agarose bound lectins  (Vector Laboratories)


Bioz Verified Symbol Vector Laboratories is a verified supplier
Bioz Manufacturer Symbol Vector Laboratories manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93
    Name:
    Agarose bound Concanavalin A Con A
    Description:
    Concanavalin A agarose bound recognizes α linked mannose present as part of a core oligosaccharide in many serum and membrane glycoproteins At neutral and alkaline pH Con A exists as a tetramer of four identical subunits below pH 5 6 Con A dissociates into active dimers of 52 kDa Acetylation succinylation or other derivatizations can also produce stable forms with dimeric structures See succinylated Con A Nicks in the sequence are often present in the purest preparations due to hydrolytic damage within the seeds Con A requires calcium or manganese ions at each of its four saccharide binding sites Although these divalent metal ions are bound tightly to the polypeptide structure buffers which can bind calcium such as phosphate generally should be avoided in diluting Con A since a gradual loss in activity may occur Agarose bound Con A is prepared using our affinity purified lectins Heat stable cross linked 4 agarose beads with a molecular weight exclusion limit of about 2x107 daltons are used as the solid phase matrix to which the lectins are covalently coupled The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix This coupling method provides several advantages over the traditional cyanogen bromide procedure Maximum carbohydrate binding activity of the coupled lectins is retainedLinkage is stable over a range of pH valuesConjugated proteins are not leached off the beads by Tris or other routinely used buffersNo residual charges are present after conjugation This minimizes non specific binding to the matrix Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads Each lot is tested for its binding capacity using glycoproteins known to bind the lectin This provides a guideline for the user and assures the quality of our agarose bound lectins Inhibiting Eluting Sugar mixture of 200 mM α methylmannoside 200 mM α methylglucoside 6 mg lectin ml gel
    Catalog Number:
    AL-1003
    Price:
    None
    Category:
    Proteins
    Size:
    10 ml
    Buy from Supplier


    Structured Review

    Vector Laboratories agarose bound lectins
    Agarose bound Concanavalin A Con A
    Concanavalin A agarose bound recognizes α linked mannose present as part of a core oligosaccharide in many serum and membrane glycoproteins At neutral and alkaline pH Con A exists as a tetramer of four identical subunits below pH 5 6 Con A dissociates into active dimers of 52 kDa Acetylation succinylation or other derivatizations can also produce stable forms with dimeric structures See succinylated Con A Nicks in the sequence are often present in the purest preparations due to hydrolytic damage within the seeds Con A requires calcium or manganese ions at each of its four saccharide binding sites Although these divalent metal ions are bound tightly to the polypeptide structure buffers which can bind calcium such as phosphate generally should be avoided in diluting Con A since a gradual loss in activity may occur Agarose bound Con A is prepared using our affinity purified lectins Heat stable cross linked 4 agarose beads with a molecular weight exclusion limit of about 2x107 daltons are used as the solid phase matrix to which the lectins are covalently coupled The attachment of the lectins to the beads is carefully controlled to preserve lectin activity and minimize conformational changes of the bound lectins that might result in nonspecific ionic or hydrophobic interactions The technique we have developed to couple lectins to agarose beads inserts a hydrophilic spacer arm between the lectin and the matrix This coupling method provides several advantages over the traditional cyanogen bromide procedure Maximum carbohydrate binding activity of the coupled lectins is retainedLinkage is stable over a range of pH valuesConjugated proteins are not leached off the beads by Tris or other routinely used buffersNo residual charges are present after conjugation This minimizes non specific binding to the matrix Our agarose bound lectins are supplied at a constant concentration of lectin per ml of settled beads The concentration for each lectin is selected to achieve the highest glycoconjugate binding capacity per mg of lectin present in the beads Each lot is tested for its binding capacity using glycoproteins known to bind the lectin This provides a guideline for the user and assures the quality of our agarose bound lectins Inhibiting Eluting Sugar mixture of 200 mM α methylmannoside 200 mM α methylglucoside 6 mg lectin ml gel
    https://www.bioz.com/result/agarose bound lectins/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    agarose bound lectins - by Bioz Stars, 2021-04
    93/100 stars

    Images

    1) Product Images from "Synovial fluid proteome in rheumatoid arthritis"

    Article Title: Synovial fluid proteome in rheumatoid arthritis

    Journal: Clinical Proteomics

    doi: 10.1186/s12014-016-9113-1

    Schematic of the work flow implemented in the study. Synovial fluid samples were collected from 20 RA patients. Equal amounts of proteins were taken from all samples and pooled together followed by two sets of protein enrichment: glycoprotein enrichment using multiple lectins and depletion of abundant proteins using MARS14. The enriched proteins were thereafter taken for fractionation and trypsin digestion. The fractionated tryptic peptides were then analyzed in a high resolution mass spectrometer. The data acquired were processed and subsequently analyzed using appropriate software
    Figure Legend Snippet: Schematic of the work flow implemented in the study. Synovial fluid samples were collected from 20 RA patients. Equal amounts of proteins were taken from all samples and pooled together followed by two sets of protein enrichment: glycoprotein enrichment using multiple lectins and depletion of abundant proteins using MARS14. The enriched proteins were thereafter taken for fractionation and trypsin digestion. The fractionated tryptic peptides were then analyzed in a high resolution mass spectrometer. The data acquired were processed and subsequently analyzed using appropriate software

    Techniques Used: Flow Cytometry, Protein Enrichment, Fractionation, Mass Spectrometry, Software

    2) Product Images from "Biochemical enrichment and biophysical characterization of a taste receptor for L-arginine from the catfish, Ictalurus puntatus"

    Article Title: Biochemical enrichment and biophysical characterization of a taste receptor for L-arginine from the catfish, Ictalurus puntatus

    Journal: BMC Neuroscience

    doi: 10.1186/1471-2202-5-25

    Lectin labelling of solubilized barbel epithelial proteins SDS-PAGE (4–20%) of 10 μg of solubilized barbel homogenate stained with silver ( Lane
    Figure Legend Snippet: Lectin labelling of solubilized barbel epithelial proteins SDS-PAGE (4–20%) of 10 μg of solubilized barbel homogenate stained with silver ( Lane "Sp" ) or probed with PHA-E lectin ( Lane "PHA" ) or RCA-I lectin ( Lane "RCA" ) using lectins at 10 μg/ml with ABC detection. Both lectins label a band at 82 – 84 kDa and lightly label at least two other bands, one near 88 kDa, the other near 120 kDa.

    Techniques Used: SDS Page, Staining

    3) Product Images from "N-glycosylation is essential for ileal ASBT function and protection against proteases"

    Article Title: N-glycosylation is essential for ileal ASBT function and protection against proteases

    Journal: American Journal of Physiology - Cell Physiology

    doi: 10.1152/ajpcell.00023.2015

    Lectin pull-down assays for wild-type ASBT and glycosylation deficient N10Q mutant ASBT protein samples. Equal amounts protein from total cellular lysate were incubated with agarose-bound lectins (4°C) overnight along with protease inhibitor cocktail. After washing with RIPA buffer, bound samples were eluted by boiling with 2X Laemmli buffer and used for Western blotting with anti-V5 antibody. Top panel shows the pull-down fractions and bottom panel shows unbound proteins in the supernatant.
    Figure Legend Snippet: Lectin pull-down assays for wild-type ASBT and glycosylation deficient N10Q mutant ASBT protein samples. Equal amounts protein from total cellular lysate were incubated with agarose-bound lectins (4°C) overnight along with protease inhibitor cocktail. After washing with RIPA buffer, bound samples were eluted by boiling with 2X Laemmli buffer and used for Western blotting with anti-V5 antibody. Top panel shows the pull-down fractions and bottom panel shows unbound proteins in the supernatant.

    Techniques Used: Mutagenesis, Incubation, Protease Inhibitor, Western Blot

    Related Articles

    Whole Genome Amplification:

    Article Title: Membrane Glycoproteins Associated with Breast Tumor Cell Progression Identified by a Lectin Affinity Approach
    Article Snippet: .. Agarose-bound wheat germ agglutinin (WGA) and agarose-bound Concanavalin A (ConA) were purchased from Vector Laboratories (Burlingame, CA). .. Agarose-bound WGA (1 mL) and 1 mL of agarose-bound ConA were packed into a disposable screw endcap spin column with filters at both ends.

    Affinity Chromatography:

    Article Title: Synovial fluid proteome in rheumatoid arthritis
    Article Snippet: .. Multiple lectin affinity chromatography Glycoprotein enrichment from 20 pooled synovial fluid samples containing 2.5 mg proteins was carried out by using a mixture of three agarose-bound lectins, Wheat Germ Agglutinin, Concanavalin A and Jacalin (Vector laboratories, USA), as described previously by our group [ , ]. .. Briefly, pooled lectin beads were incubated with protein samples in Tris-buffered saline (0.05 M Tris–HCl, pH 7.5, 0.15 M NaCl).

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 93
    Vector Laboratories jacalin
    a, Collapse assays showing depletion of collapse activity in rat forebrain extract (RFE) by use of immobilized <t>jacalin;</t> immobilized BSA was used as an additional control. b, Collapse assays showing quantification of PACMA31 dose/response relationship. c, Collapse assay and GSH titration. d, Collapse assays testing the NO scavenger myoglobin (20μM). e, Collapse assays testing the NO scavenger C-PTIO. f, Collapse assays using dialysed extracts from human 1718 astrocytic cells, testing activity before and after depletion by immobilized PNA and jacalin; immobilized BSA was used as an additional control. g, Western blot of rat cortical astrocyte cell surface preparation using anti-PDI antibody, showing one band at 57KDa in the centre of the blot. The doublet (right) is control purified bovine PDI (500ng), and the lower band indicates that this control sample was partially oxidised. Molecular weight markers (10μl; BLUeye Prestained Wide Range Protein ladder, Geneflow) are shown (left), transferred from the gel to the blot. h, Collapse assays testing reactivity of chick retinal axon growth cones to PDI+GSNO.
    Jacalin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/jacalin/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    jacalin - by Bioz Stars, 2021-04
    93/100 stars
      Buy from Supplier

    92
    Vector Laboratories jacalin agarose
    Binding of salivary components to rPAc. The binding to rPAc of high-molecular-mass glycoprotein and sIgA components separated from salivary agglutinin by electrophoretic fractionation, sIgA purified by using <t>jacalin-agarose,</t> and salivary lysozyme was determined by BIAcore assay. Values are given as the means ± standard deviations of RU in triplicate assays. Symbols: ○, salivary agglutinin; •, high-molecular-mass glycoprotein separated by electrophoretic fractionation; □, sIgA components separated by electrophoretic fractionation; ▪, sIgA purified by using jacalin-agarose; ▵, salivary lysozyme.
    Jacalin Agarose, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/jacalin agarose/product/Vector Laboratories
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    jacalin agarose - by Bioz Stars, 2021-04
    92/100 stars
      Buy from Supplier

    93
    Vector Laboratories agarose bound lectins
    Lectin pull-down assays for wild-type ASBT and glycosylation deficient N10Q mutant ASBT protein samples. Equal amounts protein from total cellular lysate were incubated with agarose-bound <t>lectins</t> (4°C) overnight along with protease inhibitor cocktail. After washing with RIPA buffer, bound samples were eluted by boiling with 2X Laemmli buffer and used for Western blotting with anti-V5 antibody. Top panel shows the pull-down fractions and bottom panel shows unbound proteins in the supernatant.
    Agarose Bound Lectins, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/agarose bound lectins/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    agarose bound lectins - by Bioz Stars, 2021-04
    93/100 stars
      Buy from Supplier

    Image Search Results


    a, Collapse assays showing depletion of collapse activity in rat forebrain extract (RFE) by use of immobilized jacalin; immobilized BSA was used as an additional control. b, Collapse assays showing quantification of PACMA31 dose/response relationship. c, Collapse assay and GSH titration. d, Collapse assays testing the NO scavenger myoglobin (20μM). e, Collapse assays testing the NO scavenger C-PTIO. f, Collapse assays using dialysed extracts from human 1718 astrocytic cells, testing activity before and after depletion by immobilized PNA and jacalin; immobilized BSA was used as an additional control. g, Western blot of rat cortical astrocyte cell surface preparation using anti-PDI antibody, showing one band at 57KDa in the centre of the blot. The doublet (right) is control purified bovine PDI (500ng), and the lower band indicates that this control sample was partially oxidised. Molecular weight markers (10μl; BLUeye Prestained Wide Range Protein ladder, Geneflow) are shown (left), transferred from the gel to the blot. h, Collapse assays testing reactivity of chick retinal axon growth cones to PDI+GSNO.

    Journal: bioRxiv

    Article Title: Regulation of nerve growth and patterning by cell surface protein disulphide isomerase

    doi: 10.1101/838771

    Figure Lengend Snippet: a, Collapse assays showing depletion of collapse activity in rat forebrain extract (RFE) by use of immobilized jacalin; immobilized BSA was used as an additional control. b, Collapse assays showing quantification of PACMA31 dose/response relationship. c, Collapse assay and GSH titration. d, Collapse assays testing the NO scavenger myoglobin (20μM). e, Collapse assays testing the NO scavenger C-PTIO. f, Collapse assays using dialysed extracts from human 1718 astrocytic cells, testing activity before and after depletion by immobilized PNA and jacalin; immobilized BSA was used as an additional control. g, Western blot of rat cortical astrocyte cell surface preparation using anti-PDI antibody, showing one band at 57KDa in the centre of the blot. The doublet (right) is control purified bovine PDI (500ng), and the lower band indicates that this control sample was partially oxidised. Molecular weight markers (10μl; BLUeye Prestained Wide Range Protein ladder, Geneflow) are shown (left), transferred from the gel to the blot. h, Collapse assays testing reactivity of chick retinal axon growth cones to PDI+GSNO.

    Article Snippet: Agarose bound Peanut Agglutinin (Lot#ZA0611; binding capacity > 4.5mg asialofetuin/ml of gel) and Agarose bound Jacalin (Lot#ZA1021) were from Vector Laboratories.

    Techniques: Activity Assay, Titration, Western Blot, Purification, Molecular Weight

    Binding of salivary components to rPAc. The binding to rPAc of high-molecular-mass glycoprotein and sIgA components separated from salivary agglutinin by electrophoretic fractionation, sIgA purified by using jacalin-agarose, and salivary lysozyme was determined by BIAcore assay. Values are given as the means ± standard deviations of RU in triplicate assays. Symbols: ○, salivary agglutinin; •, high-molecular-mass glycoprotein separated by electrophoretic fractionation; □, sIgA components separated by electrophoretic fractionation; ▪, sIgA purified by using jacalin-agarose; ▵, salivary lysozyme.

    Journal: Infection and Immunity

    Article Title: Binding of Salivary Glycoprotein-Secretory Immunoglobulin A Complex to the Surface Protein Antigen of Streptococcus mutans

    doi:

    Figure Lengend Snippet: Binding of salivary components to rPAc. The binding to rPAc of high-molecular-mass glycoprotein and sIgA components separated from salivary agglutinin by electrophoretic fractionation, sIgA purified by using jacalin-agarose, and salivary lysozyme was determined by BIAcore assay. Values are given as the means ± standard deviations of RU in triplicate assays. Symbols: ○, salivary agglutinin; •, high-molecular-mass glycoprotein separated by electrophoretic fractionation; □, sIgA components separated by electrophoretic fractionation; ▪, sIgA purified by using jacalin-agarose; ▵, salivary lysozyme.

    Article Snippet: High-molecular-mass glycoprotein and sIgA components separated by electrophoretic fractionation did not bind to rPAc, but native sIgA purified by using jacalin-agarose bound weakly to rPAc (Fig. ).

    Techniques: Binding Assay, Fractionation, Purification

    Lectin pull-down assays for wild-type ASBT and glycosylation deficient N10Q mutant ASBT protein samples. Equal amounts protein from total cellular lysate were incubated with agarose-bound lectins (4°C) overnight along with protease inhibitor cocktail. After washing with RIPA buffer, bound samples were eluted by boiling with 2X Laemmli buffer and used for Western blotting with anti-V5 antibody. Top panel shows the pull-down fractions and bottom panel shows unbound proteins in the supernatant.

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: N-glycosylation is essential for ileal ASBT function and protection against proteases

    doi: 10.1152/ajpcell.00023.2015

    Figure Lengend Snippet: Lectin pull-down assays for wild-type ASBT and glycosylation deficient N10Q mutant ASBT protein samples. Equal amounts protein from total cellular lysate were incubated with agarose-bound lectins (4°C) overnight along with protease inhibitor cocktail. After washing with RIPA buffer, bound samples were eluted by boiling with 2X Laemmli buffer and used for Western blotting with anti-V5 antibody. Top panel shows the pull-down fractions and bottom panel shows unbound proteins in the supernatant.

    Article Snippet: Agarose-bound lectins were purchased from Vector Laboratories (Burlingame, CA).

    Techniques: Mutagenesis, Incubation, Protease Inhibitor, Western Blot