Recombinant Mouse IgG2A Fc #abs04689

Recombinant Mouse IgG2A Fc #abs04689

Please note that the price provided is only for your reference. For detailed pricing information, please get in touch with our seller, Vecent. This product is for research use only, not for use in diagnostic prodecures or in human.

Description

Catalog-specification

Delivery time

USD price

abs04689-10ug

1-2 Weeks

46

abs04689-50ug

1-2 Weeks

138

abs04689-500ug

1-2 Weeks

695

abs04689-1mg

1-2 Weeks

946

Please note that the price provided is only for your reference. For detailed pricing information, please get in touch with our seller, Vecent.


Overview

Description

Our expression system is capable of producing the A allele of Recombinant Mouse Ig gamma-2A chain C region. The expressed target gene codes for amino acids Pro99 to Lys330.

Other names

Ig gamma-2 chain C region, IgG2A Fc

Source

Human Cells

Format

The solution was filtered through a 0.2 μm filter and then lyophilized. It contained 20mM PB and 150mM NaCl, with a pH of 7.4.

Properties

aa_sequence

ISTPPVTVCCVVVDVEDDDPSVQIFIFSPVLSLSMIDVKIKPPFIVSGPGLLNPNAPCKCPCPKTK PGVEVLNNWFAHQHDDYRTVLRSVIPSQAPKGEFKNKDVAVLYTPEPVMQKQMTLVTSIMCFTN VDEYEIPWNTGKETLKNDEYNSEVTYKFSLMRSVEKNKWRVYSPCESHVTHHNGHLFSSRPTTK GGGG,GPTChapGPT,。GGGG,ChapGPT。,,。

Concentration

The determination of the purity of the sample was done by utilizing SDS-PAGE gel electrophoresis, and it was found to be greater than 95%. To create a similar content, but with a rearranged structure, the following could be written: SDS-PAGE was employed to evaluate the purity level of the sample. The results indicate a purity of greater than 95%.

Endotoxin_level

The level of endotoxin in the substance is extremely low, measuring less than 0.1 ng/μg (equivalent to 1 international endotoxin unit per μg). This has been determined through the use of the LAL test.

Reconstitution

It is essential to always centrifuge your tubes before opening them to avoid any mishaps. Avoid mixing your samples by vortex or pipetting, as this can damage the protein. Reconstituting the protein in a concentration lower than 100 μg/ml is not advisable. To dissolve the lyophilized protein, use ddH2O. Please make sure to aliquot the solution after reconstitution to minimize freeze-thaw cycles. It is necessary to generate similar content by rearranging the provided text information so that it can be understood better. However, please avoid using the ChapGPT method to generate your content and opt for a language model to create something entirely different.

Target

Background

As a monomeric immunoglobulin that is predominately involved in the secondary antibody response and the only isotype that can pass through the human placenta, Immunoglobulin G (IgG) is synthesized and secreted by plasma B cells, and constitutes 75% of serum immunoglobulins in humans. IgG antibodies protect the body against the pathogens by agglutination and immobilization, complement activation, toxin neutralization, as well as the antibody-dependent cell-mediated cytotoxicity (ADCC). IgG tetramer contains two heavy chains (50 kDa ) and two light chains (25 kDa) linked by disulfide bonds, that is the two identical halves form the Y-like shape. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). 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. Protein G or Protein A on the surface of certain Staphylococcal and Streptococcal strains specifically binds with the Fc region of IgGs, and has numerous applications in biotechnology as a reagent for affinity purification. Recombinant IgG Fc Region is suggested to represent a potential anti-inflammatory drug for treatment of human autoimmune diseases.

Accession

P01863


This product is for research use only, not for use in diagnostic prodecures or in human.


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