Human Krueppel-like factor 15 (KLF15) ELISA Kit

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AE36619HU
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Product Name Human Krueppel-like factor 15 (KLF15) ELISA Kit
Description KLF15 protein is 84% identical to the rat Klf15 protein, contains 3 zinc finger motifs at its C terminus, N-terminal serine-rich stretches, and a central proline-rich segment. EMSA analysis confirmed that KLF15 and MAZ interact with the GA element of the CLCNKA promoter and showed that KLF15 binds with higher affinity and is a functional competitor of MAZ. Northern blot analysis revealed highest expression of a 2.5-kb KLF15 transcript in liver, followed by heart, skeletal muscle, and kidney. No expression was found in bone marrow or lymphoid tissues. KLF15 was also expressed in cardiac and skeletal muscle interstitial cells and in kidney inner medulla, glomeruli, and cortical interstitium. Immunofluorescence microscopy, however, demonstrated no colocalization of KLF15 with CLCNKA. This assay has high sensitivity and excellent specificity for detection of Human KLF15. No significant cross-reactivity or interference between Human KLF15 and analogues was observed.
Synonyms DKFZp779M1320, KKLF, kidney-enriched Kruppel-like factor
Method Sandwich ELISA
Detection Range 0.156-10 ng/mL
Sensitivity 0.068 ng/mL
Reactivity Human
Sample Types Serum, Plasma, Other biological fluids.
Background KLF15 protein is 84% identical to the rat Klf15 protein, contains 3 zinc finger motifs at its C terminus, N-terminal serine-rich stretches, and a central proline-rich segment. EMSA analysis confirmed that KLF15 and MAZ interact with the GA element of the CLCNKA promoter and showed that KLF15 binds with higher affinity and is a functional competitor of MAZ. Northern blot analysis revealed highest expression of a 2.5-kb KLF15 transcript in liver, followed by heart, skeletal muscle, and kidney. No expression was found in bone marrow or lymphoid tissues. KLF15 was also expressed in cardiac and skeletal muscle interstitial cells and in kidney inner medulla, glomeruli, and cortical interstitium. Immunofluorescence microscopy, however, demonstrated no colocalization of KLF15 with CLCNKA.
Supplier Abebio

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