Rat Biglycan, BGN ELISA Kit
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Biglycan is a small leucine-rich repeat proteoglycan (SLRP) which is found in a variety of extracellular matrix tissues, including bone, cartilage and tendon. In humans, biglycan is encoded by the BGN gene which is located on the X chromosome.
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.
| Evidence | Serum | Plasma | Cell culture supernatants | Ascites | Tissue homogenates |
|---|---|---|---|---|---|
| Compatibility |
This product is manufactured by BT LAB 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.
BGN (biglycan) is a small leucine-rich extracellular-matrix proteoglycan involved in collagen fibril assembly, connective-tissue organization and tissue-remodelling biology.
Biological function: Biglycan is an extracellular-matrix structural proteoglycan. Human NCBI evidence supports roles in collagen fibril assembly, bone growth, muscle development and regeneration, while reviewed UniProt supports involvement in collagen-fiber assembly and extracellular-matrix structure.
