ANK1 Monoclonal / Alexa Fluor 647 / S388A-60
Product Details
Description | Detects 200kDa. Cross-reacts with Ankyrin-B and Ankyrin-G. | |
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Conjugate | Alexa Fluor 647 | |
Clone | S388A-60 | |
Target Species | Human, Mouse, Rat | |
Applications | ICC, IF, WB, IHC | |
Supplier | Novus Biologicals | |
Catalog # | Sign in to view product details, citations, and spectra | |
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About ANK1
Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008]
Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008]
About Alexa Fluor 647
Alexa Fluor™ 647 (AF647, Alexa 647) has an excitation peak at 650 nm and an emission peak at 665 nm, and is spectrally similar to Cy®5 (GE Healthcare), iFluor® 647 (ATT Bioquest), and DyLight™ 650 (Thermo Fisher Scientific). Alexa 647 is commonly used for flow cytometry, microscopy, super-resolution microscopy applications. It is very bright, photostable, and pH insensitive, all of which contribute to sensitive detection while using this dye.
Alexa Fluor™ 647 (AF647, Alexa 647) has an excitation peak at 650 nm and an emission peak at 665 nm, and is spectrally similar to Cy®5 (GE Healthcare), iFluor® 647 (ATT Bioquest), and DyLight™ 650 (Thermo Fisher Scientific). Alexa 647 is commonly used for flow cytometry, microscopy, super-resolution microscopy applications. It is very bright, photostable, and pH insensitive, all of which contribute to sensitive detection while using this dye.
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