Anti-Mouse/Human CD49d (Clone PS/2) – Purified in vivo PLATINUM™ Functional Grade

P815 DBA/2 murine mastocytoma cells.

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.

Functional grade preclinical antibodies are manufactured in an animal free facility using in vitro cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.

To protect mouse colonies from infection by pathogens and to assure that experimental preclinical data is not affected by such pathogens, all of Leinco’s Purified Functional PLATINUM^TM antibodies are tested and guaranteed to be negative for all pathogens in the IDEXX IMPACT I Mouse Profile.

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.

Next Day 2-8°C

FA, IHC

PS/2 activity is directed against mouse CD49d and is cross reactive against human CD49d.

CD49d is expressed on T cells, B cells, NK , dendritic cells, thymocytes, monocytes, eosinophils, mast cells.

Integrins are a large family of heterodimeric transmembrane molecules that mediate adhesion, migration, cell survival, and cell differentiation. CD49d is a single-pass type I membrane glycoprotein also known as integrin alpha-4 (Uniprot Accession P13612). CD49d is the α4 subunit of integrin heterodimers alpha-4/beta-1 (VLA-4; CD49d/CD29; α4β1 integrin) and alph-4/beta-7 (LPAM-1)¹. These integrins act as receptors for fibronectin and VCAM1 (CD106). Integrin alpha-4/beta-7 is also a receptor for MADCAM1.

CD49d is expressed on most lymphocytes, granulocytes, monocytes, and thymocytes. CD49d/CD29 (VLA-4; α4β1) is expressed at high levels on the surface of lymphohematopoietic progenitors and is involved in their development and proliferation. CD49d/CD29 integrin/VCAM-1 interactions facilitate B cell adhesion to stromal cells and enhance B cell activation. In the absence of alpha-4 integrins, pre-B cells fail to transmigrate and proliferate.

PS/2 recognizes murine and human CD49d². PS/2 was generated by immunizing Fisher rats with P815 cells and subsequently fusing the spleen cells with Sp2/0. Hybridoma supernatants were screened by cell adhesion assay and cells producing blocking antibodies were cloned. Adhesion is blocked in a dose dependent manner when PS/2 is used with P815 and +/+ 2.4 stromal cells. 70Z/3 cells are also sensitive to PS/2 inhibition. PS/2 is known to block binding of CD49d to its ligands³. Lymphocyte production is completely blocked when PS/2 is included in Whitlock-Witte culture². PS/2 is IgG2b κ.

Fibronectin, VCAM-1, MAdCAM-1

Lymphocyte migration, T cell activation, stem cell differentiation.

1. Holzmann B, Weissman IL. EMBO J. 8(6):1735-1741. 1989.
2. Miyake K, Weissman IL, Greenberger JS, et al. J Exp Med. 173(3):599-607. 1991.
3. Andrew DP, Berlin C, Honda S, et al. J Immunol. 153(9):3847-3861. 1994.
4. Miyake K, Medina K, Ishihara K, et al. J Cell Biol. 114(3):557-565. 1991.
5. Enghofer M, Bojunga J, Ludwig R, et al. Am J Physiol. 274(5):E928-E935. 1998.
6. Hokibara S, Takamoto M, Isobe M, et al. Clin Exp Immunol. 114(2):236-244. 1998.
7. Fukuoka M, Fukudome K, Yamashita Y, et al. Blood. 96(13):4267-4275. 2000.
8. Omenetti S, Brogi M, Goodman WA, et al. Cell Mol Gastroenterol Hepatol. 1(4):406-419. 2015.
9. Chung KJ, Chatzigeorgiou A, Economopoulou M, et al. Nat Immunol. 18(6):654-664. 2017.
10. Tanneau GM, Hibrand-Saint Oyant L, Chevaleyre CC, et al. J Histochem Cytochem. 47(12):1581-1592. 1999.
11. Tchilian EZ, Owen JJ, Jenkinson EJ. Immunology. 92(3):321-327. 1997.
12. Liu ZJ, Tanaka Y, Fujimoto H, et al. J Immunol. 163(9):4901-4908. 1999.
13. Bellingan GJ, Xu P, Cooksley H, et al. J Exp Med. 196(11):1515-1521. 2002.
14. Bowden RA, Ding ZM, Donnachie EM, et al. Circ Res. 90(5):562-569. 2002.
15. Hirata T, Furie BC, Furie B. J Immunol. 169(8):4307-4313. 2002.
16. Maus UA, Srivastava M, Paton JC, et al. J Immunol. 173(2):1307-1312. 2004.
17. Eshghi S, Vogelezang MG, Hynes RO, et al. J Cell Biol. 177(5):871-880. 2007.
18. Li W, Ishihara K, Yokota T, et al. Glycobiology. 18(1):114-124. 2008.
19. Vaz R, Martins GG, Thorsteinsdóttir S, et al. Cell Tissue Res. 348(3):569-578. 2012.
20. Zhang Y, Chen YC, Krummel MF, et al. J Immunol. 189(8):3914-3924. 2012.
21. Sens C, Altrock E, Rau K, et al. J Bone Miner Res. 32(1):70-81. 2017.