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G1044

Sigma-Aldrich

Monoclonal Anti-Granzyme B antibody produced in mouse

clone GrB7, tissue culture supernatant

Sinônimo(s):

Anti-C11, Anti-CCPI, Anti-CGL-1, Anti-CGL1, Anti-CSP-B, Anti-CSPB, Anti-CTLA1, Anti-CTSGL1, Anti-HLP

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

mouse

Nível de qualidade

conjugado

unconjugated

forma do anticorpo

tissue culture supernatant

tipo de produto de anticorpo

primary antibodies

clone

GrB7, monoclonal

descrição

not suitable for immunocytochemistry (frozen sections)

peso molecular

antigen 33 kDa

reatividade de espécies

human

técnica(s)

immunocytochemistry: 1:20 using pretreated tissues
western blot: suitable

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... GZMB(3002)

Especificidade

Does not cross-react with granzyme A.

Imunogênio

recombinant human granzyme B.

Aplicação

Monoclonal Anti-Granzyme B antibody is suitable for western blot and immunocytochemistry at a dilution of 1:20 using pretreated tissues.

Ações bioquímicas/fisiológicas

Granzyme B, neutral serine protease, is expressed in cytoplasmic granules of activated cytotoxic T lymphocytes and natural killer cells. It contains a leader sequence (cleaved by a signal peptidase) and two amino acid prodomains (cleaved by the lysosomal cysteine protease DPPI). It plays a major role in the caspase dependent apoptotic pathway by activating most of the caspases in vitro and in vivo. It cleaves the aspartic acid residues, to facilitate cell death by various pathways. It has been shown that granzyme B has capacity to facilitate cytochrome C release from the mitochondria in a caspase independent way.

forma física

Supplied in serum-free culture medium containing 1% bovine serum albumin and 0.1% sodium azide.

Exoneração de responsabilidade

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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S Shresta et al.
Current opinion in immunology, 10(5), 581-587 (1998-10-31)
CD8+ cytotoxic lymphocytes, natural killer cells and lymphokine-activated killer cells depend primarily on the perforin/granzyme system to kill their targets, while CD4+ T cells utilize Fas and other mechanisms to induce cell death. The molecular mechanisms used by these pathways
J A Kummer et al.
Journal of immunological methods, 163(1), 77-83 (1993-07-06)
The human serine proteases granzymes A and B are expressed in cytoplasmic granules of activated cytotoxic T lymphocytes and natural killer cells. Recombinant granzyme A and granzyme B proteins were produced in bacteria, purified and then used to raise specific
J A Heibein et al.
Journal of immunology (Baltimore, Md. : 1950), 163(9), 4683-4693 (1999-10-21)
CTLs kill targets by inducing them to die through apoptosis. A number of morphological and biochemical events are now recognized as characteristic features of the apoptotic program. Among these, the disruption of the inner mitochondrial transmembrane potential (Delta Psi m)
J A Trapani et al.
Immunology today, 20(8), 351-356 (1999-08-04)
Viral strategies for escaping apoptosis have co-evolved with the immune system, resulting in a complex balance of pro- and anti-apoptotic forces in virus-infected cells under attack by cytotoxic T lymphocytes (CTLs). Here, Joseph Trapani and colleagues argue that CTL cytolytic
J A Trapani et al.
Current opinion in immunology, 12(3), 323-329 (2000-04-27)
Recent advances in our understanding of cytolytic effector mechanisms include the partial characterization of caspase-independent apoptotic pathways triggered by granzymes, a realization of the vital importance of perforin and granzymes in the defence against certain virus infections in vivo and

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