Recombinant Human CD97 His-tag Protein, CF Summary
Details of Functionality |
Measured by the ability of the immobilized protein to support the adhesion of human red blood cells. Hamann, J. et al. (1996) J. Exp. Med. 184:1185. The ED50 for this effect is 0.05-0.4 μg/mL.
|
Source |
Chinese Hamster Ovary cell line, CHO-derived human CD97 protein Gln21-Gln398, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
No results obtained. Gln21 is inferred from enzymatic pyroglutamate treatment revealing Asp22. |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>90%, 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 |
42 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 |
60-90 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 |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 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 CD97 His-tag Protein, CF
Background
CD97 is a member of
the epidermal growth factor-seven transmembrane (EGF-TM7) subfamily of G-protein
coupled receptors (1). Mature human CD-97 contains a large extracellular domain
(ECD) followed by 7 transmembrane domains. Alternative splicing encodes 3 isoforms of the ECD with varying numbers of EGF-like repeats (4). Isoform 1, being
the longest, contains 5 EGF-like domains, while isoform 2, which is described
in this insert, is missing amino acids (aa) 116-208, corresponding to EGF-like
domains 3 and 4. Mature isoform 2 of human
CD97 shares 50% aa identity with the mouse protein. The EGF-like domains
mediate binding to chondroitin sulfate and the complement regulatory protein
CD55 (2, 3). CD97 may play a role inflammatory and immune responses as well as
the progression of several types of cancer (3). Cells known to express CD97 include monocytes, macrophages, T cells, select B
cells, dendritic cells and, potentially, vascular and visceral smooth muscle
cells (5-7). CD97 is also differentially expressed on murine hematopoietic
stem- and progenitor-cells (7). CD55 (decay accelerating factor), a GPI-linked
cell surface molecule with short consensus repeats that regulates complement
activation on cell surfaces, chondroiten sulfate and the integrin alpha 5 beta
(also known as VLA-5) have been identified as cellular ligands for CD97 (7).
The composition of the EGF domain region defines the ligand specificity of the
different CD97 isoforms (7). The first and second EGF domains interact with
CD55, whereas the fourth EGF domain binds chondroitin sulfate (7). The ligand
affinity of the CD97 isoforms differs (7). While affinity for CD55 is
significantly higher for the smaller isoforms, chondroitin sulfate interacts
exclusively with the largest isoforms (7). Lymphocytes and erythrocytes (red
blood cells) have been shown to specifically adhere to CD97-transfected COS
cells. The adhesion of red blood cells to CD97 transfectants was blocked using
a mAb which recognizes CD55 (8). It has also been demonstrated that CD97 is
required for neutrophil migration and host defense (9).
- Veninga, H. et al. (2008) J. Immunol. 181:6574.
- Wobus, M. et al. (2004) Int. J. Cancer. 112:815.
- Lin, H.H. et al. (2001) J. Biol. Chem. 276:24160.
- Gray, J.X. et al. (1996) J. Immunol. 157:5438.
- McKnight, A.J. and S. Gordon (1998) J Leukoc. Biol. 63:271.
- Jaspars, L.H. et al. (2001) Tissue Antigens 57:325.
- Van Pel, M. et al. (2008) Haematologica 93:1137.
- Hamann, J. et al. (2019) J Exp Med. 184:1185.
- Leemans, J.C. et al. (2004) J. Immunol. 172:1125.
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