Peptides
Peptides
Novus Biologicals™ Asparagine synthetase Recombinant Protein Antigen
Highly purified. Generating reliable and reproducible results. Applications: Antibody Competition
Novus Biologicals™ Asparagine synthetase Recombinant Protein Antigen
Highly purified. Generating reliable and reproducible results. Applications: Antibody Competition
Novus Biologicals™ ASRGL1 Recombinant Protein Antigen
Highly purified. Generating reliable and reproducible results. Applications: Antibody Competition
Lkt Laboratories CAS 9015-68-3, ≥98%, Catalyzes hydrolysis of asparagine to aspartate and ammonia. It treats leukemias by depleting asparagine levels and inhibiting cell growth.
Asparaginase is an enzyme that catalyzes the hydrolysis of asparagine to aspartate and ammonia, depleting asparagine levels and inhibiting cell growth; it is commonly used as an anticancer chemotherapeutic and anti-angiogenic compound in the treatment of leukemia. Asparaginase inhibits proliferation of acute myelogenous leukemia (AML) cells, inducing apoptosis mediated by apoptosis-inducing factor (AIF). Asparaginase decreases β1 integrin binding and phosphorylation of FAK, inducing autophagy; this decreases microvascular endothelial cell tube formation and inhibits invasion of ovarian cancer cells. In clinical settings, asparaginase may induce thrombotic effect, as administration often results in depletion of anti-thrombin, and it may also increase serum triglycerides.
Medchemexpress LLC HY-P1923 1mg Medchemexpress, L-Asparaginase CAS:9015-68-3 Purity:>98%
Medchemexpress, HY-P1923 1mg L-Asparaginase CAS:9015-68-3 L-Asparaginase (L-ASNase), a hydrolase that catalyzes the conversion of L-asparagine, used in acute lymphoblastic leukemia treatment. L-Asparaginase depletes L-asparagine from plasma resulting in inhibition of RNA and DNA synthesis with the subsequent blastic cell apoptosis [1] . Purity:>98% Medchemexpress has over 10000 novel life-science reagents, reference compounds, APIs and natural compounds for laboratory and scientific use. Other quantity can also be offered.
Bachem Fmoc-Asn(GlcNAc(Ac)3-b-D)-OH
Fmoc-Asn(GlcNAc(Ac)3-b-D)-OH, 131287-39-3, C33H37N3O13, Mr 683.67, 100mg. N-a-Fmoc-N-g-(2-acetamido-2-deoxy-3,4,6-tri-O-acetyl-b-D-glucopyranosyl)-L-asparagine.
New England Biolabs, Inc. PNGase F (Glycerol-free), Recombinant – 75000 units
PNGase F is the most effective enzymatic method for removing almost all N-linked oligosaccharides from glycoproteins. PNGase F (Glycerol-free), Recombinant is a recombinant amidase, which cleaves between the innermost GlcNAc and asparagine residues of high mannose, hybrid, and complex oligosaccharides.
Carbosynth LLC. Fmoc-Asn[per-O-Boc-(Fucα1-6GlcNAcß)], 10mg, MF= C58H81N3O24
Nα-9-Fluorenylmethoxycarbonyl-Nomega-[2,3,4-tri-O-t-Butyloxycarbonyl-α-L-Fucopyranosyl-(1→6)-3,4-di-O-t-Butyloxycarbonyl-2-Acetamido-2-Deoxy-β-D-Glucopyranosyl]-L-Asparagine, Application: Boc-Protected Disaccharide Derivative for N-Linked Glycopeptide Synthesis;Fmoc-Amino Acid for the Synthesis of Fucα(1-6)GlcNAc-β-Asn-Containing Peptide, Notes: For the chemical synthesis of glycopeptides, acetyl group has been widely used for the protection of hydroxy groups in sugar moieties. Scientists at The Noguchi Institute recently developed Boc-protected disaccharide building block which does not require troublesome acetyl deprotection in basic condition. Using this derivative, N-linked glycopeptide synthesis can be achieved moreconveniently and efficiently by standard Fmoc-SPPS., MW: 1204.3
Carbosynth LLC. Z-Ala-Ala-Asn-MCA (5 mg vial), 1ea, MW: 565.57, Molecular formula: C28H31N5O8, CAS# 149697-16-5
This item has a minimum order quantity of 2 per supplier requirements
Synonyms: Benzyloxycarbonyl-L-Alanyl-L-Alanyl-L-Asparagine-4-Methyl-Coumaryl-7-Amide, Z-Ala-Ala-Asn-AMC, Z-AAN-AMC, ZAAN-MCA, Application: Substrate for Legumain, Storage Temperature: -20C, References: A.A. Kembhavi, D.J. Buttle, C.G. Knight, and A.J. Barret, Arch. Biochem. Biophys., 303, 208 (1993)., J.-M. Chen, P.M. Dando, N.D. Rawlings, M.A. Brown, N.E. Young, R.A. Stevens, E. Hewitt, C. Watts, and A.J. Barret, J. Biol. Chem., 272, 8090 (1997)., B. Manoury, E.W. Hewitt, N. Morrice, P.M. Dando, A.J. Barret, and C. Watts, Nature, 396, 695 (1998).