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AB285909

Recombinant human Clusterin protein (Active)

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Recombinant human Clusterin protein (Active) is a Human Fragment protein, in the 23 to 449 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, FuncS, Size Exclusion Chromatography.

View Alternative Names

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

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Functional Studies - Recombinant human Clusterin protein (Active) (AB285909)
  • FuncS

Supplier Data

Functional Studies - Recombinant human Clusterin protein (Active) (AB285909)

Functional studies of ab285909.

Human Procathepsin K was activated at pH 4 in the presence and absence of ApoJ, and then its overall activity was measured by Cathepsin K Activity Assay Kit. The above results indicate that ApoJ slows the activation/degradation process of Procathepsin K under chemical stress.

Size Exclusion Chromatography - Recombinant human Clusterin protein (Active) (AB285909)
  • Size Exclusion Chromatography

Supplier Data

Size Exclusion Chromatography - Recombinant human Clusterin protein (Active) (AB285909)

SEC analysis of a mixture of Thyroglobulin and ApoJ at room temperature (A) and after heating at 60°C for 1 h (B) confirming the chaperone activity of ApoJ by protecting Thyroglobulin when exposed to stress conditions such as heat.

SDS-PAGE - Recombinant human Clusterin protein (Active) (AB285909)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human Clusterin protein (Active) (AB285909)

SDS-PAGE analysis of ab285909.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

SDS-PAGE, Size Exclusion Chromatography, FuncS

applications

Biologically active

Yes

Biological activity

The chaperone activity of ApoJ was confirmed by its ability to bind to proteins under physical stress such as heat (e.g. Thyroglobulin) and chemical stress such as change in pH (e.g. Procathepsin K).

Accession

P10909

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in water

Storage buffer

pH: 7.5 Constituents: 0.58% Sodium chloride, 0.41% Sodium phosphate

storage-buffer

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Reactivity data

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

This product is manufactured by BioVision, an Abcam company and was previously called 7584 ApoJ/Clusterin, human recombinant. 7584-50 is the same size as the 50 µg size of ab285909.
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Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":449,"aminoAcidStart":23,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P10909","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate long-term storage conditions
-20°C
True
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Supplementary information

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.
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Specifications

Form

Lyophilized

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General info

Function

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).

Sequence similarities

Belongs to the clusterin family.

Post-translational modifications

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).

Subcellular localisation

Nucleus

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Product protocols

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Target data

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
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