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Descripción: Ácido L-α-Aminoadípico
Numero del catalogo: APOSBIA4025-1G
UOM: 1 * 1 g
Proveedor: Apollo Scientific


Descripción: L(+)-Arginina Ph. Eur., USP, puro
Numero del catalogo: A1345.0500
UOM: 1 * 500 g
Proveedor: PanReac AppliChem

Certificados


Descripción: L(+)-Arginina ≥98%
Numero del catalogo: A15738.36
UOM: 1 * 500 g
Proveedor: Thermo Fisher Scientific

FDS Certificados


Descripción: Ácido D-α-Aminoadípico 98%
Numero del catalogo: ACRO441960050
UOM: 1 * 5 g
Proveedor: Thermo Fisher Scientific

FDS


Descripción: DL-α-Fenilalanina ≥98.0% (by HPLC, titration analysis)
Numero del catalogo: TCIAP0136-25G
UOM: 1 * 25 g
Proveedor: TCI


Descripción: Ácido 1-naftilacético 95%
Numero del catalogo: ACRO349640250
UOM: 1 * 25 g
Proveedor: Thermo Fisher Scientific

FDS


Descripción: Eflornithine hydrochloride monohydrate
Numero del catalogo: ACRO462700010
UOM: 1 * 1 g
Proveedor: Thermo Fisher Scientific


Descripción: Activates PPAR alpha and the phospholipase C (PLC) signalling pathway. Stimulates peroxisomal fatty acyl-CoA oxidase activity. These effects can be blocked by staurosporine (Prod. No. ALX-380-014). Exhibits significant cytotoxic activities against numerous tumor cell lines. Binds tubulin. Inhibits angiogenesis. Reduces HIF-1alpha protein levels. Induces apoptosis. Antifungal.
Numero del catalogo: ENZOALX350108M001
UOM: 1 * 1 mg
Proveedor: ENZO LIFE SCIENCES


Descripción: Ácido D-α-Aminoadípico 97%
Numero del catalogo: APOSOR471645-25G
UOM: 1 * 25 g
Proveedor: Apollo Scientific


Descripción: Animal-free amino acid. Polar. Amide.
Numero del catalogo: 94341-100G
UOM: 1 * 100 g
Proveedor: VWR Chemicals

FDS Certificados


Descripción: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Zince lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30 to 40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.
Numero del catalogo: BOSSBS-15969R-CY7
UOM: 1 * 100 µl
Proveedor: Bioss


Descripción: Ácido 2-piridincarboxílico ≥99%
Numero del catalogo: A14749.14
UOM: 1 * 25 g
Proveedor: Thermo Fisher Scientific

FDS Certificados


Descripción: (R)-(-)-N-(3,5-Dinitrobenzoyl)-α-phenylglycine ≥98.0% (by HPLC, titration analysis)
Numero del catalogo: TCIAD1853-5G
UOM: 1 * 5 g
Proveedor: TCI


Descripción: Neotame ≥98.0% (by HPLC, titration analysis)
Numero del catalogo: TCIAN1112-5G
UOM: 1 * 5 g
Proveedor: TCI


Descripción: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.
Numero del catalogo: BOSSBS-12463R-A680
UOM: 1 * 100 µl
Proveedor: Bioss


Descripción: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Zince lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30 to 40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.
Numero del catalogo: BOSSBS-15969R-A555
UOM: 1 * 100 µl
Proveedor: Bioss


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