LM10 [Anti-Xylan] Antibody

LM10 Anti-Xylan Antibody AB-LM10
Reference code: AB-LM10

2 mL

This product has been discontinued

Content: 2 mL
Shipping Temperature: Ambient
Storage Temperature: Short term stability: 2-8oC,
Long term stability: Below -10oC (Avoid freeze/thaw cycles)
Physical Form: Liquid
Stability: > 4 years at 4oC
Antibody Name: LM10
Antigen: Heteroxylan
Epitope: Unsubstituted β-1,4-Xylan
Conjugate: Unconjugated
Buffer: Serum-free cell culture supernatant, 0.02% sodium azide
Tested Application: Immunofluorescence (1:10); ELISA (1:10)
Positive Control: Xylan (Beechwood; purified) (P-XYLNBE)
Clonality: Monoclonal
Isotype: IgG2c
Host Species: Rat

This product has been discontinued (read more).

The LM10, rat, monoclonal antibody was generated using a neoglycoprotein (xylopentaose-BSA) and is a high affinity antibody to the non-reducing end of (1,4)-β-D-xylosyl residues that constitute the backbone of xylans. LM10 antibody has no cross-reactivity to highly substituted xylan such as wheat arabinoxylan where the xylan backbone is substituted with sidechains of arabinofuranosyl residues.

From the laboratory of Paul Knox, PhD, University of Leeds.

This product does not contain fetal bovine serum.

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Data Sheet

Dynamic changes in primexine during the tetrad stage of pollen development.

Wang, R., Owen, H. A. & Dobritsa, A. A. (2021). Plant Physiology, kiab426.

Formation of pollen wall exine is preceded by the development of several transient layers of extracellular materials deposited on the surface of developing pollen grains. One such layer is primexine (PE), a thin, ephemeral structure that is present only for a short period of time and is difficult to visualize and study. Recent genetic studies suggested that PE is a key factor in the formation of exine, making it critical to understand its composition and the dynamics of its formation. In this study, we used high-pressure frozen/freeze-substituted samples of developing Arabidopsis (Arabidopsis thaliana) pollen for a detailed transmission electron microscopy analysis of the PE ultrastructure throughout the tetrad stage of pollen development. We also analyzed anthers from wild-type Arabidopsis and three mutants defective in PE formation by immunofluorescence, carefully tracing several carbohydrate epitopes in PE and nearby anther tissues during the tetrad and the early free-microspore stages. Our analyses revealed likely sites where these carbohydrates are produced and showed that the distribution of these carbohydrates in PE changes significantly during the tetrad stage. We also identified tools for staging tetrads and demonstrate that components of PE undergo changes resembling phase separation. Our results indicate that PE behaves like a much more dynamic structure than has been previously appreciated and clearly show that Arabidopsis PE creates a scaffolding pattern for formation of reticulate exine.

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