Human IgG4 Fc Protein 4760

$75.00 – $250.00

Summary

Expression: HEK293
Binding assay: Yes (SPR)
Amino Acid Range: Glu99-Gly326

SKU: 4760parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P01861
express system	HEK293
product tag	No Tag
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	It is known as a IgG4-related disease and its differentiation is based on the analysis of IgG4 levels in the affected tissues. The IgG4-related disease is considered to be a generalized pathological process involving a wide spectrum of various disorders that may affect distant organs.
molecular weight	The protein has a predicted MW of 25.8 kDa. Due to glycosylation, the protein migrates to 30-35 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human IgG4 Fc Protein 4760

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
It is known as a IgG4-related disease and its differentiation is based on the analysis of IgG4 levels in the affected tissues. The IgG4-related disease is considered to be a generalized pathological process involving a wide spectrum of various disorders that may affect distant organs.
Protein names Immunoglobulin heavy constant gamma 4 (Ig gamma-4 chain C region)
Gene names IGHG4,IGHG4
Mass 9606Da
Function Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
Subellular location [Isoform 1]: Secreted .; [Isoform 2]: Cell membrane ; Single-pass membrane protein .
Structure Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked.
Post-translational modification Glycosylation on Asn-177 is required for interaction with Fc receptors and ability to activate the complement pathway.; (Microbial infection) Deglycosylation on Asn-177 by S.pyogenes EndoS or Endos2 endoglucosidases prevents interaction between immunoglobulin-gamma (IgG) and Fc receptors, impairing ability to activate the complement pathway.
Target Relevance information above includes information from UniProt accession: P01861
The UniProt Consortium

Data

Human FcRn, His Tag captured on CM5 Chip via Anti-His Antibody can bind Human IgG4 Fc, No Tag with an affinity constant of 1.365 µM as determined in SPR assay (Biacore T200).

The purity of Human IgG4 Fc is greater than 95% as determined by SEC-HPLC.

Human IgG4 Fc on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.