You Searched For: (S)-beta-(Carbobenzoxyamino)-gamma-butyrolactone


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Catalog Number: (10162-870)
Supplier: Genetex
Description: Rabbit Polyclonal antibody to CaMK2 beta/ gamma/ delta (phospho Thr287)


Catalog Number: (10406-398)
Supplier: Bioss
Description: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. Polymer of 16 chains, four each of alpha, beta, gamma, and delta. Alpha and beta are regulatory chains, gamma is the catalytic chain, and delta is calmodulin. The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.


Catalog Number: (10406-848)
Supplier: Bioss
Description: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. Polymer of 16 chains, four each of alpha, beta, gamma, and delta. Alpha and beta are regulatory chains, gamma is the catalytic chain, and delta is calmodulin. The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.


Catalog Number: (76085-736)
Supplier: Bioss
Description: S adenosylmethionine synthetase catalyzes the formation of S adenosylmethionine from methionine and ATP. In mammalian tissues, there are three distinct forms of AdoMet synthases designated as alpha, beta, and gamma. Alpha and beta are expressed only in adult liver, while gamma is widely distributed in extrahepatic tissues.


Catalog Number: (10097-826)
Supplier: Prosci
Description: IFN gamma receptor beta is part of the receptor for interferon gamma. This class II cytokine receptor pairs with CDw119 to form the IFN gamma receptor and is an integral part of the IFN gamma signal transduction pathway. CDw119 serves as the IFN gamma binding chain and associates with the IFN gamma beta chain which is required for receptor signaling. The extracellular portion of both the IFN gamma receptor alpha and beta chains must be species matched. The IFN gamma receptor beta chain is expressed on T and B cells, NK cells, monocytes/ macrophages, and fibroblasts. Binding of IFN gamma induces receptor dimerization, internalization, Jak1 and Jak2 protein kinase activation and, ultimately, STAT1 activation. It is also likely to interact with GAF. IFN gamma initiates and regulates a variety of immune responses and is required for signal transduction. Contains 2 fibronectin type III domains. Defects in IFN gamma Receptor beta are a cause of mendelian susceptibility to mycobacterial disease (MSMD), a rare condition that confers predisposition to illness caused by several mycobacteria strains


Catalog Number: (10097-836)
Supplier: Prosci
Description: IFN gamma receptor beta is part of the receptor for interferon gamma. This class II cytokine receptor pairs with CDw119 to form the IFN gamma receptor and is an integral part of the IFN gamma signal transduction pathway. CDw119 serves as the IFN gamma binding chain and associates with the IFN gamma beta chain which is required for receptor signaling. The extracellular portion of both the IFN gamma receptor alpha and beta chains must be species matched. The IFN gamma receptor beta chain is expressed on T and B cells, NK cells, monocytes/ macrophages, and fibroblasts. Binding of IFN gamma induces receptor dimerization, internalization, Jak1 and Jak2 protein kinase activation and, ultimately, STAT1 activation. It is also likely to interact with GAF. IFN gamma initiates and regulates a variety of immune responses and is required for signal transduction. Contains 2 fibronectin type III domains. Defects in IFN gamma Receptor beta are a cause of mendelian susceptibility to mycobacterial disease (MSMD), a rare condition that confers predisposition to illness caused by several mycobacteria strains


Catalog Number: (76079-498)
Supplier: Bioss
Description: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. Polymer of 16 chains, four each of alpha, beta, gamma, and delta. Alpha and beta are regulatory chains, gamma is the catalytic chain, and delta is calmodulin. The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.


Catalog Number: (10396-858)
Supplier: Bioss
Description: Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.


Catalog Number: (10782-924)
Supplier: Biosensis
Description: Enolase is a metalloenzyme that catayzes the reaction between 2-phospho-D-glycerate and phosphoenolpyruvate during glycolysis. Mammalian enolase is composed of 3 subunits; alpha, beta and gamma (Neuron-specific enolase). These subunits can form homodimers or heterodimers. The alpha/gamma heterodimer and the gamma/gamma homodimer are found primarily in neurons.


Catalog Number: (10096-496)
Supplier: Proteintech
Description: There are five tubulins in human cells: alpha, beta, gamma, delta, and epsilon. Tubulins are conserved across species. They form heterodimers, which multimerize to form a microtubule filament. An alpha and beta tubulin heterodimer is the basic structural unit of microtubules. The heterodimer does not come apart, once formed. The alpha and beta tubulins, which are each about 55 kDa MW, are homologous but not identical. Alpha, beta, and gamma tubulins have all been used as loading controls. Tubulin expression may vary according to resistance to antimicrobial and antimitotic drugs.


Catalog Number: (10396-862)
Supplier: Bioss
Description: Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.


Catalog Number: (76078-234)
Supplier: Bioss
Description: Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.


Catalog Number: (76078-236)
Supplier: Bioss
Description: Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.


Catalog Number: (10749-370)
Supplier: Prosci
Description: BACE Antibody: Accumulation of the amyloid-beta (Abeta) plaque in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. Abeta peptide is generated by proteolytic cleavage of the beta-amyloid protein precursor (APP) at beta- and gamma-sites by two proteases. APP is first cleaved by beta-secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide, which is deposited in the brains of all suffers of Alzheimer's disease. The long-sought beta-secretase was recently identified by several groups independently and designated beta-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2). BACE/Asp2 is a novel transmembrane aspartic protease and colocalizes with APP.


Catalog Number: (10395-642)
Supplier: Bioss
Description: S adenosylmethionine synthetase catalyzes the formation of S adenosylmethionine from methionine and ATP. In mammalian tissues, there are three distinct forms of AdoMet synthases designated as alpha, beta, and gamma. Alpha and beta are expressed only in adult liver, while gamma is widely distributed in extrahepatic tissues.


Catalog Number: (10491-892)
Supplier: Bioss
Description: Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated α, β and γ. Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. γS-crystallin (Gamma-crystallin S), also known as Beta-crystallin S, is a 178 amino acid protein that exists as a monomer which does not aggregate. γS-crystallin contains a two-domain beta structure and belongs to the beta/gamma-crystallin gene family mapping to human chromosome 3. γS-crystallin has been linked to congenital cataract development, a disorder signified by increasing levels of lens opacity.


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