Mouse anti-Camelid IgG2/3 (heavy chain) Antibody, clone P17JE11

Camelidae family that includes camels and llamas are the only mammals reported to have heavy-chain (IgG-like) antibodies. Camelids produce conventional antibodies, but they also produce antibodies that do not associate with light chains. They produce functional antibodies devoid of light chains of which the single N-terminal domain is fully capable of antigen binding. Their VHH domain is located on a single stretch of amino acids and retains its antigen-recognition capability. Their heavy chains are devoid of the CH1 domain and have modified VH domain. Camelid heavy-chain antibodies (HCAbs) comprise about 50% of serum IgG in Llama and about 75% in Camelus species. HCAbs exhibit a molecular mass of about 100 kDa, which is smaller than conventional IgG1 and allows it to bind epitopes that may not be accessible to conventional antibodies. Also, the smaller size and single domain make it easier to transform them into bacterial cells for larger production needs. HCAbs are reported to display similar specificities, but are more robust in some cases. (Ref.: Daley LP et al. (2010). Clin. Vaccine Immunol. 17(2); 239-246; Harmsen, MM., and De Haard, HJ (2007) Appl Microbiol Biotechnol 77(1):13-22).

Clone P17JE11 detects Camelid IgG2/igG3 heavy chain. Displays trivial to none reactivity with other species.

Camelid heavy-chain immunoglobulin G (clgG2/3).

Mouse anti-Camelid IgG2/3 (heavy chain), clone P17JE11 detects Camelid IgG2/igG3 heavy chain. It has been tested for use in ELISA.

Research Sub Category
Secondary & Control Antibodies

Evaluated by ELISA in IgG as tested in various species.

ELISA Analysis: 2 µg/mL of this antibody detected Camelid IgG2/3 (heavy chain).

Format: Purified

Protein G purified

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.

Concentration: Please refer to lot specific datasheet.

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