Recombinant Human ICAM-4 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human Integrin alpha L beta 2
(Catalog #
3868-AV) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human ICAM-4 Fc Chimera (Catalog
# 10407-IC) binds with an ED 50 of 0.25-1.5 μg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human ICAM-4 protein Human ICAM-4 (Ala31-Ala240) Accession # Q14773.1 | DIEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Ala31 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
50 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
50-60 kDa & 70-80 kDa, under reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 400 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human ICAM-4 Fc Chimera Protein, CF
Background
ICAM-4 (intercellular adhesion molecule-4), also known as CD242,
is a transmembrane cell adhesion glycoprotein and a member of the
immunoglobulin protein superfamily. The ICAM sub-family consists of five
members, ICAM-1 through ICAM-5, and they vary in their tissue expression and
number of Ig-like domains in the extracellular domain (ECD) (1). Full-length human
ICAM-4 contains 2 Ig-like domains in the ECD, a single transmembrane domain and
short intracellular domain. Alternative splicing of ICAM-4 results in at least
one soluble form (2). The ECD of mature human ICAM-4 shares 68% and 67% amino
acid sequence identity with mouse and rat ICAM-4, respectively. ICAM-4 expression
is limited to erythroid and possibly placental tissue but its biological role
remains poorly defined (3). ICAM-4 has
been shown to bind alpha 4 beta 1 and alpha V family
integrins as well as displaying broad ligand binding specificity for some beta 1,
beta 2, beta 3 and beta 5 integrins (4, 5). ICAM-4 binding
to endothelial alpha v beta 3 has been indicated as a factor in vaso-occlusion,
particularly in sickle cell disease (6). ICAM-4 is expressed on red blood cells
(RBC), erythroid precursor cells, and possibly placental tissue (3, 7). ICAM-4 has shown to bind alpha 4 beta 1
on hemopoietic cells, alpha V family integrins (avb1, avb3,
and avb5)
on non-hemopoietic cells as well as displaying broad ligand binding specificity
for some beta 1, beta 2, beta 3 and beta 5
integrins (4, 5, 7). Studies have shown aLb2 integrin interacts through the first
Ig-like domain of ICAM-4, whereas aMb2 and aXb2 integrins interact through both Ig-like
domains of ICAM-4 (7). In addition, initiation of vaso-occlusion in sickle cell
disease is implicated by ICAM-4 binding to endothelial alpha v beta 3 integrin (6). The ability of ICAM-4 to interact selectively
with different integrins suggests its importance in RBC physiology and
pathology as well as its therapeutic value.
- Gahmberg, C.G. et al. (1997) Eur. J. Biochem. 245, 215.
- Lee, G. et al. (2003) Blood 101:1790.
- Southcott, M.J.G. et al. (1999) Blood 93:4425.
- Spring, F.A. et al. (2001) Blood. 98:458.
- Hermand, P. et al. (2003) J Biol Chem. 278:4892.
- Kaul, D.K. et al. (2006) Am J Physiol Cell Physiol. 291:C922.
- Ihanus, E. et al. (2007) Blood 109:802.
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