Recombinant Human CD45RB Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human Galectin-9
(Catalog #
2045-GA)
is immoblized at 1 µg/mL (100 µL/well), the concentration of Recombinant Human CD45RB Fc Chimera (Catalog # 10477-CD) that produces a 50% optimal binding response is found to be 125-750 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human CD45RB protein Human CD45RB (Gln26-Lys463) Accession # XP_006711537.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gln26, inferred by deblocking revealing Ser25 |
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 |
75.6 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 |
123-152 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 250 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 CD45RB Fc Chimera Protein, CF
Background
CD45, previously
called LCA (leukocyte common antigen), T200, or Ly5 in mice, is member C of the
class 1 (receptor-like) protein tyrosine phosphatase family (PTPRC) (1, 2). It
is a variably glycosylated 180-220 kDa transmembrane protein that is abundantly
expressed on all nucleated cells of hematopoietic origin (1-3). Multiple
splicing isoforms of exon 4 (A), 5 (B), and 6 (C) are expressed according to
cell type, developmental stage and antigenic exposure (1-5). The longest form,
CD45RABC (called B220 in mouse) is expressed on B lymphocytes and the shortest
form, CD45R0 is expressed on memory cells (5). Isoform CD45RB contains exon 5
(B exon) in the extracellular domain, which shares 41% and 40% homology with
the ECD of mouse and rat CD45RB. CD45 has been best studied in T cells, where
it determines T cell receptor signaling thresholds (3, 6-8). CD45 is moved into
or out of the immunological synapse (IS) membrane microdomain depending on the
relative influence of interaction with the extracellular galectin lattice or
the intracellular actin cytoskeleton (9, 10). Interaction of galaction can be
fine-tuned by varying usage of the heavily O-glycosylated spliced regions and
sialylation of N-linked carbohydrates of CD45 (4, 9). Within the immunological
synapse, CD45 dephosphorylates and negatively regulates the Src family kinase,
Lck (8-10). In other leukocytes, CD45 influences differentiation and links
immunoreceptor signaling with cytokine secretion and cell survival, partially
overlapping in function with DEP-1/CD148 (11-14). CD45 deletion causes in
severe immunodeficiency, while point mutations may be associated with
autoimmune disorders (6, 7).
- Anderson, J.N. et al. (2004) FASEB J. 18:8.
- Streuli, M. et al. (1987) J. Exp. Med. 166:1548.
- Hermiston, M.L. et al. (2003) Annu. Rev. Immunol. 21:107.
- Earl, L.A. and L.G. Baum (2008) Immunol. Cell Biol. 86:608.
- Ralph, S.J. et al. (1987) EMBO J. 6:1251.
- Falahti, R. and D. Leitenberg (2008) J. Immunol. 181:6082.
- Tchilian, E.Z. and P.C.L. Beverley (2006) Trends Immunol. 27:146.
- McNiell, L. et al. (2007) Immunity 27:425.
- Chen, I-J. et al. (2007) J. Biol. Chem. 282:35361.
- Freiberg, B.A. et al. (2002) Nat. Immunol. 3:911.
- Zhu, J.W. et al. (2008) Immunity 28:183.
- Huntington, N.D. et al. (2006) Nat. Immunol. 7:190.
- Hesslein, D.G. et al. (2006) Proc. Natl. Acad. Sci. USA 103:7012.
- Cross, J.L. et al. (2008) J. Immunol. 180:8020.
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