JavaScript is disabled in your browser. Please enable JavaScript to view this website.
AB109150

Recombinant Human Clusterin protein

Recombinant Human Clusterin protein

Be the first to review this product! Submit a review

|

(0 Publication)

Recombinant Human Clusterin protein is a Human Full Length protein, in the 1 to 449 aa range, expressed in HEK 293 cells, with >90%, < 0.1 EU/µg endotoxin level, suitable for SDS-PAGE.

別名を表示する

APOJ, CLI, KUB1, AAG4, CLU, Clusterin, Aging-associated gene 4 protein, Apolipoprotein J, Complement cytolysis inhibitor, Ku70-binding protein 1, NA1/NA2, Sulfated glycoprotein 2, Testosterone-repressed prostate message 2, Apo-J, SGP-2, TRPM-2

Key facts

精製度

>90% SDS-PAGE

エンドトキシンレベル

< 0.1 EU/µg

発現系

HEK 293 cells

タグ

DDDDK tag C-Terminus

アプリケーション

SDS-PAGE

applications

生物活性

No

アクセッション番号

P10909

アニマルフリー

No

キャリアフリー

No

Human

再構成

Reconstitute in 100 µL of water

バッファー組成

pH: 7.2 Constituents: PBS

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

製品の詳細

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.

配列情報

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"80 kDa","actualMolecularWeight":null,"aminoAcidEnd":449,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P10909","tags":[{"tag":"DDDDK","terminus":"C-Terminus"}]}]

出荷温度及び保存条件

出荷温度
Blue Ice
短期保存温度
-20°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
False

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

Clusterin also known as Apolipoprotein J (ApoJ) is a glycoprotein with a mass of approximately 75-80 kDa. Scientists find clusterin expressed widely in the human body including the brain kidney and reproductive organs. This protein exists in two isoforms a secreted form and a nuclear form each with different locations and functions within the cells.
Biological function summary

Clusterin plays multiple roles particularly in lipid transport apoptosis and cell-cell interactions. It does not form part of a larger protein complex but it acts as a molecular chaperone that helps in folding and clearance of damaged proteins. This capability allows clusterin to protect cells against stress conditions such as oxidative stress by preventing abnormal protein aggregation.

Pathways

Clusterin is involved in pathways related to cell survival and lipid metabolism. It plays a role in the insulin signaling pathway and interacts with proteins like Heat Shock Protein 70 (HSP70) to assist in protein folding and in the activation of apoptotic pathways when needed. Clusterin's function in these processes helps in maintaining cellular homeostasis.

Scientists associate clusterin with Alzheimer’s disease and cancer progression. Elevated levels of clusterin have been observed in Alzheimer's patients suggesting a role in amyloid-beta plaque formation. In cancer clusterin expression influences tumor progression and resistance to therapies. Its interaction with other proteins such as Bax modulates the apoptotic pathways impacting cancer cell survival and chemotherapy resistance.

製品の性状

製品の状態

Lyophilized

補足情報

ab109150 is 0.2µm filtered

一般的な情報

機能

Isoform 1. Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed : 11123922, PubMed : 19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed : 11123922, PubMed : 12176985, PubMed : 17260971, PubMed : 19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed : 12047389, PubMed : 17407782, PubMed : 17412999). Does not require ATP (PubMed : 11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed : 11123922). Does not refold proteins by itself (PubMed : 11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed : 21505792). Protects cells against apoptosis and against cytolysis by complement (PubMed : 2780565). Intracellular forms 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 (PubMed : 20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed : 20068069). Modulates NF-kappa-B transcriptional activity (PubMed : 12882985). A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed : 16113678, PubMed : 17689225). Plays a role in the regulation of cell proliferation (PubMed : 19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed : 22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed : 24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).. Isoform 6. Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity.. Isoform 4. Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed : 24073260). Promotes cell death through interaction with BCL2L1 that releases and activates BAX (PubMed : 21567405).

配列の類似性

Belongs to the clusterin family.

翻訳後修飾

Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen (PubMed:2387851). Proteolytic cleavage is not necessary for its chaperone activity (PubMed:25402950). All non-secreted forms are not proteolytically cleaved (PubMed:24073260). Chaperone activity of uncleaved forms is dependent on a non-reducing environment (PubMed:25402950).. Polyubiquitinated, leading to proteasomal degradation (PubMed:17451556, PubMed:19137541). Under cellular stress, the intracellular level of cleaved form is reduced due to proteasomal degradation (PubMed:17451556).. Extensively glycosylated with sulfated N-linked carbohydrates (PubMed:17260971, PubMed:2387851). About 30% of the protein mass is comprised of complex N-linked carbohydrate (PubMed:2387851). Endoplasmic reticulum (ER) stress induces changes in glycosylation status and increases level of hypoglycosylated forms (PubMed:22689054). Core carbohydrates are essential for chaperone activity (PubMed:25402950). Non-secreted forms are hypoglycosylated or unglycosylated (PubMed:24073260).

細胞内局在性

Nucleus

製品プロトコール

ターゲットの情報

Isoform 1. Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed : 11123922, PubMed : 19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed : 11123922, PubMed : 12176985, PubMed : 17260971, PubMed : 19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed : 12047389, PubMed : 17407782, PubMed : 17412999). Does not require ATP (PubMed : 11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed : 11123922). Does not refold proteins by itself (PubMed : 11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed : 21505792). Protects cells against apoptosis and against cytolysis by complement (PubMed : 2780565). Intracellular forms 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 (PubMed : 20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed : 20068069). Modulates NF-kappa-B transcriptional activity (PubMed : 12882985). A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed : 16113678, PubMed : 17689225). Plays a role in the regulation of cell proliferation (PubMed : 19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed : 22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed : 24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).. Isoform 6. Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity.. Isoform 4. Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed : 24073260). Promotes cell death through interaction with BCL2L1 that releases and activates BAX (PubMed : 21567405).
See full target information CLU

Abcam product promise

当社は、高品質な試薬を通じてお客様の研究を力強くサポートすることをお約束いたします。ご使用いただく各段階で、常にお客様をサポートできる体制を整えております。万が一、製品が期待通りに機能しない場合は、「Abcam Product Promise」による当社保証制度に基づき、安心してご利用いただけます。
保証に関する詳細については利用規約をご確認ください。

Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.

For licensing inquiries, please contact partnerships@abcam.com