G1044
モノクローナル抗グランザイムB抗体 マウス宿主抗体
clone GrB7, tissue culture supernatant
別名:
Anti-C11, Anti-CCPI, Anti-CGL-1, Anti-CGL1, Anti-CSP-B, Anti-CSPB, Anti-CTLA1, Anti-CTSGL1, Anti-HLP
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すべての画像(1)
About This Item
結合体:
unconjugated
application:
ICC
WB
WB
クローン:
GrB7, monoclonal
化学種の反応性:
human
citations:
6
テクニック:
immunocytochemistry: 1:20 using pretreated tissues
western blot: suitable
western blot: suitable
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由来生物
mouse
品質水準
結合体
unconjugated
抗体製品の状態
tissue culture supernatant
抗体製品タイプ
primary antibodies
クローン
GrB7, monoclonal
詳細
not suitable for immunocytochemistry (frozen sections)
分子量
antigen 33 kDa
化学種の反応性
human
テクニック
immunocytochemistry: 1:20 using pretreated tissues
western blot: suitable
UniProtアクセッション番号
輸送温度
dry ice
保管温度
−20°C
ターゲットの翻訳後修飾
unmodified
遺伝子情報
human ... GZMB(3002)
特異性
グランザイムAとの交差反応性はありません。
免疫原
リコンビナントヒトグランザイムB。
アプリケーション
Monoclonal Anti-Granzyme B antibody is suitable for western blot and immunocytochemistry at a dilution of 1:20 using pretreated tissues.
生物化学的／生理学的作用
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.
物理的形状
無血清培養上清 (0.7% BSA, 0.1%アジ化ナトリウム含有)。
免責事項
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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保管分類コード
12 - Non Combustible Liquids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
G1044-VAR:
G1044-1ML:
G1044-BULK:
G1044-1ML-PW:
最新バージョンのいずれかを選択してください：
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 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 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 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
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
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