Product Name: GZMK Antibody
Species Reactivity: Human
Tested Applications: ELISA, WB
Applications: GZMK antibody can be used for detection of GZMK by ELISA at 1:62500. GZMK antibody can be used for detection of GZMK by western blot at 0.5 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50,000 – 100,000.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight: 26 kDa
Immunogen: Antibody produced in rabbits immunized with a synthetic peptide corresponding a region of human GZMK.
Host Species: Rabbit
Purification: Antibody is purified by peptide affinity chromatography method.
Physical State: Lyophilized
CAS NO.: 243966-09-8
LY294002
Buffer: Antibody is lyophilized in PBS buffer with 2% sucrose. Add 50 μL of distilled water. Final antibody concentration is 1 mg/mL.
Concentration: 1 mg/ml
Storage Conditions: For short periods of storage (days) store at 4˚C. For longer periods of storage, store GZMK antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: GZMK, TRYP2
Accession NO.: NP_002095
Protein Ino: 4504235
Official Symbol: GZMK
Geneid: 3003
Background: GZMK is a member of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes (CTL) and natural killer (NK) cells share the remarkable ability to recognize, bind, and lyse specific target cells. They are thought to protect their host by lysing cells bearing on their surface nonself antigens, usually peptides or proteins resulting from infection by intracellular pathogens. The protein described here lacks consensus sequences for N-glycosylation present in other granzymes.This gene product is a member of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes (CTL) and natural killer (NK) cells share the remarkable ability to recognize, bind, and lyse specific target cells. They are thought to protect their host by lysing cells bearing on their surface nonself antigens, usually peptides or proteins resulting from infection by intracellular pathogens. The protein described here lacks consensus sequences for N-glycosylation present in other granzymes.
PubMed ID:http://aac.asm.org/content/21/1/1.abstract
