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Wyszukano: alpha-Chloralose


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Producent: Abcam
Opis: Rabbit monoclonal [EP933Y] to GSK3 (alpha + beta).

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Numer katalogowy: (ABCAAB106009-100)
Producent: Abcam
Opis: Rabbit polyclonal to Macrophage Inflammatory Protein 3 alpha.
j.m.: 1 * 100 µG


Numer katalogowy: (BOSSBS-15969R)
Producent: Bioss
Opis: 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. [provided by RefSeq, Jul 2008].
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-6871R)
Producent: Bioss
Opis: Produced by macrophages, IFN alpha have mainly antiviral activities.
j.m.: 1 * 100 µl


Producent: Apollo Scientific
Opis: 4-Nitro-α,α,α-trifluorotoluene 98%

Numer katalogowy: (BOSSBS-12970R-A680)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-12963R-A680)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-15969R-A350)
Producent: Bioss
Opis: 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.
j.m.: 1 * 100 µl


Producent: Abcam
Opis: Rabbit monoclonal [Y62] to 14-3-3 alpha + beta.

Producent: Thermo Fisher Scientific
Opis: α,α,α',α'-Tetrabromo-o-ksylen 97%
Numer katalogowy: (USBIM4692-25E)
Producent: US Biological
Opis: Anti-MSH alpha Guinea pig Polyclonal Antibody
j.m.: 1 * 50 µl


Numer katalogowy: (BSENS-075-50)
Producent: Biosensis
Opis: Alpha synuclein is an abundant 140 amino acid neuronal protein, expressed primarily at presynaptic terminals in the central nervous system. Alpha synuclein has been associated with several neurodegenerative diseases. A point mutation in the gene coding for the alpha-synuclein protein was the first discovery linking this protein to a rare familial form of Parkinson's disease (PD). Subsequently, other mutations in the alpha-synuclein gene have been identified in familial PD. The aggregated proteinaceous inclusions called Lewy bodies found in PD and cortical Lewy body dementia (LBD) were discovered to be predominantly alpha-synuclein. Aberrant aggregation of alpha-synuclein has been detected in an increasing number of neurodegenerative diseases, collectively known as synucleopathies. Alpha-synuclein exists physiologically in both soluble and membrane-bound states, in unstructured and alpha-helical conformations, respectively. The physiological function of alpha-synuclein appears to require its translocation between these subcellular compartments and interconversion between the 2 conformations. Abnormal processing of alpha-synuclein is predicted to lead to pathological changes in its binding properties and function.
j.m.: 1 * 50 µG


Producent: Abcam
Opis: Rabbit monoclonal [EP2527Y] to alpha Actinin/ACTN1.

Numer katalogowy: (ABCAAB19079-50)
Producent: Abcam
Opis: Mouse monoclonal [UC45] to Fibrinogen alpha chain.
j.m.: 1 * 50 µG


Numer katalogowy: (ABCAAB220-100)
Producent: Abcam
Opis: Mouse monoclonal [44H6] to Integrin alpha 4/CD49D.
j.m.: 1 * 100 µG


Numer katalogowy: (ABCAAB3980-100)
Producent: Abcam
Opis: Mouse monoclonal [AFP-01] to alpha 1 Fetoprotein.
j.m.: 1 * 100 µG


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Zapasy tego artykułu są ograniczone, ale możliwe, że jest on dostępny w pobliskim magazynie. Upewnij się, że jesteś zalogowany na stronie, aby móc sprawdzić dostępność zapasów. Jeśli call ciągle się wyświetla i potrzebujesz pomocy, zadzwoń na 58 323 82 00.
Ten produkt jest ograniczony w dostępie i można go zamówić tylko przy użyciu zaaprobowanego konta. Jeśli potrzebujesz pomocy, napisz do Działu Prawnego VWR na tomasz.chrobak@pl.vwr.com
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Ten produkt jest zablokowany na stronie internetowej. W celu zamówienia, skontaktuj się z Działem Obsługi Klienta.
Produkt oryginalny został wycofany. Dostępny jest wskazny zamiennik .
Wybrany produkt został wycofany - sprzedaż do wyczerpania zapasów. Dostępne zamienniki można znaleźć poprzez wpisanie powyższego numeru katalogowego VWR w okno wyszukiwarki. Jeśli potrzebujesz dalszej pomocy, prosimy o kontakt z Działem Doradztwa Produktowego pod numerem telefonu 58 3238 220.
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