Anti-tdTomato, AlpSdAbs® VHH(iFluor488)
Code: 026-101-007
Specification:
Applications: WB,ELISA,ICC/IF,Flow Cyt
Reactivity: tdTomato
Conjugate: iFluor488
Advantages:
High lot-to-lot consistency Increased sensitivity and higher affinity Animal-free production
Product Detail
Product Detail
Description:
Anti-tdTomato, AlpSdAbs® VHH(iFluor488) is designed for detecting tdTomato fusion proteins. Anti-tdTomato, AlpSdAbs® VHH(iFluor488) is based on monoclonal, recombinant, single domain antibody to tdTomato coupled to iFluor488. Based on immunoelectrophoresis and/or ELISA, Anti-tdTomato, AlpSdAbs® VHH(iFluor488) detects the tdTomato selectively, no reactivity with other proteins.
Immunogen: tdTomato
Host: Alpaca pacous
Isotype: VHH domain of alpaca IgG2b/2c
Conjugate: iFluor488(Ex: 495nm, Em: 519nm)
Specificity: tdTomato
Cross-Reactivity: Highly selective for tdTomato
Purity: Recombinant Expression and Affinity purified
Concentration: 1mg/ml
Formation: Liquid, 10mM PBS (pH 7.5), 0.05% sucrose, 0.1% trehalose, 0.01% proclin300, 50% Glycerol
Storage: Store at –20 °C(Avoid freeze / thaw cycles), protect from light
Background:
The tandem dimer Tomato (tdTomato) is a genetically improved version of Discosoma sp. fluorescent protein (dsRed). tdTomato is an extremely bright red fluorescent protein, being one of the brightest red-shifted fluorescent proteins available and six times brighter than eGFP. One of the main advantages of fluorescent proteins is that they do not require substrates or reagents for detection, however most of them do need oxygen for the formation of their chromophores. Besides, fluorescent proteins can be measured without lysing cells, whereas this is difficult for luciferases. One of the biggest disadvantages of fluorescent reporters is that they need to overcome cellular autofluorescence. However, in general cellular autofluorescence is lower for the emission wavelength of the red channel, favoring a red fluorescent protein such as tdTomato.
VHH are single-domain antibodies derived from the variable regions of heavy chain of Camelidae immunoglobulin. The size of VHH is extremely small(<15KDa) compared to other forms of antibody fragment, which significantly increase the permeability of VHH. Thus VHH is considered of great value for research, diagnostics and therapeutics.
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