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AB34717

Rhodamine Anti-R Phycoerythrin/rpeA antibody

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(1 Publication)

Goat Polyclonal PHEB antibody - conjugated to Rhodamine. Suitable for Flow Cyt, WB, IM and reacts with Red Algae samples. Cited in 1 publication.

View Alternative Names

R phycoerythrin alpha subunit, R phycoerythrin beta subunit, rpeA, rpeB

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Conjugation

Rhodamine

Excitation/Emission

Ex: 550nm, Em: 570nm

Carrier free

No

Reacts with

Red Algae

Applications

Flow Cyt, WB, IM

applications

Specificity

This antibody recognizes R Phycoerythrin/rpeA conjugated IgG. It will also cross react with B Phycoerythrin.

Reactivity data

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Product details

Label: Tetramethylrhodamine isothiocyanate (TRITC) (Molecular Weight 444 daltons). Absorption Wavelength: 550 nm. Emission Wavelength: 570 nm. Fluorochrome/Protein Ratio: 4.0 moles TRITC per mole of Goat IgG.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
This antibody was purified from monospecific antiserun by immunoaffinity chromatography using a R Phycoerythrin/rpeA coupled to agarose beads followed by solid phase adsorption to remove any unwanted reactivities.
Storage buffer
Preservative: 0.01% Thimerosal (merthiolate) Constituents: 1% BSA, 0.88% Sodium chloride, 0.424% Potassium phosphate solution
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

R Phycoerythrin also known as rpeA is a light-harvesting protein found mainly in red algae and cyanobacteria. It plays a mechanical role in collecting light energy and assisting in photosynthesis. R Phycoerythrin features a mass of approximately 240 kDa and expresses primarily within the cells of these aquatic organisms. Its bright red color and fluorescence make it important in various biotechnological applications including bioimaging and flow cytometry.
Biological function summary

This chromoprotein functions as part of the phycobilisome complex serving as an accessory pigment that captures light and transfers energy to chlorophyll. This complex enhances the efficiency of photosynthesis by expanding the range of light wavelengths that organisms can use. The phycobilisome complex attaches to the thylakoid membranes aiding in the capture and channeling of light energy. Given these capabilities R Phycoerythrin proves to be an important component in maximizing photonic energy conversion within these photosynthetic organisms.

Pathways

R Phycoerythrin plays an important part in the photosynthetic light-harvesting pathway where it directly transmits energy to photosystem II. It engages with other proteins such as allophycocyanin and chlorophyll-binding proteins to optimize the capture of light. This efficient pathway enables organisms to perform photosynthesis even under low-light conditions ensuring survival in diverse aquatic environments.

Abnormal expressions or malfunctions within this light-harvesting system do not frequently align directly with human diseases. However R Phycoerythrin's analogous pigments in other biological contexts may offer insights into photodamage and oxidative stress-related disorders. While the absence of direct association with specific human disorders limits its direct medical implications its study aids in understanding similar conditions linked to oxidative stress and metabolic processes.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Scientific reports 3:3171 PubMed24201379

2013

Identification of telomere-associated molecules by engineered DNA-binding molecule-mediated chromatin immunoprecipitation (enChIP).

Applications

Unspecified application

Species

Unspecified reactive species

Toshitsugu Fujita,Yoshinori Asano,Junko Ohtsuka,Yoko Takada,Kazunobu Saito,Rieko Ohki,Hodaka Fujii
View all publications

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