Integrin alpha 4/CD49d Antibody (HP2/1) - BSA Free, Novus Biologicals™

Integrin alpha 4/CD49d

1 mg/mL

Flow Cytometry, Immunohistochemistry, Immunohistochemistry (Frozen), Immunoprecipitation

Unconjugated

Mouse

Cancer, Cellular Markers, Cytoskeleton Markers

P13612

3676

JM leukaemia line (Human).

Primary

Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.

HP2/1

Flow Cytometry 1ug/5 x 10^5 cells, Immunohistochemistry 1:10-1:500, Immunoprecipitation 1:10-1:500, Immunohistochemistry-Frozen 1:10-1:500

Monoclonal

Purified

RUO

Human

269C wild type, CD49 antigen-like family member D, CD49d, CD49d antigen, CD49Dantigen CD49D, alpha-4 subunit of VLA-4 receptor, IA4, integrin alpha 4, integrin alpha-4, integrin alpha-4 subunit, Integrin alpha-IV, integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor), MGC90518, very late activation protein 4 receptor, alpha 4 subunit, VLA-4 subunit alpha

ITGA4

IgG1

Protein A or G purified

Mouse anti Human CD49d monoclonal antibody, clone HP2/1 recognizes human CD49d also known as integrin alpha-4 or VLA-4 subunit alpha. CD49d is a ∼150kDa single pass type 1 transmembrane glycoprotein with seven FG-GAP repeats, characteristic of alpha integrins, in its extracellular domain. CD49d can be proteolytically cleaved to yield framents of 80 and 70kDa (Hemler et al. 1987). CD49d associates with either CD29 to form VLA-4 or with Integrin beta-7 to form The Peyer patches-specific homing receptor LPAM-1, involved in the lymphocyte migration and homing to gut-associated lymphoid tissue (Sackstein 2006) through its interaction with MadCam-1, preferentially expressed on Peyer's patch high endothelial venules and postcapillary venules in lamina propria (Briskin et al. 1997). Mouse anti human CD49d, clone HP2/1 binds to both intact and the 80kDa fragment of integrin alpha-4. CD49d is expressed on monocytes, T cells, B cells, thymocytes and Langerhans cells (de Graaf et al. 1995). Mouse anti Human CD49d, clone HP2/1 can be used in basic studies of VLA-4 mediated adhesion and its interaction with the VCAM-1 structure and has been demonstrated to inhibit cell binding to soluble VCAM-1 (Weller et al. 1991).