Exoglucanase Isoenzyme 1 (EXO1) antibody

Antigen: Exoglucanase Isoenzyme 1 (EXO1)

Clonality: Polyclonal

Host: Rabbit

Reactivity: Barley (Hordeum vulgare)

Application: Western Blotting (WB), ELISA

Catalog no.: ABIN249341

Additional Information

Immunogen: synthetic peptide conjugated to KLH

Format: Lyophilized

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

Specificity: Predicted reactivity: Oryza sativa, Zea mays.

Application Details

Application Notes: Recommended Dilution 1: 5 000 with standard ECL (WB) , 1: 10 000 (ELISA).

Purity: Serum

Storage: store lyophilized/reconstituted at -20°C, once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior toopening them to avoid any losses that might occur from lyophilized materialadhering to the cap or sides of the tubes.

Research Area: Plant/Algal Physiology

Restrictions: For Research Use only

Publications

Publications: Hrmova, De Gori, Smith et al.: "Structural basis for broad substrate specificity in higher plant beta-D-glucan glucohydrolases." in: The Plant cell, Vol. 14, Issue 5, pp. 1033-52, 2002 (PubMed).