SI

  • Official Full Name

    sucrase-isomaltase (alpha-glucosidase)
  • Overview

    This gene encodes a sucrase-isomaltase enzyme that is expressed in the intestinal brush border. The encoded protein is synthesized as a precursor protein that is cleaved by pancreatic proteases into two enzymatic subunits sucrase and isomaltase. These two subunits heterodimerize to form the sucrose-isomaltase complex. This complex is essential for the digestion of dietary carbohydrates including starch, sucrose and isomaltose. Mutations in this gene are the cause of congenital sucrase-isomaltase deficiency.
  • Synonyms

    SI;sucrase-isomaltase (alpha-glucosidase);sucrase isomaltase;sucrase-isomaltase, intestinal;Oligosaccharide alpha 1;6 glucosidase;Isomaltase;MGC131621;MGC131622;Oligosaccharide alpha 1, 6 glucosidase;sucrase isomaltase alpha glucosidase;SUIS_HUMAN;OTTHUMP00000212594;oligosaccharide alpha-1,6-glucosidase

Recombinant Proteins

  • Human
  • Rat
  • Baculovirus-Insect cells
  • E. coli
  • Wheat Germ
  • Mammalian Cell
  • E.coli
  • Insect Cells
  • In vitro E. coli expression system
  • HEK293
  • His
  • Non
  • His&S
  • His&Fc&Avi
Cat.# Product name Source (Host) Species Tag Protein Length Price
SI-0515H Recombinant Human SI Protein (Asn932-Ser1827), C-His-tagged Baculovirus-Insect cells Human His Asn932-Ser1827
SI-0516H Recombinant Human SI Protein (Lys62-Trp931), C-His-tagged Baculovirus-Insect cells Human His Lys62-Trp931
SI-0517H Recombinant Human SI Protein (Lys62-Trp931), C-His-tagged E. coli Human His Thr263~Asp369
SI-29814TH Recombinant Human SI Wheat Germ Human Non 99 amino acids
SI-5396R Recombinant Rat SI Protein Mammalian Cell Rat His
SI-7918H Recombinant Human SI protein, His & S-tagged E.coli Human His&S Asn1717~Ser1827
SI-0514H Recombinant Human SI protein, His-tagged Insect Cells Human His 1008-1827 aa
SI-193H Recombinant Human SI Transmembrane protein, His-tagged In vitro E. coli expression system Human His 2-1007aa
SI-5055R Recombinant Rat SI Protein, His (Fc)-Avi-tagged HEK293 Rat His&Fc&Avi
SI-5055R-B Recombinant Rat SI Protein Pre-coupled Magnetic Beads HEK293 Rat
SI-6289H Recombinant Human SI Protein (Asn932-Ser1827), C-His tagged E.coli Human His Asn932-Ser1827
SI-6290H Recombinant Human SI protein, His-tagged E. coli Human His 1008-1827 aa

    Involved Pathway

    SI involved in several pathways and played different roles in them. We selected most pathways SI participated on our site, such as Galactose metabolism,Starch and sucrose metabolism,Metabolic pathways, which may be useful for your reference. Also, other proteins which involved in the same pathway with SI were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein
    Starch and sucrose metabolism GPIA,HKDC1,G6PC3,UGT1A4,TREH,G6PCA.1,GUSB,AMY2A4,GANC,UGT1A3
    Galactose metabolism GLA,UGP2A,G6PC,PFKM,G6PC2,PGM1,PGM2,Akr1b3,GLB1,GALK1
    Metabolic pathways DHRS4L2,MTMR6,MUT,CRYL1,UCK2B,FAM213B,B3GNT5,IMPDH1B,MTHFR,NADKB
    Carbohydrate digestion and absorption PRKCB,HK3,AMY1B,AKT1,AKT2,GNAT3,AMY2A,ATP1B4,TAS1R3,PIK3R2

    Protein Function

    SI has several biochemical functions, for example, alpha-1,4-glucosidase activity,carbohydrate binding,oligo-1,6-glucosidase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by SI itself. We selected most functions SI had, and list some proteins which have the same functions with SI. You can find most of the proteins on our site.

    Function Related Protein
    alpha-1,4-glucosidase activity GANC
    carbohydrate binding CLEC2H,ITLN1,CLC,LAYN,GRIFIN,REG1B,CLEC4A2,CD209B,REG3G,PRG3

    Interacting Protein

    SI has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with SI here. Most of them are supplied by our site. Hope this information will be useful for your research of SI.

    Resources

    References

    • Nguyen, AT; van Doorn, R; et al. Flow-Through Microbial Capture by Antibody-Coated Microsieves. ADVANCED MATERIALS INTERFACES 2:-(2015).
    • Ko, KI; Coimbra, LS; et al. Diabetes reduces mesenchymal stem cells in fracture healing through a TNF alpha-mediated mechanism. DIABETOLOGIA 58:633-642(2015).

    Reviews

    Q&As

    There is a weak signal in lane 1 at a somewhat higher MW of ~130 kD for SI-0515H. I presume this is the actual enzyme which appears as a ~130 kD protein. This was also observed in the COA for SI-1516H, as shown below, but with a much higher signal. The concentrations of SI-0515H and SI-0516H are 0.12 mg/mL and 0.38 mg/mL, respectively. The signal in the Western blots do not scale comparably for the two enzymes. Am I reading these WB correctly, and if so, what may could account for what appears to be >50-fold differences in signal whereas there only a ~3-fold difference in protein concentration? 09/11/2024

    The strength of the WB band signal is not only related to the protein concentration, but also related to the binding affinity between protein and the antibody. Due to the differences in structure, SI-0515H and SI-0516H could have different binding affinity to the antibody, thus the WB results are different.

    Would it be fair to say that the higher MW band of ~130kD in Lane 1 for both enzymes is likely due to glycosylation? 09/11/2024

    Yes, it is likely that the band shifting was due to glycosylation.

    I see that the expression system was changed from baculovirus to HEK293 from the samples provided back in April compared with the two recent samples. The WB from the samples in April are shown below, which shows a primary signal at ~105 kD, along with some minor bands at 70-80 kD. Was the shift the HEK293 due to the fact that only a single band showed up in the WB? 09/11/2024

    Different expression system has different post-translational modification. The SI proteins expressed from HEK293 were in soluble form, which is more close to its native status.

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