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Anti-Heat-labile enterotoxin B chain mAbs

简要描述:

The epitope of this antibody is the sequence: VEVPGSQHIDSQKKA from Cholera toxin peptide 3 (CTP3)

产品参数:

Cat. No.:MABL-1792

Species:Engineer

Species Reactivity:Vibrio cholerae, Escherichia coli

Type:Recombinate

Application:crystallography, in vitro, SPR, WB, ELISA

详细介绍

Key features and   details


Cat. No.

MABL-1792

Name

Anti-Heat-labile   enterotoxin B chain mAbs

Clone No.

AFD- anti-CTP3-TE33

From

Recombinant Antibody

Isotype

Engineer antibody

Application

crystallography, in vitro, SPR, WB, ELISA

Species Reactivity

Vibrio cholerae, Escherichia coli

Basic Information


Specificity

The epitope of this antibody is the   sequence: VEVPGSQHIDSQKKA from Cholera toxin peptide 3 (CTP3)

Alternative Name

CTB; eltB; ltpB; CTP3; LT-B; LTP-B; ctxB;   porcine; Cholera enterotoxin B- subunit; Cholera enterotoxin subunit B;   Cholera toxin B protein

UniProt

P32890; Q57193

Immunogen

The original antibody was raised by immunizing   a Balb/c mouse with amino acid residues 50- 64 of the B subunit of cholera   toxin coupled to tetanus toxoid

Application Notes

The original antibody was used for  fluorescence quenching on DNP-CTP3. This experiment was performed to   determine the binding affinity of this antibody, which is 1.2 x 10^6 M^-1.   The antibody was used for a radioimmunoassay on cholera toxin and H-LT, a   heat-labile toxin produced by enterotoxigenic strains of E. coli isolated   from humans. The antibody bound to both antigens. The antibody was used for a   western blot on cholera toxin and H-LT, a heat-labile toxin produced by   enterotoxigenic strains of E. coli isolated from humans. Which showed the   same results as the radioimmunoassay (Anglister et al., 1988; PMID:2450576).   The structure of this antibody was determined using NMR measurements (Zilber   et al., 1990; PMID:2271636). The structure of this antibody was determined   using X-ray crystallography (Shoham, 1993; PMID:7690406). This antibody was   used for Phage-colony dot immunoblotting. 

Antibody First   Published

Anglister et al. NMR study of the complexes   between a synthetic peptide derived from the B subunit of cholera toxin and  three monoclonal antibodies against it Biochemistry. 1988 Jan   26;27(2):717-24. PMID:2450576

Note on publication

In the original paper the contact   interactions between a synthetic peptide and three different anti-peptide   monoclonal antibodies have been studied by nuclear magnetic resonance (NMR).

COA Information For reference only, actual COA shall prevail

Size

100 μg Purified   antibody.

Concentration

1 mg/ml.

Purification

Protein A affinity   purified

Buffer

PBS with 0.02% Proclin   300.

Concentration

1 mg/ml.

Storage   Recommendation

Store at 4⁰C for up to 3   months. For longer storage, aliquot and store at - 20⁰C.


 


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