Recombinant Human Fc mu R/FAIM3 Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When human IgM is immobilized at 2 μg/mL, 100 μL/well, Recombinant Human Fc mu R/FAIM3 binds with an ED50 of 0.4-2 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human Fc mu R/FAIM3 protein
Human Fc mu R/FAIM3 (Arg18-Gly251) Accession # O60667-1
>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
Bioactivity
Theoretical MW
27 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
39-50 kDa, reducing conditions
Publications
Read Publication using 9494-MU in the following applications:
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 200 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 Fc mu R/FAIM3 Protein, CF
FAIM3
Fas apoptotic inhibitory molecule 3
Fc mu R
Fc mu receptor
FCMR
immunoglobulin mu Fc receptor
Regulator of Fas-induced apoptosis Toso
Toso
TOSOIgM Fc receptor
Background
The
human FAIM3 gene (also known as FCMR or TOSO), is a transmembrane sialoglycoprotein expressed mainly
by lymphocytes. FAIM3 is a type I membrane protein with an intracellular
C-terminal domain and an extracellular N-terminal
domain (1). The extracellular
domain has homology to the immunoglobulin variable
region domains (1) and FAIM3 is identified as an Fc receptor for IgM (2, 3). The amino acid sequence of human FAIM3 is 58% and 55%
identical to that of mouse and rat FAIM3, respectively. FAIM3 was shown to be
over-expressed in chronic lymphocytic leukemia (CLL) (4) and associated with
disease progression (5, 6). FAIM3 has also been linked to the homeostasis and
activation of the innate immune system (7). Interestingly, there is growing
evidence that neurodegenerative diseases are associated with the activation of
the immune surveillance system. This system is responsible for controlling
danger signals and responding accordingly to the magnitude and duration of the
threat (8, 9).
Song, Y. et al (2005) J. Biol. Chem. 280(10):9618.
Shima H et al. (2010) Int. Immunol. 22:149.
Kubagawa H et al. (2009) J. Exp. Med. 206:2779.
Proto-Siqueira R et al. (2008) Blood, 112:394.
Pallasch, C et al. (2008) Blood, 112:4213.
Pallasch, C P et al (2009) Leukemia & lymphoma, 50:498.
Sigruener, A et al (2007) Biochemical and biophysical research communications, 359:723.
Richards R I et al (2016) Front. Neurosci. 10:193.
Planells-Ferrer L et al (2016) J Neurochem. 139:11.
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