Comparison

In vivo Grade Recombinant Chimeric Human IgG2 Isotype Control Antibody European Partner

Item no. YR0353-1mg
Manufacturer Abclonal
Amount 1 mg
Category
Applications WB, FC, IP, IHC, ELISA, IV
Specific against other
Isotype IgG1 Kappa
Purity >95% Determined by SDS-PAGE
Available
Manufacturer - Applications
an isotype-matched negative control used in ELISA, Western Blot (WB), Flow Cytometry (Flow), Immunoprecipitation (IP), Immunohistochemistry (Paraffin) (IHC (P)), Immunohistochemistry (Frozen) (IHC (F)), and in vivo animal model research
Manufacturer - Category
Biosimilar
Manufacturer - Conjugate / Tag
<5% Determined by SECP
Storage Conditions
2 - 8°C for up to 4 weeks and -80°C for long term storage (Avoid repeated freezing and thawing)
Background
Naturally synthesized and secreted by plasma B cells, the immunoglobulin G (IgG) antibody is the most abundant antibody isotype found in blood and extracellular fluid. There are four IgG subclasses (IgG1, IgG2, IgG3, and IgG4) in humans, of which IgG1 is the most abundantnamed in serum. IgG antibodies are large molecules of about 150 kDa composed of four peptide chains, two identical heavy chains of about 50 kDa and two identical light chains of about 25 kDa. The four peptides are arranged in a Y-shape tetramer by disulfide bonds formed between the two heavy chains and between a heavy chain and a light chain.The arms of the Y, also called the Fab (fragment, antigen-binding) region containing an identical antigen binding site, is composed of one variable (located at amino terminal end, VH and VL) and one constant domain (CH1 and CL) from each heavy and light chain of the antibody. VH and VL, also called the FV region, is the most important region for binding to antigens. Three variable loops of β-strands, also called the complementarity determining regions (CDRs or idiotypes), on VH and VL respecetively are responsible for binding to the antigen.The base of the Y, also called the Fc (Fragment, crystallizable) region and composed of two heavy chains with two or three constant domains depending on the class of the antibody, binds to a specific class of Fc receptors and other immune molecules, such as complement proteins, to induce an appropriate immune response for a given antigen. The Fc region bears two highly conserved N-glycosylation sites, one on each heavy chain. The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. In addition, small amounts of these N-glycans also bear bisecting GlcNAc and α-2, 6-linked sialic acid residues.
Manufacturer - Cross Reactivity
<1EU/mg (<0.001EU/μg)Determined by LAL gel clotting assay
Route
1×PBS pH 7.0

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 1 mg
Available: In stock
available

Delivery expected until 12/4/2025 

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