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G1044

Sigma-Aldrich

Monoclonal Anti-Granzyme B antibody produced in mouse

clone GrB7, tissue culture supernatant

Synonym(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

MDL number:
MFCD01865484
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

200

conjugate

unconjugated

antibody form

tissue culture supernatant

antibody product type

primary antibodies

clone

GrB7, monoclonal

description

not suitable for immunocytochemistry (frozen sections)

mol wt

antigen 33 kDa

species reactivity

human

technique(s)

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

UniProt accession no.

P10144

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GZMB(3002)

Specificity

Does not cross-react with granzyme A.

Immunogen

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.

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

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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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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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