Antibody data
- Antibody Data
- Antigen structure
- References [3]
- Comments [0]
- Validations [0]
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- Product number
- 611302 - Provider product page
- Provider
- BioLegend
- Proper citation
- BioLegend Cat#611302, RRID:AB_2227126
- Product name
- Purified anti-APC7
- Antibody type
- Polyclonal
- Antigen
- Recombinant (partial), N-terminal
- Description
- APC7 (anaphase-promoting complex subunit 7) is a member of the E3 enzyme family. This protein contains TPR repeats and has a molecular weight of approximately 63 kD. The APC7 protein is located in the nucleus during interphase and the centrosome during metaphase/anaphase. This protein probably recruits Cdh1 into the APC complex. The APC7 protein functions with other members of the APC complex as a multisubunit cell cycle ubiquitin ligase, and a regulator of sister chromatid separation by degrading securins. In addition, this protein functions in ubiquitin-dependent cyclin catabolism, metaphase/anaphase transition, and spindle elongation. The APC7 protein comprises one subunit of the anaphase promoting complex including APC1-8, and other probable complex proteins APC9-11, Cdc26, Mnd2, Swm1. The APC complex is inactivated by protein kinase A and is activated by CDC20 and Cdh1.
- Reactivity
- Human
- Host
- Rabbit
- Conjugate
- Unconjugated
- Vial size
- 200 µl
- Storage
- Upon receipt, store frozen at -20° C.
Submitted references Pathogenic role of macrophages in intradermal infection of methicillin-resistant Staphylococcus aureus in thermally injured mice.
Uncoupling of the spindle-checkpoint and chromosome-congression functions of BubR1.
Accumulation of substrates of the anaphase-promoting complex (APC) during human cytomegalovirus infection is associated with the phosphorylation of Cdh1 and the dissociation and relocalization of APC subunits.
Asai A, Tsuda Y, Kobayashi M, Hanafusa T, Herndon DN, Suzuki F
Infection and immunity 2010 Oct;78(10):4311-9
Infection and immunity 2010 Oct;78(10):4311-9
Uncoupling of the spindle-checkpoint and chromosome-congression functions of BubR1.
Elowe S, Dulla K, Uldschmid A, Li X, Dou Z, Nigg EA
Journal of cell science 2010 Jan 1;123(Pt 1):84-94
Journal of cell science 2010 Jan 1;123(Pt 1):84-94
Accumulation of substrates of the anaphase-promoting complex (APC) during human cytomegalovirus infection is associated with the phosphorylation of Cdh1 and the dissociation and relocalization of APC subunits.
Tran K, Mahr JA, Choi J, Teodoro JG, Green MR, Spector DH
Journal of virology 2008 Jan;82(1):529-37
Journal of virology 2008 Jan;82(1):529-37
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