Recombinant Human Clusterin protein (ab109150)
Key features and details
- Expression system: HEK 293 cells
- Purity: > 90% SDS-PAGE
- Endotoxin level: < 0.100 Eu/µg
- Tags: DDDDK tag C-Terminus
- Suitable for: SDS-PAGE
製品の詳細
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製品名
Recombinant Human Clusterin protein
Clusterin タンパク質・ペプチド 製品一覧 -
精製度
> 90 % SDS-PAGE.
ab109150 is 0.2µm filtered -
エンドトキシン・レベル
< 0.100 Eu/µg -
発現系
HEK 293 cells -
アクセッション番号
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タンパク質長
Full length protein -
Animal free
No -
由来
Recombinant -
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生物種
Human -
予測される分子量
80 kDa including tags -
領域
1 to 449 -
タグ
DDDDK tag C-Terminus
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関連製品
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Related Products
特性
Our Abpromise guarantee covers the use of ab109150 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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アプリケーション
SDS-PAGE
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製品の状態
Lyophilized -
備考
Working aliquots are stable for up to 3 months when stored at -20°C.
The secreted form of Apolipoprotein J is a heterodimeric disulfide-linked glycoprotein of 76–80 kDa.
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Concentration information loading...
前処理および保存
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保存方法および安定性
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
pH: 7.20
Constituent: PBS -
再構成Reconstitute with 100µl sterile water. PBS containing at least 0.1% BSA should be used for further dilutions.
関連情報
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別名
- 40
- AAG 4
- AAG4
see all -
機能
Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. -
組織特異性
Detected in blood plasma, cerebrospinal fluid, milk, seminal plasma and colon mucosa. Detected in the germinal center of colon lymphoid nodules and in colon parasympathetic ganglia of the Auerbach plexus (at protein level). Ubiquitous. Detected in brain, testis, ovary, liver and pancreas, and at lower levels in kidney, heart, spleen and lung. -
配列類似性
Belongs to the clusterin family. -
翻訳後修飾
Isoform 1 is proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen.
Polyubiquitinated, leading to proteasomal degradation.
Heavily N-glycosylated. About 30% of the protein mass is comprised of complex N-linked carbohydrate. -
細胞内局在
Secreted. Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress and Nucleus. Cytoplasm. Mitochondrion membrane. Cytoplasm, cytosol. Microsome. Endoplasmic reticulum. Cytoplasmic vesicle, secretory vesicle, chromaffin granule. Isoforms lacking the N-terminal signal sequence have been shown to be cytoplasmic and/or nuclear. Secreted isoforms can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. - Information by UniProt
プロトコール
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
データシートおよび資料
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Datasheet download
参考文献 (0)
ab109150 は論文での使用が確認できていません。