Ensuring timely antibody delivery in the face of supply chain challenges - contact us for solutions

Mouse Anti-Human CD11a-LE/AF (38)

Cat. No.:
Low Endotoxin/Azide Free Anti-Human CD11a antibody for use in flow cytometry, immunohistochemistry, immunoprecipitation, ELISA, blocking, and adhesion assays.
Size Price (USD) Quantity
0.5 mg $314.00
More Information
Clone 38
Isotype Mouse (BALB/c) IgG2aκ
Isotype Control Mouse IgG2a-LE/AF (HOPC-1)
Specificity Human CD11a
Alternative Names LFA-1α, integrin αL, ITGAL
Description CD11a, also known as leukocyte function-associated antigen-1 (LFA-1α), represents the 180 kDa integrin αL subunit which combines with the CD18 β2 integrin subunit to form the αLβ2 integrin heterodimer. It is expressed on lymphocytes, granulocytes, monocytes, and macrophages and is upregulated on activated T cells. CD11a mediates adhesion of lymphocytes to vascular endothelium and is involved in costimulation.
Immunogen Fibronectin purified monocytes
Conjugate LE/AF (Low Endotoxin/Azide Free)
Buffer Formulation Phosphate buffered saline, pH 7.4
Clonality Monoclonal
Concentration 0.5 mg/mL
Volume 1.0 mL
Recommended Storage 2-8°C; Handle under aseptic conditions
Applications Flow Cytometry – Quality tested 6
Immunohistochemistry-Frozen Sections – Reported in literature 7
Immunoprecipitation – Reported in literature 1
Blocking – Reported in literature 2-6
Adhesion – Reported in literature 2-6
ELISA – Reported in literature 8

RRID Number AB_2796733
Gene ID 3683 (Human)
Gene ID Symbol ITGAL (Human)
Gene ID Aliases CD11A; LFA-1; LFA1A
UniProt ID P20701 (Human
UniProt Name ITAL_HUMAN (Human)

Certificate of Analysis Lookup

Enter the Catalog Number and Lot Number for the Certificate of Analysis you wish to view

Need help with this product?
or call 800.722.2255
  1. 1. Dransfield I, Hogg N. Regulated expression of Mg2+ binding epitope on leukocyte integrin α subunits. EMBO J. 1989;8:3759-65. (IP)
  2. 2. Dransfield I, Cabañas C, Barrett J, Hogg N. Interaction of leukocyte integrins with ligand is necessary but not sufficient for function. J Cell Biol. 1992;116:1527-35. (Adhesion, Block)
  3. 3. Landis RC, McDowall A, Holness CL, Littler AJ, Simmons DL, Hogg N. Involvement of the "I" domain of LFA-1 in selective binding to ligands ICAM-1 and ICAM-3. J Cell Biol. 1994;126:529-37. (Adhesion, Block)
  4. 4. Holness CL, Bates PA, Littler AJ, Buckley CD, McDowall A, Bossy D, et al. Analysis of the binding site on intercellular adhesion molecule 3 for the leukocyte integrin lymphocyte function-associated antigen 1. J Biol Chem. 1995;270:877-84. (Adhesion, Block)
  5. 5. Porter JC, Hogg N. Integrin cross talk: activation of lymphocyte function-associated antigen-1 on human T cells alters α4β1- and α5β1-mediated function. J Cell Biol. 1997;138:1437-47. (Adhesion, Block)
  6. 6. Weerasinghe D, McHugh KP, Ross FP, Brown EJ, Gisler RH, Imhof BA. A role for the αvβ3 integrin in the transmigration of monocytes. J Cell Biol. 1998;142:595-607. (FC, Adhesion, Block)
  7. 7. Demetter P, van Huysse JA, de Keyser F, van Damme N, Verbruggen G, Mielants H, et al. Increase in lymphoid follicles and leukocyte adhesion molecules emphasizes a role for the gut in spondyloarthropathy pathogenesis. J Pathol. 2002;198:517-22. (IHC-FS)
  8. 8. Last-Barney K, Davidson W, Cardozo M, Frye LL, Grygon CA, Hopkins JL, et al. Binding site elucidation of hydantoin-based antagonists of LFA-1 using multidisciplinary technologies: evidence for the allosteric inhibition of a protein-protein interaction. J Am Chem Soc. 2001;123:5643-50. (ELISA)
See All References