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{{/_source.additionalInfo}}Anti-12S seed storage protein CRC
(Cat#: AS20 4403)
Description
- Immunogen: Native, 12S globulin alpaha subunit purified from Arabidopsis thaliana and excised from SDS-PAGE gel. UniProt: Q96318, TAIR: At4g28520
- 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), Immunolocalization (IL) using electron microscopy, Immunohistochemistry (IHC), Western blot (WB)
- Recommended dilutions: Assay dependent (ELISA), 1: 50 (IL by electron microscopy), 1: 100 (IHC), 1: 3000 - 1: 10 000 (WB)
- Expected | apparent MW: 58 | 30 kDa (alpha subunit)
- Confirmed reactivity: Arabidopsis thaliana
- Not reactive in: No confirmed exceptions from predicted reactivity are currently known
- Major 12S seed storage protein CRC (globulin) is synthesized on the endoplasmic reticulum as precursor and then transported to storage vacuoles, where it is processed at a conserved Asn-Gly peptide bond by an asparaginyl endopeptidase to produce two mature polypeptides referred to as alpha and beta subunits that are joined together by a disulfide bond. Phosphorylated in seeds on some Tyr residues in response to abscisic acid (ABA). 12S CRC protein is cleaved to alpha and beta chains. Cellular localisation: vacuole.Alternative protein names: Cruciferin 3, Cruciferin C Legumin-type globulin Cruciferin1, Legumin-type globulin storage protein CRU1.
- Shirakawa et al. (2014). CONTINUOUS VASCULAR RING (COV1) is a trans-Golgi network-localized membrane protein required for Golgi morphology and vacuolar protein sorting. Plant Cell Physiol. 2014 Apr;55(4):764-72.doi: 10.1093/pcp/pct195. (Immunohistochemistry, Western blot)Li et al. MAG2 and three MAG2-INTERACTING PROTEINs form an ER-localized complex to facilitate storage protein transport in Arabidopsis thaliana. Plant J. 2013 Dec;76(5):781-91.doi: 10.1111/tpj.12347. (Immunolocalisation by electron microscopy, Western blot)
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