Lectins
Cayman Chemical Cholesteryl Stearate 500mg
A modulator of IRE1a function binds to the ATP-binding site on IRE1a where it inhibits autophosphorylation (IC50 280 nM) and enhances its RNase function (EC50 460 nM) restores the ability of dephosphoylated IRE1a to cleave XBP1 mRNA in a dose-dependent manner enhances IRE1a oligomerization in a crosslinking assay
Cayman Chemical Cholesteryl Stearate 250mg
A modulator of IRE1a function binds to the ATP-binding site on IRE1a where it inhibits autophosphorylation (IC50 280 nM) and enhances its RNase function (EC50 460 nM) restores the ability of dephosphoylated IRE1a to cleave XBP1 mRNA in a dose-dependent manner enhances IRE1a oligomerization in a crosslinking assay
Sigma Aldrich Fine Chemicals Biosciences Lectin from Phytolacca ame5MG
Lectins are proteins of plant origin which have the ability to bind to certain neuronal surface glycoproteins and glycolipids. This ability of theirs helps them to be used as neuroanatomical tracers as they are taken and transported in a retrograde or anterograde fashion.
Sigma Aldrich Fine Chemicals Biosciences Lectin from Arachis hypoga
LECTIN Lectin from Arachis hypoga
Sigma Aldrich Fine Chemicals Biosciences Lectin from Phytolacca ame5MG
Lectins are carbohydrate-binding proteins omnipresent found in fungi plants and animals. The structure of lectin is diversely studied in plants and animals. The secondary structure of this protein is rich in -strands and possesses a carbohydrate binding sites on the surface.
Sigma Aldrich Fine Chemicals Biosciences Lectin from Phytolacca ame10MG
Lectins are proteins of plant origin which have the ability to bind to certain neuronal surface glycoproteins and glycolipids. This ability of theirs helps them to be used as neuroanatomical tracers as they are taken and transported in a retrograde or anterograde fashion.
Sigma Aldrich Fine Chemicals Biosciences Lectin from Bandeiraea sim1MG
Lectin from Bandeiraea simplicifolia (Griffonia simplicifolia) has A and B subunits which recognizesGalNAc andGal-end groups respectively. Lectins are extracted from the seeds of the legume shrub Griffonia simplicifolia which are carbohydrate binding proteins.
Sigma Aldrich Fine Chemicals Biosciences Lectin from Arachis hypoga25MG
Lectin from Arachis hypogaea (peanut) is a homotetrameric protein of 110 kDa.
Sigma Aldrich Fine Chemicals Biosciences Lectin from Phytolacca ame10MG
Lectins are carbohydrate-binding proteins omnipresent found in fungi plants and animals. The structure of lectin is diversely studied in plants and animals. The secondary structure of this protein is rich in -strands and possesses a carbohydrate binding sites on the surface.
Cayman Chemical Cholesteryl-d7 PalmItate 5mg
An analytical reference standard categorized as a phytocannabinoid metabolite a metabolite of cannabichromene intended for research and forensic applications
Cayman Chemical Cholesteryl-d7 PalmItate 10mg
An inhibitor of the protein-microRNA precursor interaction between Lin28 and let-7 binds to the cold-shock domain of Lin28 to inhibit let-7 binding inhibits Lin28-mediated let-7 oligouridylation (IC50 ~27 UM) increases the levels of mature let-7b -7c -7f -7g and -7i as well as the levels of miR-16 which is not regulated by Lin28 at 100 UM in K562 leukemia cells but also increases the levels of miR-16 which is not regulated by Lin28 increases the levels of mature let-7a-i without increasing miR-16 levels in Lin28a/Lin28b double-knockout mESCs expressing exogenous wild-type Lin28a inhibits the protein-protein interaction between PfCoSP and PfDNA or Pfa/B-tubulin is active against P. falciparum strain 3D7 and the chloroquine-resistant strain RKL-9 (IC50s 1.35 and 6.3 nM respectively)
Sigma Aldrich Fine Chemicals Biosciences Lectin from Phaseolus vulg5MG
Phytohemagglutinin (PHA) derived from Phaseolus vulgaris is a tetrameric glycoprotein. It consists of two different subunits that weighs 120 kDa.
Sigma Aldrich Fine Chemicals Biosciences Lectin from Triticum vulga10MG
Lectins are carbohydrate-binding proteins. They are omnipresent and usually found in fungi plants and animals. The secondary structure of this protein is rich in -strands and possesses carbohydrate binding sites on the surface.
