IGG-HM001-100μg / 询价
IGG-HM001-500μg / 询价
IGG-HM001-500μgx2 / 询价
Human IgG1 Fc Protein
Recombinant Human IgG1 Fc is expressed from HEK293 without tag. It contains Asp104-Lys330.[Accession | P01857-1]
The protein has a predicted MW of 25.5 kDa. Due to glycosylation, the protein migrates to 31-33 kDa based on Tris-Bis PAGE result.
Less than 1EU per μg by the LAL method.
> 95% as determined by Tris-Bis PAGE
> 95% as determined by HPLC
Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.
-20 to -80°C for 12 months as supplied from date of receipt.
-80°C for 3-6 months after reconstitution.
2-8°C for 2-7 days after reconstitution.
Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Human IgG1 Fc on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.
The purity of Human IgG1 Fc is greater than 95% as determined by SEC-HPLC.
Human FcRn, His Tag captured on CM5 Chip via anti-his antibody can bind Human IgG1 Fc, No Tag with an affinity constant of 0.28 μM as determined in SPR assay (Biacore T200).
IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues.IgG1 Fc was reported has a novel role as a potential anti-inflammatory drug for treatment of human autoimmune diseases.
IgG1; Igh-4; RGD1359539; VH7183
(1)Ponstingl H, Hilschmann N. [Rule of antibody structure. The primary structure of a monoclonal IgG1 immunoglobulin (myeloma protein Nie), II: isolation and amino acid sequence of the tyrptic peptides from the H-chain (author's transl)].[J]. Hoppe Seylers Zeitschrift Für Physiologische Chemie, 1976, 357(11):1541.
