AK1 Antibody (C-term) Blocking Peptide

Background:
Adenylate kinase is an enzyme involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate group among adinine nucleotides. Three isozymes of adenylate kinase have been identified in vertebrates, adenylate isozyme 1 (AK1), 2 (AK2) and 3 (AK3). AK1 is found in the cytosol of skeletal muscle, brain and erythrocytes, whereas AK2 and AK3 are found in the mitochondria of other tissues including liver and heart. AK1 was identified because of its association with a rare genetic disorder causing nonspherocytic hemolytic anemia where a mutation in the AK1 gene was found to reduce the catalytic activity of the enzyme.

Other Names: Adenylate kinase isoenzyme 1 {ECO:0000255|HAMAP-Rule:MF_03171}, AK 1 {ECO:0000255|HAMAP-Rule:MF_03171}, 2743 {ECO:0000255|HAMAP-Rule:MF_03171}, 2746 {ECO:0000255|HAMAP-Rule:MF_03171}, ATP-AMP transphosphorylase 1 {ECO:0000255|HAMAP-Rule:MF_03171}, ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03171}, Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03171}, Myokinase {ECO:0000255|HAMAP-Rule:MF_03171}, AK1 {ECO:0000255|HAMAP-Rule:MF_03171}

Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP8160b was selected from the C-term region of human AK1 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.

Type: Synthetic peptide

Primary Accession: P00568

Gene ID: 203

Gene Name: AK1 {ECO:0000255|HAMAP-Rule:MF_03171}

Format: The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.

Bio References:
Corrons, J.L., et al., Blood 102(1):353-356 (2003).Toren, A., et al., Br. J. Haematol. 87(2):376-380 (1994).Zuffardi, O., et al., Hum. Genet. 82(1):17-19 (1989).Matsuura, S., et al., J. Biol. Chem. 264(17):10148-10155 (1989).Miwa, S., et al., Am. J. Hematol. 14(4):325-333 (1983).