Recombinant Human BAG3 Protein (GST Tag) supplied by Elabscience with collaborator-provided technical specifications.
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Recombinant Human BAG3 Protein (GST Tag) is a research-use recombinant protein from Elabscience preparation representing BAG3 supplied as Lyophilized. Review the expression, purity, formulation and storage specifications below before selecting it for an assay or functional workflow.
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 | Bioactivity | Binding | Cell-Based | In Vivo | ELISA Capture |
|---|---|---|---|---|---|
| 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.
BAG cochaperone 3 (BAG3), also known as BIS, is a stress-responsive HSP70-family co-chaperone involved in protein quality control and proteostasis. This target page groups ABMIUM catalogue reagents for studying BAG3-dependent chaperone responses, selective protein disposal and cellular stress biology.
Biological function: BAG3 binds HSP70-family chaperones through its BAG domain and helps coordinate chaperone-dependent protein quality control. It participates in stress-responsive proteostasis and can connect chaperone-bound clients to selective autophagic disposal pathways, supporting removal of damaged or aggregation-prone proteins.
