BD Pharmingen- Purified Mouse Anti-Human Caspase-9_BD Pharmingen
产品信息
抗原名称
Caspase-9
宿主
Mouse IgG1, κ
免疫原
Human caspase-9 N-terminal fragment aa 1-134
简单描述
The caspase family of cysteine proteases plays a key role in apoptosis and inflammation. Caspases are synthesized as inactive proenzymes containing three domains, that are processed into large and small subunits that associate to form the active enzyme. Processing can occur in apoptotic cells by either transactivation, self-proteolysis or cleavage by another protease. While caspases share a common structure, there are some differences, such as the preferred substrate specificity. These sequence differences in specificity, as well as the size of the NH2 -terminal prodomain, can be used to catagorize the caspases into functional groups including apoptotic initiators (long prodomains), apoptotic executioners (short prodomains), and cytokine processors. Caspase-9 is a member of the apoptotic initiator group of caspases which include caspases-2, -8, and -10. Activation of caspase-9 occurs in the presence of cytochrome c, following an interaction between caspase-9 and APAF-1. Activation may also be triggered directly by the cytotoxic T-cell protease, granzyme B. Active caspase-9 cleaves and thus activates caspase-3, and is also a relevant target of active caspase-3. Caspase-9 can also cleave the nuclear protein PARP. Northern blot analysis suggests that high expression of caspase-9 is found in the heart, testis, and ovary. The antibody recognizes the 47 kDa proform and 37 kDa cleaved form of human caspase-9. The N-terminal fragment (amino acids 1-134) of human caspase-9 was used as an immunogen.
商品描述
2-22
The caspase family of cysteine proteases plays a key role in apoptosis and inflammation. Caspases are synthesized as inactive proenzymes containing three domains, that are processed into large and small subunits that associate to form the active enzyme. Processing can occur in apoptotic cells by either transactivation, self-proteolysis or cleavage by another protease. While caspases share a common structure, there are some differences, such as the preferred substrate specificity. These sequence differences in specificity, as well as the size of the NH2 -terminal prodomain, can be used to catagorize the caspases into functional groups including apoptotic initiators (long prodomains), apoptotic executioners (short prodomains), and cytokine processors. Caspase-9 is a member of the apoptotic initiator group of caspases which include caspases-2, -8, and -10. Activation of caspase-9 occurs in the presence of cytochrome c, following an interaction between caspase-9 and APAF-1. Activation may also be triggered directly by the cytotoxic T-cell protease, granzyme B. Active caspase-9 cleaves and thus activates caspase-3, and is also a relevant target of active caspase-3. Caspase-9 can also cleave the nuclear protein PARP. Northern blot analysis suggests that high expression of caspase-9 is found in the heart, testis, and ovary. The antibody recognizes the 47 kDa proform and 37 kDa cleaved form of human caspase-9. The N-terminal fragment (amino acids 1-134) of human caspase-9 was used as an immunogen.
同种型
Mouse IgG1, κ
克隆号
克隆 2-22 (RUO)
浓度
0.5 mg/ml
产品详情
Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
应用
实验应用
Western blot (Routinely Tested)
反应种属
Human (QC Testing)
目标/特异性
Caspase-9
背景
别名
ICE-LAP-6, Mch6, Apaf-3
制备和贮存
存储溶液
Aqueous buffered solution containing ≤0.09% sodium azide.
保存方式
Aqueous buffered solution containing ≤0.09% sodium azide.
参考图片
Western blot analysis of caspase-9. Lysates from control (lanes 1-3) and amptothecin treated Jurkat cells (lanes 4-6) were probed with anti-human caspase-9 (clone 2-22, Cat. No. 551247) at concentrations of: 1.0 (lane 1), 0.5 (lane 2), and 0.25 µg/ml (lane 3). Caspase-9 is identified as a band of 47 kDa (proform), and 37 kDa (intermediate) in treated cells, and the 47 kDa band in control cells.
(+) = positive, (-) = negative, (NT) = not tested
Western blot analysis of caspase-9. Lysates from control (lanes 1-3) and amptothecin treated Jurkat cells (lanes 4-6) were probed with anti-human caspase-9 (clone 2-22, Cat. No. 551247) at concentrations of: 1.0 (lane 1), 0.5 (lane 2), and 0.25 µg/ml (lane 3). Caspase-9 is identified as a band of 47 kDa (proform), and 37 kDa (intermediate) in treated cells, and the 47 kDa band in control cells.
(+) = positive, (-) = negative, (NT) = not tested
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