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G1044

Sigma-Aldrich

Monoclonal Anti-Granzyme B antibody produced in mouse

clone GrB7, tissue culture supernatant

Synonyme(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

Numéro MDL:
MFCD01865484
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

200

Conjugué

unconjugated

Forme d'anticorps

tissue culture supernatant

Type de produit anticorps

primary antibodies

Clone

GrB7, monoclonal

Description

not suitable for immunocytochemistry (frozen sections)

Poids mol.

antigen 33 kDa

Espèces réactives

human

Technique(s)

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

Numéro d'accès UniProt

P10144

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... GZMB(3002)

Spécificité

Does not cross-react with granzyme A.

Immunogène

recombinant human granzyme B.

Application

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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)
M J Smyth et al.
Journal of immunology (Baltimore, Md. : 1950), 154(12), 6299-6305 (1995-06-15)
Human granzyme B (hGrzB) is the key member of a family of granule serine proteases (granzymes) that participate in target cell death inflicted by cytotoxic lymphocytes. The proenzyme activation peptide predicted from the cDNA encoding hGrzB is composed of two
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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