CD156c polyclonal antibody; host Rabbit; reactivity Human, Mouse, Rat
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ADAM metallopeptidase domain 10(ADAM10) Homo sapiens Members of the ADAM family are cell surface proteins with a unique structure possessing both potential adhesion and protease domains. This gene encodes and ADAM family member that cleaves many proteins including TNF-alpha and E-cadherin. Alternate splicing results in multiple transcript variants encoding different proteins that may undergo similar processing. [provided by RefSeq, Feb 2016],
Fully tested in-house by ABMIUM, or supported by an advanced validation report from a partner reviewed 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 / reactivity | WB | IHC-P | IF | ELISA |
|---|---|---|---|---|
| Human,Mouse,Rat |
This product is manufactured by Reed Biotech and sold through ABMIUM without relabelling.
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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.
ADAM metallopeptidase domain 10 (ADAM10), also known as CD156c, is a membrane-associated disintegrin and metalloprotease. This ABMIUM target record links ADAM10 biology, verified identifiers and catalogue-backed research products.
Biological function: ADAM10 is a cell-surface metalloprotease with disintegrin and protease domains. Curated records describe ectodomain cleavage of multiple membrane proteins, supporting roles in regulated protein shedding, cell adhesion and signalling.
