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카탈로그 번호 | CAS 번호 | 설명 | 상태 | 단위 | 판매가 | 할인가 | 가격(VAT포함) | 수량 / 장바구니 / 찜 |
4400 | - | Takara 4400 Sialic Acid Fluorescence Labeling Kit, 100 Rxns pk | 재고문의 | pk | 1,111,000원 | - | 1,222,100원 | |
4456 | - | Takara 4456 Lacto-N-biosidase, 100 uU pk | 재고문의 | pk | 679,000원 | - | 746,900원 | |
635647 | - | Takara 635647 Glycoprotein Enrichment Resin, 10 mL pk | 재고문의 | pk | 546,000원 | - | 600,600원 | |
4462 | - | Takara 4462 SCDase (Sphingolipid ceramide N-deacylase), 250 mU pk | 재고문의 | pk | 529,000원 | - | 581,900원 | |
4455 | - | Takara 4455 Cloned alpha 2,3-Sialidase, 5 Units pk | 재고문의 | pk | 502,000원 | - | 552,200원 | |
4453 | - | Takara 4453 Alpha 1, 3/4-L-Fucosidase, 100 uU pk | 재고문의 | pk | 473,000원 | - | 520,300원 | |
4460 | - | Takara 4460 rEGCase II, 100 mU pk | 재고문의 | pk | 440,000원 | - | 484,000원 | |
635648 | - | Takara 635648 Glycoprotein Western Detection Kit, 20 Rxns pk | 재고문의 | pk | 422,000원 | - | 464,200원 | |
4450 | - | Takara 4450 Glycopeptidase F (Peptide: N-glycosidase F), 25 mU pk | 재고문의 | pk | 339,000원 | - | 372,900원 |
Glycan analysis often involves structural determination of oligosaccharide components of glycoproteins, glycolipids, glycosphingolipids, and other glycan-containing biological molecules.
Sensitive carbohydrate chemistry techniques require specific enzymes such as fucosidase, sialidase, biosidase, and other hydrolytic enzymes with activities specific for certain linkages. Sequential treatment of glycan-containing samples can allow structural determination of the original moiety, a fundamental technique of glycan analysis.
Precise, pure enzymes from Takara Bio for carbohydrate chemistry analyses include alpha-1,2 fucosidase, alpha-1,3/1,4 fucosidase, alpha 2,3-sialidase, Lacto-N-biosidase, and glycan hydrolases useful for sphingolipid analysis such as recombinant endoglycoceramidase II.
In some situations such as proteomic analysis, it may be desirable to remove oligosaccharide structures prior to analysis of protein fractions by MALDI-TOF mass spectrometry. PNGase (also known as glycopeptidase F) is widely used for this purpose to deglycosylate protein samples.
Additional products for glycoprotein research include the Sialic Acid Florescence Labeling Kit for efficient modification of sialic acid-containing moieties with DMB prior to detection by HPLC, and kits for purification of glycan samples (including hydrazine-treated samples) prior to fluorescent labeling with 2-aminopyridine (pyridylamination reaction).
Cat. # | Product | Size | License | Quantity | Details | |
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4453 | Alpha 1, 3/4-L-Fucosidase | 100 uU | * | |||
This enzyme catalyses the hydrolytic cleavage of α-fucoside bonds and releases L-fucose. This enzyme specifically cleaves α1, 3- and α1, 4-fucoside bonds. It also releases L-fucose from α1-acid glycoprotein. ##### Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back Substrate specificity for alpha 1,3/1,4 fucosidase (Cat.# 4453) --------------------------------------------------------------- Substrate specificity for alpha 1,3/1,4 fucosidase (Cat.# 4453). Back 4453: Alpha-1,3/4-L-Fucosidase ------------------------------ |
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4455 | Cloned alpha 2,3-Sialidase | 5 Units | * | |||
This sialidase has a 260-fold kinetic preference for the α2,3 sialyl linkage. The enzyme efficiently cleaves sialyl groups from glycoproteins and glycolipids. It may not release sialic acid from O-linked oligosaccharides on glycoproteins. ##### Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back 4455: Alpha-2,3-Sialidase ------------------------- |
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4450 | Glycopeptidase F (Peptide: N-glycosidase F) | 25 mU | * | |||
PNGase F (Glycopeptidase F) removes N-glycans from glycoproteins and enables proteomic analysis, including MALDI-TOF mass spectrometry. ##### Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back 4450: Glycopeptidase F (Peptide:N-glycosidase F) ------------------------------------------------ |
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635647 | Glycoprotein Enrichment Resin | 10 mL | * | |||
Glycoprotein Enrichment Resin is an agarose-based phenylboronic acid resin that provides quick, easy, and specific enrichment of glycosylated proteins from complex samples such as human serum. The resin may be used with either simple gravity flow columns or medium pressure methods such as FPLC to remove nonglycosylated proteins and enrich glycosylated proteins. ##### Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back Molecular mechanism of saccharide binding to Glycoprotein Enrichment Resin -------------------------------------------------------------------------- Molecular mechanism of saccharide binding to Glycoprotein Enrichment Resin. Back SDS-PAGE and Western blot analysis of Clontech’s Glycoprotein Enrichment Resin column fractions demonstrate more effective glycoprotein enrichment than a competitor’s resin ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SDS-PAGE and Western blot analysis of Clontech’s Glycoprotein Enrichment Resin column fractions demonstrate more effective glycoprotein enrichment than a competitor’s resin. Left panel. Fractions from gravity flow enrichment procedures were analyzed by SDS-PAGE. As seen in the Coomassie-stained gel, the Competitor S Resin showed binding of HSA (human serum albumin) to the column (Lane 6) and leakage of IgG in the flowthrough fraction (Lane 5). Right panel. Fractions from the column were also analyzed by Western blotting with an antibody to human IgG. The Clontech resin retained glycosylated IgG (Lane 3), with no visible loss of IgG in the flowthrough fraction (Lane 2). In contrast, the Competitor S Resin exhibited a loss of IgG in the flowthrough fraction (Lane 5). Lane M: molecular weight marker. Lanes 1, 4: human serum. Lanes 2, 5: flowthrough. Lanes 3, 6: eluate (glycoproteins). Back Western blot analysis of column fractions obtained using Clontech’s Glycoprotein Enrichment Resin demonstrates the specific enrichment of high-abundance and low-abundance serum glycoproteins ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Western blot analysis of column fractions obtained using Clontech’s Glycoprotein Enrichment Resin demonstrates the specific enrichment of high-abundance and low-abundance serum glycoproteins. Panel A. Specific enrichment of high-abundance serum glycoprotein IgG, detected with an antibody against IgG. Lane 1: human serum, Lane 2: flowthrough, Lane 3: eluate (glycoprotein). Panels B and C: Enriched fractions from the column containing Clontech’s Glycoprotein Enrichment Resin were analyzed by Western blotting with antibodies for two specific low-abundance serum glycoproteins, alpha-1 acid glycoprotein (Panel B) and alpha-1 antitrypsin (Panel C).Lane 1: human serum. Lane 2: eluted fraction. Lane 3: eluted fraction. Back 635647: Glycoprotein Enrichment Resin ------------------------------------- |
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635648 | Glycoprotein Western Detection Kit | 20 Rxns | * | |||
The Glycoprotein Western Detection Kit is an accessory product to our Glycoprotein Enrichment Resin (Cat. No. 635647). It is designed for the selective staining of glycoproteins on Western membranes using a modification of the periodic acid-Schiff method. ##### Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back Highly sensitive and selective detection of purified glycoproteins with Clontech’s Glycoprotein Western Detection Kit --------------------------------------------------------------------------------------------------------------------- Highly sensitive and selective detection of purified glycoproteins with Clontech’s Glycoprotein Western Detection Kit. Panel A. Varying amounts of purified horseradish peroxidase (HRP), a known glycoprotein (Lanes 1–4), and soybean trypsin inhibitor (SBTI), a nonglycosylated protein (Lanes 5–8), were electrophoresed on a 4–15% SDS-PAGE gel and transferred to a nitrocellulose membrane. Glycoprotein bands were specifically detected in Lanes 1–4, but not Lanes 5–8, using the Glycoprotein Western Detection Kit. Lane M: molecular weight marker. Lane 1: 700 ng HRP. Lane 2: 350 ng HRP. Lane 3: 140 ng HRP. Lane 4: 70 ng HRP. Lane 5: 700 ng SBTI. Lane 6: 350 ng SBTI. Lane 7: 140 ng SBTI. Lane 4: 70 ng SBTI. Panel B. Varying amounts of three different purified glycoproteins [fetuin (Lanes 1–5), alpha-1 acid glycoprotein (AGP; Lanes 6–10), and horseradish peroxidase (HRP; Lanes 11 & 12)] were electrophoresed on a 4–15% SDS-PAGE gel, transferred to a nitrocellulose membrane, and detected using the Glycoprotein Western Detection Kit, according to the user manual. Lane M: molecular weight marker. Lane 1: 1 μg fetuin. Lane 2: 500 ng fetuin. Lane 3: 200 ng fetuin. Lane 4: 100 ng fetuin. Lane 5: 50 ng fetuin. Lane 6: 1 μg AGP. Lane 7: 500 ng AGP. Lane 8: 200 ng AGP. Lane 9: 100 ng AGP. Lane 10: 50 ng AGP. Lane 11: 350 ng HRP. Lane 12: 140 ng HRP. Back 635648: Glycoprotein Western Detection Kit ------------------------------------------ |
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4456 | Lacto-N-biosidase | 100 uU | * | |||
This enzyme specifically hydrolyzes oligosaccharides with type I chains and produces lacto-N-biose (Galb-3GlcNAc). It does not hydrolyze oligosaccharides with type II chain. The structure of the substrate essential for the enzyme activity is the terminal lacto-N-biosyl residue (Galb1-3GlcNAc). The enzyme does not hydrolyze a 2,3-sialyllacto-N-tetraose, lacto-N-fucopentaose I and II. One vial of this product (100 μl) allows 50–100 reactions of enzyme digestion of sugar chain up to 10 pmol. ##### Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back 4456: Lacto-N-biosidase ----------------------- |
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4460 | rEGCase II | 100 mU | * | |||
Endoglycoceramidase II (EGCase II) cleaves the linkage between the oligosaccharide and ceramide of various acidic and neutral glycosphingolipids, producing intact oligosaccharides and ceramides. This enzyme does not act on galactosyl- and glucosyl-ceramides, glycoglycerolipids, or glycoproteins. Note: This product contains detergents and is not active without them. Do not use on living cells. ##### Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back 4460: rEGCase II ---------------- |
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4462 | SCDase (Sphingolipid ceramide N-deacylase) | 250 mU | * | |||
SCDase (Sphingolipid ceramide N-deacylase) from Pseudomonas species hydrolyzes the N-acyl linkage between fatty acids and sphingosine bases in ceramides of various sphingolipids. The enzyme also catalyzes the reverse reaction and possesses transacylation activity. The enzyme acts on various acidic and neutral glycosphingolipids and sphingomyelin; however, it exhibits low activity on ceramide. ##### Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components You May Also Like Image Data Back 4462: SCDase (Sphingolipid ceramide N-deacylase) ------------------------------------------------ |
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4400 | Sialic Acid Fluorescence Labeling Kit | 100 Rxns | * | |||
The fluorescence labeling of sialic acid with 1, 2-diamino-4, 5-methyleneoxybenzene (DMB) is a simple and very sensitive analytical method in which free sialic acids are analyzed by reverse-phase HPLC after labeling with DMB. The sialic acids which are bound to the sugar chains in glycoproteins or glycolipids can also be measured after pre-treatment with sialidases or acid hydrolysis. The detection limit of DMB-sialic acid is 57 fmol. TaKaRa`s Sialic Acid Fluorescence Labeling Kit is designed to simplify the DMB-derivatization procedure. The reagents are provided in aqueous solutions and the protocol only involves mixing of reagents and incubation. By combination of this DMB method with Pyridylamino (PA) derivatization, sialoglycoconjugates can be analyzed with extremely high sensitivity. ##### Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back 4400: Sialic Acid Fluorescence Labeling Kit ------------------------------------------- |
Fast, simple, and efficient protein digestion with Capturem Trypsin
Capturem Trypsin digests proteins more rapidly and completely than trypsin in solution, as demonstrated using apomyoglobin, a common protein mapping standard, and myoglobin, a tightly folded protein. This makes it a powerful tool for proteomic analysis. Apomyoglobin peptides generated by Capturem Trypsin digestion were shown to provide good sequence coverage using mass spectrometry, while digestion of a whole-cell lysate enabled the identification of 2,320 unique proteins via LC/MS-MS analysis.
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