Rabbit Recombinant Monoclonal Fukutin antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 4 publications.
pH: 7.2 - 7.4
Preservative: 0.01% Sodium azide
Constituents: 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 9% PBS, 0.05% BSA
IHC-P | IP | Flow Cyt | WB | |
---|---|---|---|---|
Human | Tested | Not recommended | Not recommended | Tested |
Mouse | Predicted | Not recommended | Not recommended | Predicted |
Rat | Predicted | Not recommended | Not recommended | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/100 - 1/250 | Notes Perform heat-mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol. |
Species | Dilution info | Notes |
---|---|---|
Species Mouse, Rat | Dilution info - | Notes - |
Species | Dilution info | Notes |
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Species Human, Mouse, Rat | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human, Mouse, Rat | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/1000 - 1/10000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse, Rat | Dilution info - | Notes - |
Catalyzes the transfer of a ribitol-phosphate from CDP-ribitol to the distal N-acetylgalactosamine of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:26923585, PubMed:27194101, PubMed:29477842). This constitutes the first step in the formation of the ribitol 5-phosphate tandem repeat which links the phosphorylated O-mannosyl trisaccharide to the ligand binding moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1 (PubMed:17034757, PubMed:25279699, PubMed:26923585, PubMed:27194101, PubMed:29477842). Required for normal location of POMGNT1 in Golgi membranes, and for normal POMGNT1 activity (PubMed:17034757). May interact with and reinforce a large complex encompassing the outside and inside of muscle membranes (PubMed:25279699). Could be involved in brain development (Probable).
FCMD, FKTN, Ribitol-5-phosphate transferase FKTN, Fukutin, Fukuyama-type congenital muscular dystrophy protein, Ribitol-5-phosphate transferase
Rabbit Recombinant Monoclonal Fukutin antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 4 publications.
pH: 7.2 - 7.4
Preservative: 0.01% Sodium azide
Constituents: 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 9% PBS, 0.05% BSA
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
Fukutin also known as FKRP or FKTN is a glycosyltransferase enzyme weighing approximately 55 kDa. This protein participates in the process of adding sugar chains to proteins primarily glycosylating α-dystroglycan. Fukutin is highly expressed in muscle tissues including skeletal and cardiac muscles and plays a role in the central nervous system. Its activity is important for the proper function of these tissues.
Fukutin plays a fundamental role in maintaining the structure and function of muscle cells by participating in the glycosylation of α-dystroglycan. This modification allows α-dystroglycan to bind to extracellular matrix proteins. Fukutin operates as part of the dystrophin-glycoprotein complex which is essential for muscle integrity and stability. This complex anchors the cytoskeleton of a muscle cell to the surrounding extracellular matrix.
This protein fukutin participates in the dystroglycan pathway affecting the integrity of muscle cells. It works closely with other proteins like LARGE1 which also modifies α-dystroglycan. Fukutin's activity ensures that α-dystroglycan has the necessary post-translational modifications to perform its function within the laminin-binding pathway linking the extracellular matrix to the cytoskeleton.
Alterations in fukutin mutations can lead to muscular dystrophies such as Fukuyama congenital muscular dystrophy and Walker-Warburg syndrome. In these conditions the fukutin-related glycosylation of α-dystroglycan is disrupted which impairs muscle cell stability and function. Other proteins like dystrophin and sarcoglycans associated with the dystrophin-glycoprotein complex also play roles in these disorders further linking fukutin to muscle disease mechanisms.
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We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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All lanes: Western blot - Anti-Fukutin antibody [EPR7913] (ab131280) at 1/1000 dilution
Lane 1: HeLa cell lysate at 10 µg
Lane 2: A549 cell lysate at 10 µg
Lane 3: Fetal heart tissue lysate at 10 µg
Lane 4: BxPC-3 cell lysate at 10 µg
All lanes: HRP labelled goat anti-rabbit at 1/2000 dilution
Predicted band size: 53 kDa
Immunohistochemical analysis of paraffin-embedded Human kidney tissue labelling Fukutin with ab131280 at 1/100 dilution.
Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.
We have systematically measured KD (the equilibrium dissociation constant between the antibody and its antigen), of more than 840 recombinant antibodies to assess not only their individual KD values but also to see the average affinity of antibody.
Based on the comparison with published literature values for mouse monoclonal antibodies, Recombinant antibodies appear to be on average 1-2 order of magnitude higher affinity.
Image collected and cropped by CiteAb under a CC-BY license from the publication
Fukutin western blot using anti-Fukutin antibody [EPR7913] ab131280. Publication image and figure legend from Gerin, I., Ury, B., et al., 2016, Nat Commun, PubMed 27194101.
ab131280 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab131280 please see the product overview.
FKTN and FKRP can transfer ribitol phosphate to recombinant α-dystroglycan.(a) Schematic representation of α-dystroglycan fragments used in this study. (b) Transfer of [3H]-ribitol from CDP-[1-3H]-ribitol to α-dystroglycan (∼1 μg) by recombinant FKTN and FKRP (∼0.1 and ∼0.4 μg, respectively). After incubation for 16 h at 30 °C, proteins were recovered using streptavidin beads and incorporated radioactivity was determined with a scintillation counter. Values are means±s.d. of three biological replicates from one representative experiments out of three. Asterisks indicate P<0.05 in Student's t-test. (c) Incorporation of [32P] from [32P]-CDP-ribitol to different fragments of α-dystroglycan by FKTN and FKRP. After 16 h of incubation at 30 °C, proteins were incubated with (+) or without (−) alkaline phosphatase (AP) and resolved by SDS–PAGE. 32P was detected with a storage phosphorimager. (d) Effect of deglycosylation of α-dystroglycan (aa 1–485) with a ‘deglycosylation mix' on the incorporation of radioactivity from [32P]-CDP-ribitol catalysed by FKRP or FKTN. The deglycosylation treatment of α-dystroglycan performed either before (two left panels) or after (two right panels) ribitol-phosphorylation decreased the apparent molecular weight of α-dystroglycan, but did not reduce the incorporated radioactivity.
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