Anti-Human CLU Antibody [A868] with collaborator-tested evidence for WB, Flow Cyt, ICC/IF.
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Anti-Human CLU Antibody [A868] is a research-use antibody from Elabscience for studying CLU in WB, Flow Cytometry, IF/ICC workflows with listed reactivity for Human. Specifications and supporting documents below should be reviewed when planning the experiment.
Fully tested in-house by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
| Species | WB | IHC-P | IHC-Fr | IF/ICC | Flow Cyt | IP | ChIP | ICC/IF |
|---|---|---|---|---|---|---|---|---|
| Human |
This product is manufactured by Elabscience and sold through ABMIUM without relabelling.
ABMIUM supports global orders. Availability, shipping requirements and applicable import arrangements are confirmed before fulfilment where required.
Yes. Send your target, sample, application and experimental conditions through ABMIUM MATCH or technical support.
Unless the listing expressly states otherwise, ABMIUM products are supplied for research use only and are not for diagnostic or therapeutic use.
Clusterin (CLU), also known as apolipoprotein J or ApoJ, is a secreted extracellular chaperone protein. This target guide connects human NCBI Gene 1191, UniProtKB P10909 and ABMIUM catalogue products associated with clusterin / CLU.
Biological function: Clusterin functions as an extracellular chaperone that helps prevent aggregation of non-native and stress-damaged proteins. The major secreted form can inhibit formation of several amyloid fibrils in vitro and maintain partially unfolded proteins in a state that can be handled by other chaperone systems.
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