Product Name: Arginase 1 Antibody [T1ARG-1]
Species Reactivity: Human
Tested Applications: IF, IHC-P, WB
Applications: Immunofluorescence: 1-2 ug/mlWestern blot: 0.5-1 ug/mlImmunohistochemistry (FFPE): 2-4 ug/ml for 30 min at RT (1)Prediluted format : incubate for 30 min at RT (2)Optimal dilution of the Arginase 1 antibody should be determined by the researcher.1. Staining of formalin-fixed tissues requires boiling tissue sections in 10mM Citrate buffer, pH 6.0, for 10-20 min followed by cooling at RT for 20 min2. The prediluted format is supplied in a dropper bottle and is optimized for use in IHC. After epitope retrieval step (if required), drip mAb solution onto the tissue section and incubate at RT for 30 min.
User Note: Optimal dilutions for each application to be determined by the researcher
Predicted Molecular Weight:
Immunogen: A C-terminal recombinant protein fragment from ARG1 was used as the immunogen for the Arginase 1 antibody.
Host Species: Mouse
Purification: Protein G affinity chromatography
Physical State: Liquid
CAS NO.: 1223405-08-0
Product: LOXO-101 (sulfate)
Buffer: PBS with 0.1 mg/ml BSA and 0.05% sodium azide
Concentration: 0.2 mg/mL
Storage Conditions: Aliquot and Store at -20C. Avoid freez-thaw cycles.
Clonality: Monoclonal
Conjugate: Unconjugated
Alternate Names: Arginase-1, Liver-type arginase, Type I arginase, ARG1
Accession NO.:
Protein Ino:
Official Symbol: ARG1
Geneid: 383
Background: Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exist (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type I isoform is a cytosolic enzyme and expressed predominantly in the liver as a component of the urea cycle. Inherited deficiency of this enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia. Two transcript variants encoding different isoforms have been found for this gene. [RefSeq]
PubMed ID:http://aac.asm.org/content/53/4/1592.abstract