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Recombinant Biotinylated Human FcRn/FCGRT & B2M, Avi Tag (Avitag™), 25 µg  

Recombinant Biotinylated Human FcRn/FCGRT & B2M, Avi Tag (Avitag™), 25 µg

Recombinant biotinylated Human FcRn / FCGRT & B2M Heterodimer Protein (FCM-H82W4) from human HEK293 cells, (SPR verified)

Synonyms: recombinant, human, biotinylated, protein FcRN & B2M,FCGRT & B2M

More details

FCM-H82W4-25

420,00 €

Background
FCGRT & B2M heterodimer protein (FcRn complex) consist of two subunits: p51 (equivalent to FCGRT), and p14 (equivalent to beta-2-microglobulin), and forms an MHC class I-like heterodimer. Fc fragment of IgG, receptor, transporter, alpha (FCGRT) binds to the Fc region of monomeric immunoglobulins gamma and mediates the uptake of IgG from milk. FCGRT possible role in transfer of immunoglobulin G from mother to fetus. Beta-2-microglobulin (B2M) is a component of the class I major histocompatibility complex (MHC) and involved in the presentation of peptide antigens to the immune system.

Source
Recombinant Biotinylated Human FcRn Heterodimer Protein (SPR verified) (FCM-H82W4) is expressed from human 293 cells (HEK293). It contains AA Ala 24 - Ser 297 (FCGRT) & Ile 21 - Met 119 (B2M) (Accession # P55899-1 (FCGRT) & P61769-1 (B2M)).

Predicted N-terminus: Ala 24 (FCGRT) & Ile 21 (B2M)


Request for sequence

Molecular Characterization
Biotinylated Human FcRn Heterodimer Protein (SPR verified), produced by co-expression of FCGRT and B2M, has a calculated MW of 34.1 kDa (FCGRT) and 13.1 kDa (B2M). Subunit FCGRT is fused with a polyhistidine tag at the C-terminus, followed by an Avi tag (Avitag™) and subunit Beta-2 microglobulin (B2M) is fused with Strep II-tag at the C-terminus. The reducing (R) protein migrates as 38 kDa (FCGRT) and 14 kDa (B2M) respectively due to glycosylation.

Biotinylation
Biotinylation of this product is performed using Avitag™ technology. Briefly, the single lysine residue in the Avitag is enzymatically labeled with biotin.
Biotin:Protein Ratio
The biotin to protein ratio is 0.5-1 as determined by the HABA assay.

Endotoxin
Less than 1.0 EU per μg by the LAL method.

Purity
>95% as determined by SDS-PAGE.

Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.

Contact us for customized product form or formulation.

Reconstitution
Please see Certificate of Analysis for specific instructions.For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Storage
For long term storage, the product should be stored at lyophilized state at -20°C or lower. Please avoid repeated freeze-thaw cycles. No activity loss is observed after storage at: 4-8°C for 12 months in lyophilized state; -70°C for 3 months under sterile conditions after reconstitution.

Bioactivity
Biotinylated Human FcRn Heterodimer Protein (SPR verified) (Cat. No. FCM-H82W4) captured on Biotin CAP- Series S Sensor Chip can bind Herceptin with an affinity constant of 0.369 μM as determined in a SPR assay (Biacore T200) (QC tested).

Limited Use License
The Biotin AviTag technology is covered by U.S. Pat. No: 5,874,239 and includes any and all materials, methods, kits and related derivatives claimed by this patent. The purchase of the Acrosbiosystems’s Avitag™ proteins confers to the purchaser the limited right to use the Avitag™ technology for non-commercial, or research use, or for purposes of evaluating the Avitag™ technology.
Commercial use of the Avitag™ technology to manufacture a commercial product, or use of the Avitag™ technology to facilitate or advance research which will be applied to the development of a commercial product requires a license from Avidity, LLC. Examples of Commercial use include, but are not limited to biosensors, diagnostics, therapeutic applications, proximity assays, and drug screening assays. 

References

(1) Goebl NA., et al., 2008, Mol. Biol. Cell 19 (12): 5490–505.
(2) Lee TY., et al., 2008, Clin. Cancer Res. 14 (5): 1487–93.
(3) Güssow D., et al., 1987, J. Immunol. 139 (9): 3132–8.
(4) Gorevic P.D., et al., 1986, Proc. Natl. Acad. Sci. U.S.A. 83:7908-7912.

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