Exo1 | exoglucanase isoenzyme 1

AS08 322  |  Clonality: Polyclonal  |  Host:  Rabbit  |  Reactivity: Hordeum vulgare

Exo1 | exoglucanase isoenzyme 1 in the group Antibodies Plant/Algal  / Carbohydrates at Agrisera AB (Antibodies for research) (AS08 322)


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Product Information


synthetic peptide conjugated to KLH

Host Rabbit
Clonality Polyclonal
Purity Serum
Format Lyophilized
Quantity 100 ĩl
Reconstitution For reconstitution add 100 ĩl of sterile water
Storage Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
Tested applications ELISA (ELISA), Western blot (WB)
Recommended dilution 1 : 10 000 (ELISA), 1 : 5 000 (WB)
Expected | apparent MW

66 kDa


Confirmed reactivity Hordeum vulgare
Predicted reactivity Oryza sativa, Zea mays
Species of your interest not listed? Contact us
Not reactive in No confirmed exceptions from predicted reactivity are currently known

Application examples

Additional information

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Family 3 beta-d-glucan glucohydrolases are widely distributed in higher plants. The enzymes catalyse the hydrolytic removal of beta-d-glucosyl residues from non-reducing termini of a range of beta-d-glucans and beta-d-oligoglucosides. Their broad specificity can be rationalized from X-ray crystallographic data obtained from a barley beta-d-glucan glucohydrolase in complex with non-hydrolysable S-glycoside substrate analogues, and from molecular modelling of enzyme-substrate complexes. The glucosyl residue occupying binding subsite -1 is tightly locked into a fixed position through extensive hydrogen bonding with six amino acid residues near the bottom of an active site pocket. In contrast, the glucosyl residue at subsite +1 is located between two tryptophan residues at the entrance of the pocket, where it is less tightly constrained. The relative flexibility of binding at subsite +1, coupled with the projection of the remainder of bound substrate away from the enzyme’s surface, means that the overall active site can accommodate a range of substrates with variable spatial dispositions of adjacent beta-d-glucosyl residues. The broad specificity for glycosidic linkage type would enable the enzyme to perform diverse functions during plant development.

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