CTRB1 Polyklonale Antilichaam, PE-vervoeging

Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

Chymotrypsinogen B; Chymotrypsinogen B1; ChymotrypsinogenB; ChymotrypsinogenB1; CTRB 1; CTRB; FLJ42412; MGC88037; OTTHUMP00000214638_ CTRB1_HUMAN; Chymotrypsin B chain B.

Secreted, Extracellular matrix

121-230/263

CTRB1

PE

KLH conjugated synthetic peptide derived from human Chymotrypsin B chain B

WB, IF (IHC-P), IF (IHC-F), IF (ICC)

Purified by Protein A.

496,564nm/578nm

1µg/µl

WB (1:300-5000), IF (IHC-P) (1:50-200), IF (IHC-F) (1:50-200), IF (ICC) (1:50-200)

Aqueous buffered solution containing 0.01M TBS (pH 7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Unmodified

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

Human, Mouse, Rat, Cow