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>   首页   >   产品   >   一抗   >   细胞生物学   >   LARGE Antibody (Center)   

LARGE Antibody (Center)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - LARGE Antibody (Center) AP21980c
    Anti-LARGE Antibody (Center) at 1:2000 dilution + Jurkat whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 88 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession O95461
Other Accession Q66PG4, Q66PG1, Q8N3Y3, Q66PG3, Q66PG2, Q9Z1M7
Reactivity Human, Mouse
Predicted Chicken, Human, Mouse
Host Rabbit
Clonality polyclonal
Isotype Rabbit IgG
Calculated MW 88066 Da
Additional Information
Gene ID 9215
Other Names Glycosyltransferase-like protein LARGE1, 2.4.-.-, Acetylglucosaminyltransferase-like 1A, Xylosyltransferase LARGE, 2.4.2.-, Beta-1, 3-glucuronyltransferase LARGE, 2.4.1.-, LARGE, KIAA0609, LARGE1
Target/Specificity This LARGE antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 365-398 amino acids from the Central region of human LARGE.
Dilution WB~~1:2000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsLARGE Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name LARGE1 (HGNC:6511)
Synonyms KIAA0609, LARGE
Function Bifunctional glycosyltransferase with both alpha-1,3- xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the maturation of alpha-dystroglycan (DAG1) by glycosylation leading to DAG1 binding to laminin G-like domain- containing extracellular proteins with high affinity (PubMed:15661757, PubMed:15752776, PubMed:21987822, PubMed:22223806, PubMed:23125099, PubMed:25279697, PubMed:25279699). Elongates the glucuronyl-beta-1,4- xylose-beta disaccharide primer structure initiated by B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (PubMed:22223806, PubMed:23125099, PubMed:25138275, PubMed:25279697, PubMed:25279699, PubMed:32975514). Requires the phosphorylation of core M3 (O-mannosyl trisaccharide) by POMK to elongate the glucuronyl-beta-1,4-xylose-beta disaccharide primer (PubMed:21987822). Plays a key role in skeletal muscle function and regeneration (By similarity).
Cellular Location Golgi apparatus membrane; Single-pass type II membrane protein
Tissue Location Ubiquitous. Highest expression in heart, brain and skeletal muscle.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

Bifunctional glycosyltransferase with both xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine- beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:22223806). Phosphorylated O- mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity and plays a key role in skeletal muscle function and regeneration. LARGE elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated by B3GNT1/B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (PubMed:25279699).

REFERENCES

Peyrard M.,et al.Proc. Natl. Acad. Sci. U.S.A. 96:598-603(1999).
Nagase T.,et al.DNA Res. 5:31-39(1998).
Collins J.E.,et al.Genome Biol. 5:R84.1-R84.11(2004).
Dunham I.,et al.Nature 402:489-495(1999).
Fujimura K.,et al.Biochem. Biophys. Res. Commun. 329:1162-1171(2005).

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