Rabbit Polyclonal RDH5 antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human RDH5 aa 100-250.
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 20% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
IHC-P | WB | |
---|---|---|
Human | Tested | Tested |
Cow | Predicted | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/100.00000 - 1/500.00000 | Notes Use 10mM Citrate buffer or Tris-EDTA buffer (pH8.0) Perform heat-mediated antigen retrieval before commencing with IHC staining protocol. |
Species | Dilution info | Notes |
---|---|---|
Species Cow | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/500.00000 - 1/3000.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Cow | Dilution info - | Notes - |
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Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner (PubMed:10588954, PubMed:11675386, PubMed:9115228, PubMed:9931293). Has no activity towards all-trans retinal (By similarity). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE). Also recognizes steroids (androsterone, androstanediol) as its substrates (PubMed:29541409, PubMed:9931293).
HSD17B9, RDH1, SDR9C5, RDH5, Retinol dehydrogenase 5, 11-cis retinol dehydrogenase, 9-cis retinol dehydrogenase, Short chain dehydrogenase/reductase family 9C member 5, 11-cis RDH, 11-cis RoDH, 9cRDH
Rabbit Polyclonal RDH5 antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human RDH5 aa 100-250.
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 20% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
RDH5 also known as retinol dehydrogenase 5 or 11-cis retinol dehydrogenase is an enzyme that plays an important role in the visual cycle. It has a molecular mass of approximately 35 kDa and primarily functions in the conversion of 11-cis-retinol to 11-cis-retinal which is a significant step in the biosynthesis of visual pigments. RDH5 is expressed mainly in the retinal pigment epithelium of the eye where it contributes to maintaining proper vision.
11-cis retinol dehydrogenase facilitates the regeneration of 11-cis-retinal from 11-cis-retinol a critical process for photoreceptor cell function and visual cycle continuity. RDH5 operates as part of a complex of enzymes involved in the retinoid cycle which is essential for maintaining a continuous supply of 11-cis-retinal. Without RDH5 the regeneration of 11-cis-retinal would be ineffective reducing the ability to see especially in low-light conditions.
The retinol dehydrogenase 5 enzyme plays a major role in the visual cycle pathway. This pathway is necessary for converting retinoids into visual chromophores that allow vision. RDH5 interacts closely with other key enzymes such as RPE65 and RDH12 which also participate in retinoid transformations. The proper functioning of the visual cycle pathway depends on the actions of these enzymes to ensure the availability of 11-cis-retinal for photoreceptor function.
Defects in the RDH5 gene can lead to retinal degenerative diseases like fundus albipunctatus and retinitis pigmentosa. These conditions are characterized by night blindness and progressive vision loss. Mutations in RDH5 affect the synthesis of 11-cis-retinal disrupting the visual cycle and contributing to these diseases. RDH5 shares a pathway with RPE65 another protein implicated in retinal disorders highlighting the interconnectedness of proteins involved in the visual cycle and their impact on eye health.
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10% SDS-PAGE
All lanes: Western blot - Anti-RDH5 antibody (ab101457) at 1/1000 dilution
All lanes: NT2D1 whole cell lysate at 30 µg
Predicted band size: 35 kDa
Immunohistochemical analysis of RDH5 in paraffin-embedded Cal27 xenograft, using ab101457 at 1/100 dilution.
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