Clone:
REAL273
Type of antibody:
Releasable fluorochromes, Primary antibodies, Recombinant antibodies
Applications:
MICS, IHC, IF
Alternative names:
VCAM1, INCAM-100

Specifications for CD106 (VCAM-1) Antibody, anti-human, REAdye_lease™

Overview

Clone REAL273 is an antibody fragment derived from the full CD106 (VCAM-1) antibody molecule. It displays no binding to Fc receptors. The recombinantly engineered antibody fragments are multimerized to form the REAdye_lease Complex to bind markers with high avidity.
Clone REAL273 recognizes the CD106 (VCAM-1) antigen, a 110 kDa single chain type I glycoprotein also known as vascular cell adhesion protein 1 (VCAM-1) or INCAM-100. CD106 is expressed on inflamed vascular endothelium, as well as on macrophage-like and dendritic cell types in both normal and inflamed tissue. Upregulation of CD106 in endothelial cells by inflammatory stimuli and cytokines occurs as a result of increased gene transcription. Primarily, CD106 is an endothelial ligand for very late antigen-4 (VLA-4) or integrin α-4/β-7 and mediates both adhesion and signal transduction. The interactions play a pathophysiologic role in leukocyte adhesion, transmigration, and co-stimulation of T cell proliferation.
For removal of REAdye_lease fluorochromes for optional relabeling with different fluorochrome-conjugated REAdye_lease antibodies use the REAlease Support Kit (130-120-675).

Alternative names

VCAM1, INCAM-100

Detailed product information

Technical specifications

CloneREAL273
Clonalitymonoclonal
Isotype controlControl Antibody
Hostcell line
Type of antibodyReleasable fluorochromes, Primary antibodies, Recombinant antibodies
Specieshuman
AntigenCD106 (VCAM-1)
Alternative names of antigenVCAM1, INCAM-100
Distribution of antigendendritic cells, endothelial cells, macrophages

Resources for CD106 (VCAM-1) Antibody, anti-human, REAdye_lease™

Certificates

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References for CD106 (VCAM-1) Antibody, anti-human, REAdye_lease™

Publications

  1. Osborn, L. et al. (1992) Activated endothelium binds lymphocytes through a novel binding site in the alternately spliced domain of vascular cell adhesion molecule-1. J. Exp. Med. 176(1): 99-107
  2. Barreiro, O. et al. (2002) Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes. J. Cell Biol. 157(7): 1233-1245
  3. Johnson, L. A. et al. (2008) Cell traffic and the lymphatic endothelium. Ann. N. Y. Acad. Sci. 1131: 119-133
  4. Schlesinger, M. et al. (2015) Vascular cell adhesion molecule-1 (VCAM-1)--an increasing insight into its role in tumorigenicity and metastasis. Int. J. Cancer 136(11): 2504-2514

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