Rat MAb details

Overview list and short guide to our antibody probes PDF

Explore probe details and links below

Heteroxylan

LM10 – MONOCLONAL ANTIBODY to XYLAN / LM10 (Rat IgG2c)
SPECIFICITY: Generated using a neoglycoprotein (xylopentaose-BSA). It recognizes the non-reducing end (NRE) of xylans in several species. It has no cross-reactivity with wheat arabinoxylan most likely due to a modified NRE in this polymer. ►McCartney et al. (2005) J. Histochem. Cytochem 53, 543-546 ►Ruprecht et al. (2017) Plant Physiology 175, 1094-1104 

LM11 – MONOCLONAL ANTIBODY to XYLAN / ARABINOXYLAN / LM11 (Rat IgM)
SPECIFICITY: Generated using a neoglycoprotein (xylopentaose-BSA). It recognises an unsubstituted epitope of xylan backbones and binds strongly to wheat arabinoxylan differentiating it from LM10. ►McCartney et al. (2005) J. Histochem. Cytochem 53, 543-546 ►Ruprecht et al. (2017) Plant Physiology 175, 1094-1104 

LM28 – MONOCLONAL ANTIBODY to GLUCURONOXYLAN / LM28 (Rat IgM)
SPECIFICITY: Generated using a complex pectic immunogen. The monoclonal antibody can recognise glucuronosyl substituted xylans in several species and MeGlcA is not required for recognition. ►Cornuault et al. (2015) Planta 242, 1321-1334.

LM27 – MONOCLONAL ANTIBODY to GRASS XYLAN PREPARATIONS / LM27 (Rat IgM)
SPECIFICITY: Generated using a complex pectic immunogen. Epitope is unknown but LM27 binds strongly to preparations of grass xylan/glucuronoxylan and is likely to be an epitope of a complex substitution of grass heteroxylan or an associated molecule. ►Cornuault et al. (2015) Planta 242, 1321-1334.

Xyloglucan

LM15 – MONOCLONAL ANTIBODY to XYLOGLUCAN / LM15 (Rat IgG2c)
SPECIFICITY: Generated using a neoglycoprotein incorporating the xylosylated heptasaccharide from tamarind xyloglucan (XXXG-BSA). It recognises the XXXG motif of xyloglucan in several species and can accommodate to some extent a single galactosyl residue. ►Marcus et al. (2008) BMC Plant Biology 8:60

LM24 – MONOCLONAL ANTIBODY to XYLOGLUCAN / LM24, (Rat IgG2a)
SPECIFICITY: Generated using a neoglycoprotein incorporating the xylosylated/galactosylated oligosaccharides from tamarind xyloglucan (XXLG & XLLG). It binds preferentially to the galactosylated XLLG oligosaccharide motif. ►Pedersen et al. (2012) J. Biol Chem. 47, 39429–39438

LM25 – MONOCLONAL ANTIBODY to XYLOGLUCAN / LM25, (Rat IgM)
SPECIFICITY: Generated using a neoglycoprotein incorporating the xylosylated/galactosylated oligosaccharides from tamarind xyloglucan (XXLG & XLLG). It recognises a range of xyloglucan-specific oligosaccharide motifs in several species. ►Pedersen et al. (2012) J. Biol Chem. 47, 39429–39438

Heteromannan

LM21 – MONOCLONAL ANTIBODY to HETEROMANNAN / LM21 (Rat IgM)
SPECIFICITY: This antibody recognises β-linked mannan polysaccharides of plant cell walls. It has no known cross-reactivity with other polymers and can recognise heteromannan polysaccharides in several species. LM21 binds effectively to β-(1→4)-manno-oligosaccharides from DP2 to DP5. LM21 displays a wide recognition of mannan, glucomannan and galactomannan polysaccharides. ►Marcus et al. (2010) Plant Journal  64, 191-203

LM22 – MONOCLONAL ANTIBODY to HETEROMANNAN / LM22 (Rat IgM)
SPECIFICITY: This antibody recognises β-linked mannan polysaccharides of plant cell walls. It has no known cross-reactivity with other polymers and can recognise heteromannan polysaccharides in several species. LM22 binds effectively to β-(1→4)-manno-oligosaccharides from DP2 to DP5. LM22 displays recognition of mannan and glucomannan polymers although the basis of its lack of recognition of galactomannan polysaccharides is not clear. ►Marcus et al. (2010) Plant Journal 64, 191-203

Pectin

JIM5 – MONOCLONAL ANTIBODY to HOMOGALACTURONAN / JIM5 (Rat IgG)
SPECIFICITY: The antibody recognises the homogalacturonan domain of pectic polysaccharides. It has no known cross-reactivity with other polymers. It can recognise pectic polysaccharides in several species. The antibody recognises partially methyl-esterified epitopes of homogalacturonan and can also bind to un-esterified homogalacturonan. We now recommend the use of LM19 in the place of JIM5 as LM19 binds more effectively to unesterified HG. ►Knox et al. (1990) Planta 181, 512-521 ►Clausen et al. (2003) Carbohydr. Res. 338, 1797-1800 ►Verhertbruggen et al. (2009) Carbohydr. Res344, 1858–1862

JIM7 – MONOCLONAL ANTIBODY to HOMOGALACTURONAN / JIM7, (Rat IgA)
SPECIFICITY: The antibody recognises homogalacturonan polysaccharides and has no known cross-reactivity with other polymers. The antibody recognises partially methyl-esterified epitopes of homogalacturonan but does not bind to un-esterified homogalacturonan. We now recommend the use of LM20 as an antibody probe for methyl-esterified homogalacturonan. JIM7 can be a good general probe for pectic homogalacturonan. ►Knox et al. (1990) Planta 181, 512-521  ►Clausen et al. (2003) Carbohydr. Res. 338, 1797-1800  ►Verhertbruggen et al. (2009) Carbohydr. Res344, 1858–1862

LM7 – MONOCLONAL ANTIBODY to HOMOGALACTURONAN / LM7 (Rat IgM) 
SPECIFICITY: The antibody recognises the homogalacturonan domain of pectic polysaccharides. It can recognise pectic polysaccharides in several species. The antibody recognises a partially methyl-esterified epitope of HG that results from non-blockwise de-esterification processes. It does not bind to un-esterified homogalacturonan. ►Willats et al. (2001) J. Biol. Chem 276, 19404-19413 ►Clausen et al. (2003) Carbohydr. Res. 338, 1797-1800

LM18 – MONOCLONAL ANTIBODY to HOMOGALACTURONAN / LM18 (Rat IgG2c) 
SPECIFICITY: The antibody recognises the homogalacturonan domain of pectic polysaccharides. It has no known cross-reactivity with other polymers. It can recognise pectic polysaccharides in several species. The antibody has some preference for partially methyl-esterified homogalacturonan but can also bind to un-esterified homogalacturonan. ►Verhertbruggen et al. (2009) Carbohydr. Res344, 1858–1862

LM19 – MONOCLONAL ANTIBODY to HOMOGALACTURONAN / LM19 (Rat IgM)
SPECIFICITY: The antibody recognises the homogalacturonan domain of pectic polysaccharides. It has no known cross-reactivity with other polymers. It can recognise pectic polysaccharides in several species. The antibody recognises a range of homogalacturonan samples but appears to have a preference for and binds strongly to un-esterified homogalacturonan. We now recommend the use of LM19 in the place of JIM5 as LM19 binds more effectively to unesterified HG. ►Verhertbruggen et al. (2009) Carbohydr. Res344, 1858–1862

LM20 – MONOCLONAL ANTIBODY to HOMOGALACTURONAN / LM20 (Rat IgM)
SPECIFICITY: The antibody recognises the homogalacturonan domain of pectic polysaccharides. It has no known cross-reactivity with other polymers. It can recognise pectic polysaccharides in several species. The antibody requires methyl-esters for recognition of homogalacturonan and does not bind to un-esterified homogalacturonan. We now recommend the use of LM20 in the place of JIM7 as LM20 binding is more effectively lost by high pH treatments that remove HG methyl esters. ►Verhertbruggen et al. (2009) Carbohydr. Res344, 1858–1862

LM8 – MONOCLONAL ANTIBODY to XYLOGALACTURONAN / LM8 (Rat IgM)
SPECIFICITY: The antibody recognises a specific epitope of a xylogalacturonan pectic polysaccharide that is associated with cell detachment and separation in a wide range of species. It has no known cross-reactivity with other polymers. This antibody does NOT bind to all xylogalacturonans. ►Willats et al. (2004) Planta  218, 673-681

LM5 – MONOCLONAL ANTIBODY to (1-4)-β-D-GALACTAN  / LM5 (Rat IgG)
SPECIFICITY: The antibody was generated using a neoglycoprotein (galactotetraose-BSA). It recognises a linear tetrasaccharide in (1-4)-β-D-galactans. It has no cross-reactivity with (1-3)-β-D-galactans or (1-6)-β-D-galactans. It can recognise pectic polysaccharides in several species. In competitive inhibition ELISA, antibody binding to (1-4)-β-D-galactan was inhibited (50%) by 58 µg/ml (1-4)-β-D-galactotetraose and by 0.7 µg/ml lupin (1-4)-β-D-galactan. LM5 is now known to bind specifically to the non-reducing end of galactan ►Jones et al. (1997) Plant Physiol. 113, 1405-1412 Andersen et al. (2016) Carbohydrate Research 436, 36-40

LM26 – MONOCLONAL ANTIBODY to BRANCHED-GALACTAN / LM26 (Rat IgG)
SPECIFICITY: The antibody was isolated from a wide screen of cell lines obtained subsequent to immunization with cell wall polysaccharides. Glycan microarrays indicated that LM26 recognises a (1-6)-galactosyl substitution in (1-4)-beta-D-galactans and that it has no recognition of linear (1-4)-beta-D-galactan. LM26 can recognise pectic polysaccharides in several species and in a wide range of plant organs the LM26 epitope can be specifically detected in cell walls of phloem sieve elements. ►Torode et al. (2018) Plant Physiol. 176, 1547-1558

LM9 – MONOCLONAL ANTIBODY to FERULOYLATED-(1-4)-β-D-GALACTAN / LM9 (Rat IgM)
SPECIFICITY: The antibody recognises a specific epitope of a feruloylated-(1-4)-β-D-galactan that is a structural feature of the pectic polymers of plant species of the Amaranthaceae/Chenopodiaceae. It has no known cross-reactivity with other polymers. In competitive inhibition ELISAs, antibody binding to sugar beet pectin was inhibited (50%) by 15 μg/ml O-[6-O-(trans-feruloyl)-β-d-galactopyranosyl]-(1→4)-D-galactopyranose. ►Clausen et al. (2004) Planta  219, 1036-1041

LM6 – MONOCLONAL ANTIBODY to (1-5)-α-L-ARABINAN / LM6 (Rat IgG)
SPECIFICITY: Generated using a neoglycoprotein (arabinoheptaose-BSA). Recognises a linear pentasaccharide in (1-5)-α-L-arabinans. It can recognise pectic polysaccharides in several species. It has no cross-reactivity with gum arabic but it may recognize arabinogalactan-proteins (AGPs) in some species. In competitive inhibition ELISAs, antibody binding to (1-5)-α-L-arabinan was inhibited (50%) by 40 ng/ml (1-5)-α-L-arabinopentaose and 19 ng/ml (1-5)-α-L-arabinohexaose. ►Willats et al. (1998) Carbohydr. Res. 308, 149-152

LM6-M – MONOCLONAL ANTIBODY to (1-5)- α -L-ARABINAN / LM6-M (Rat IgM)
SPECIFICITY: LM6-M was generated using a preparation of sugar beet RG-I oligosaccharides. LM6-M has a similar specificity to LM6 and binds to a linear (1-5)-a-L-arabinan. Unlike LM6 (which is an IgG immunoglobulin) LM6-M is of the IgM isotype. In competitive inhibition ELISA, LM6-M binding to (1-5)-a-L-arabinan was inhibited (50%) by 7.9 µg/ml (1-5)-a-L-arabinopentaose and 3.2 µg/ml (1-5)-a-L-arabinohexaose. LM6-M can recognise pectic polysaccharides in several species. It has no cross-reactivity with gum Arabic but it may recognize arabinogalactan-proteins (AGPs) in some species. ►Cornuault et al. (2017) BioRxiv

LM13 – MONOCLONAL ANTIBODY to (1-5)-α-L-ARABINAN (linear) / LM13 (Rat IgM)
SPECIFICITY: Isolated from a high throughput screen of antibodies generated subsequent to immunization with a pectic fraction. Recognises a linear epitope in (1-5)-α-L-arabinans. Antibody recognition of arabinans increases with arabinofuranosidase action. This antibody binds to a specific subset of pectic arabinans, and to longer stretches of 1,5-linked arabinosyl residues that are likely to be more abundant in unbranched arabinans. The binding of LM13 is highly sensitive to arabinanase action. ►Moller et al. (2007) Glycoconjugate J. 25, 37-48 ►Verhertbruggen et al. (2009) Plant J. 59, 413-425.

LM16 – MONOCLONAL ANTIBODY to PROCESSED ARABINAN RG-I / LM16 (Rat IgM)
SPECIFICITY: Generated subsequent to immunization with a pectic fraction. Recognises a epitope associated with arabinans and can be generated by arabinofuranosidase action and the loss of arabinosyl residues. The binding of LM16 is sensitive to galactosidase action and the epitope may involve galactosyl residue(s) on RG backbones. ►Verhertbruggen et al. (2009) Plant J. 59, 413-425

Miscellaneous glycans and glycoproteins

LM12 – MONOCLONAL ANTIBODY to FERULOYLATED POLYMERS / LM12 (Rat IgG2c)
SPECIFICITY: The antibody recognises an epitope containing ferulic acid that is a structural feature of the pectic polymers of plant species of the Amaranthaceae/Chenopodiaceae AND also of the heteroxylan polymers of commelinid monocotyledons. It has no known cross-reactivity with non-feruloylated polymers outside these taxonomic groups. ►Pedersen et al. (2012) J. Biol Chem. 47, 39429–39438

LM23 – MONOCLONAL ANTIBODY to XYLOSYL / LM23 (Rat IgM)
SPECIFICITY: The antibody recognises non-acetylated xylosyl residues in a range of polysaccharide contexts including both pectic xylogalacturonan and xylan. ►Manabe et al. (2011) Plant Physiol. 155, 1068-1078 ►Pedersen et al. (2012) J. Biol Chem. 47, 39429–39438

Glycoproteins

LM1 – MONOCLONAL ANTIBODY to EXTENSIN / LM1 (Rat IgM)
SPECIFICITY: Generated to rice extensin hydroxyproline-rich glycoproteins (HRGPs). The antibody recognises an epitope that is carried by a range of HRGPs of the extensin class in a wide range of angiosperm species. The LM1 epitope most likely includes glycan components of extensins. ►Smallwood et al. (1995) Planta 196, 510-522

LM2 – MONOCLONAL ANTIBODY to ARABINOGALACTAN-PROTEIN / LM2 (Rat IgM)
SPECIFICITY: Generated to rice arabinogalactan-proteins (AGPs). Recognises a carbohydrate epitope containing β-linked glucuronic acid. It can recognise AGPs in several species. In competitive inhibition ELISAs antibody binding to gum arabic was inhibited (50%) by 70 mg/ml 1-O-methyl-β-D-GlcA.  The binding of the antibody to AGPs can be fully inhibited by 10 mM 1-O-methyl-β-D-GlcA. ►Smallwood et al. (1996) Planta 198, 452-459 ►Yates et al. (1996) Glycobiology 6, 131-139

LM14 – MONOCLONAL ANTIBODY to ARABINOGALACTAN-PROTEIN / LM14, (Rat IgM)
SPECIFICITY: Isolated from a high throughput screen of antibodies generated subsequent to immunization with a pectic fraction. Recognizes arabinogalactan-proteins and will also bind to larch arabinogalactan. It can recognise AGPs in several species. ►Moller et al. (2007) Glycoconjugate J. 25, 37-48

LM30 – MONOCLONAL ANTIBODY to ARABINOGALACTAN-PROTEIN / LM30 (Rat IgM)
SPECIFICITY: Isolated subsequent to immunization with a preparation of arabinogalactan-protein (AGP) obtained from wheat grain. LM30 recognizes a glycan epitope of the wheat AGP and the recognition is highly sensitive to the action of arabinofuranosidase. ►Wilkinson et al. (2017) Journal of Cereal Science 74, 155-164

Fucoidan and Alginate (BAMs)

Fucoidan

Torode TA, Marcus SE, Jam M, Tonon T, Blackburn RS, Hervé C, Knox JP (2015) Monoclonal antibodies directed to fucoidan preparations from brown algae. PloS ONE 10, e0118366 ONLINE

BAM1 un-sulfated epitope present in sulfated fucan/fucoidan preparations
BAM2 sulfated epitope present in sulfated fucan/fucoidan preparations
BAM3 possibly sulfated epitope present in sulfated fucan/fucoidan preparations
BAM4 sulfated epitope present in sulfated fucan/fucoidan preparations

Alginate

Torode TA, Siméon A, Marcus SE, Jam M, Le Moigne M-A, Duffieux D, Knox JP, Hervé C (2016) Dynamics of cell wall assembly during early embryogenesis in the brown alga Fucus. Journal of Experimental Botany 67, 6089-6100 ONLINE

BAM6 mannuronate-rich epitope
BAM7 mannuronate-guluronate
BAM8 mannuronate-guluronate
BAM9 mannuronate-guluronate
BAM10 mannuronate-guluronate epitope resistant to alginate lyase
BAM11 ~7 guluronate residues

JIMs

JIM-designated probes include anti-arabinogalactan-protein (AGP) and anti-extensin rat Mabs that were isolated in the John Innes Institute from 1986-1991. These include: anti-AGP: JIM4 JIM8, JIM13, JIM14, JIM15 & JIM16 and anti-extensin: JIM11, JIM12, JIM19 & JIM20. Reference details for these MAbs can be found in an  Overview list and short guide to our antibody probes here