Anti-TGG2 | Myrosinase 2 ( BGL37)

(Cat#: AS20 4415)
AS20_4415
AS20_4415_1
Description
  • Immunogen: BSA-conjugated peptide, derived from N-terminus of Arabidopsis thaliana TGG2, UniProt: Q9C5C2 , TAIR: At5g25980
  • Host: Rabbit
  • Clonality: Polyclonal
  • Purity: Total IgG. Protein A purified in PBS, 50% glycerol. Filter sterilized.
  • Format: Liquid at 2 mg/ml.
  • Quantity: 200 µg
  • Storage: Store at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
  • Tested applications: ELISA (ELISA), Immunolocalisation (IL), Western blot (WB)
  • Recommended dilutions: assay dependent (ELISA), (IL), 1: 1000 (WB)
  • Expected | apparent MW: 63 | 70 kDa
  • Confirmed reactivity: Arabidopsis thaliana
  • Not reactive in: No confirmed exceptions from predicted reactivity are currently known
  • TGG2 | Myrosinase 2 ( BGL37) may degrade glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products: thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones. These toxic degradation products can deter insect herbivores. Seems to function in abscisic acid (ABA) and methyl jasmonate (MeJA) signaling in guard cells. Functionally redundant with TGG1. Cellular localisation: vacuole. Alternative names: Beta-glucosidase 37, AtBGLU37, Sinigrinase 2, Thioglucosidase 2.
  • Liebminger et al. (2012). Myrosinases TGG1 and TGG2 from Arabidopsis thaliana contain exclusively oligomannosidic N-glycans. Phytochemistry. 2012 Dec;84(21):24-30.doi: 10.1016/j.phytochem.2012.08.023. (Western blot)Shirakava et al. (2010). Arabidopsis Qa-SNARE SYP2 proteins localized to different subcellular regions function redundantly in vacuolar protein sorting and plant development. Plant J. 2010 Dec;64(6):924-35.doi: 10.1111/j.1365-313X.2010.04394.x. (Western blot)Ueda et al. (2006). AtVAM3 is required for normal specification of idioblasts, myrosin cells. Plant Cell Physiol. 2006 Jan;47(1):164-75. doi: 10.1093/pcp/pci232. (Immunolocalisation, Western blot)
  • Signal peptide of 28 amino acids is removed from N-termins. Three glycosylation sites were identified in the mature form of the protein.Antibody specificity has been confirmed using wild-type and tgg2-1 mutant Ueda et al. (2006).

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