Vivo Assay
  • Life Cell Imaging
  • Western Blot (WB)
Storage:
Functional grade preclinical antibodies may be stored sterile as received at 2-8°C for up to one month. For longer term storage aseptically aliquot in working volumes without diluting and store at -70°C. Avoid Repeated Freeze Thaw Cycles.

Further Information

Concentration:
? 5.0 mg/ml
Conjugate/Tag/Label:
Purified in vivo Functional Grade, in vivo PLATINUM™
Format:
This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.
Formulation:
This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.
Immunogen:
Inflamed mouse skin
Long Description:
CD105 (endoglin) is a TGF-β superfamily co-receptor that promotes angiogenesis, is involved in endothelial integrin-mediated mural cell and leukocyte adhesion, antagonizes TGF-β mediated ERK activation, is essential to the immune response of macrophages, regulates trophoblast differentiation and invasion during pregnancy, promotes T-cell proliferation, and regulates differentiation and collagen expression in myofibroblasts1. CD105 is dysregulated in the vasculature of multiple diseases including cancer, preeclampsia, and hereditary hemorrhagic telangiectasia. Additionally, increased soluble CD105 is associated with numerous cardiovascular pathologies and metabolic disorders with some CD105 polymorphisms being associated with increased risk of cardiovascular damage. CD105 is an effective marker of the tumor vasculature and is a target for early cancer diagnosis and antiangiogenic therapies. CD105 is alternatively spliced, resulting in both long (L-endoglin) and short (S-endoglin) forms1. The predominant isoform, L-endoglin, promotes the proliferation and migration of endothelial cells via enhanced ALK1-Smad1/5 signaling and is the presumed isoform when not specified in the literature. In contrast, S-endoglin enhances ALK5-Smad2/3 signaling. Endoglin has specific receptor-ligand interactions between type I and type II TGF-β superfamily receptors when binding TGF-β superfamily ligands. Mouse CD105 has three separate regions of similarity to TGF-β receptor III but does not contain the RGD tripeptide found in human CD1052. MJ7/18 was produced by immunizing rats with inflamed mouse skin and selecting for reactivity with endothelial cells2, 3. MJ7/18 predominantly stains vascular endothelial cells and is a marker of mouse endothelium2, 4.
NCBI Gene:
2022
Purity:
?98% monomer by analytical SEC, >95% by SDS Page
Target:
CD105

References

1. Pawlak JB, Blobe GC. Dev Dyn. 251(1):137-163. 2022. 2. Ge AZ, Butcher EC. Gene. 138(1-2):201-206. 1994. 3. Berg EL, Goldstein LA, Jutila MA, et al. Immunol Rev. 108:5-18. 1989. 4. Hallmann R, Mayer DN, Berg EL, et al. Dev Dyn. 202(4):325-332. 1995. 5. Charbord P, Oostendorp R, Pang W, et al. Exp Hematol. 30(10):1202-1210. 2002. 6. Rivera LB, Brekken RA. J Cell Biol. 193(7):1305-1319. 2011. 7. Romero D, O'Neill C, Terzic A, et al. Cancer Res. 71(10):3482-3493. 2011. 8. Kruse A, Hallmann R, Butcher EC. Biol Reprod. 61(6):1393-1401. 1999. 9. Redaelli CA, Semela D, Carrick FE, et al. J Hepatol. 40(2):305-312. 2004. 10. Arguello AA, Fischer SJ, Schonborn JR, et al. Neuroscience. 159(3):1003-1010. 2009. 11. Izawa D, Tanaka T, Saito K, et al. Int Immunol. 11(12):1989-1998. 1999. 12. Lidington EA, Rao RM, Marelli-Berg FM, et al. Am J Physiol Cell Physiol. 282(1):C67-74. 2002. 13. Garton KJ, Gough PJ, Philalay J, et al. J Biol Chem. 278(39):37459-37464. 2003. 14. Kinderlerer AR, Pombo Gregoire I, Hamdulay SS, et al. Blood. 113(7):1598-1607. 2009. 15. Marelli-Berg FM, Peek E, Lidington EA, et al. J Immunol Methods. 244(1-2):205-215. 2000. 16. Ahmad SR, Lidington EA, Ohta R, et al. Immunology. 110(2):258-268. 2003. 17. Karmani L, Bouchat V, Bouzin C. Nanomedicine (Lond). 9(13):1923-1937. 2014. 18. Karmani L, Lev?que P, Bouzin C, et al. Nucl Med Biol. 43(7):415-423. 2016. 19. Engelhardt B, Conley FK, Butcher EC. J Neuroimmunol. 51(2):199-208. 1994.