Rabbit Recombinant Monoclonal Hsp47 antibody - conjugated to APC.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 98% PBS, 1% BSA
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application Antibody Labelling | Reactivity Expected | Dilution info - | Notes - |
Application Target Binding Affinity | Reactivity Expected | Dilution info - | Notes - |
Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.
CBP1, CBP2, HSP47, SERPINH2, PIG14, SERPINH1, Serpin H1, 47 kDa heat shock protein, Arsenic-transactivated protein 3, Cell proliferation-inducing gene 14 protein, Collagen-binding protein, Rheumatoid arthritis-related antigen RA-A47, AsTP3, Colligin
Rabbit Recombinant Monoclonal Hsp47 antibody - conjugated to APC.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 98% PBS, 1% BSA
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.
Hsp47 also known as the heat shock protein 47 is a molecular chaperone with a molecular weight of approximately 47 kDa. It mainly resides in the endoplasmic reticulum and participates in collagen synthesis. Hsp47 binds specifically to unfolded procollagen chains ensures their proper folding and prevents premature aggregation. Due to its specialized function Hsp47 is highly expressed in collagen-producing cells like fibroblasts. Researchers commonly study this protein using techniques like Hsp47 ELISA to measure its expression or activity levels.
Hsp47 ensures the quality control of collagen within the secretory pathway. It does not form part of any large protein complexes but operates closely with collagen molecules. By stabilizing procollagen's triple-helix structure Hsp47 plays an important role in collagen biosynthesis. Dysfunctional collagen processes can arise without this protein's presence potentially leading to cellular stress or structural weaknesses within tissues rich in collagen.
Hsp47's activity integrates into the collagen synthesis and secretion pathways. This protein is related to other molecular chaperones such as Hsp70 that assist in maintaining protein homeostasis within the cell. Hsp47’s function links to fibrosis pathways because of its role in collagen maturation. In terms of fibrotic pathologies this involvement makes the chaperoning of procollagen a critical control point.
Disrupted Hsp47 function frequently associates with fibrotic conditions and osteogenesis imperfecta. Fibrosis results from excessive collagen deposition in which Hsp47 is deeply implicated. Additionally certain cancer types have shown altered Hsp47 expression correlating with increased cancer cell invasiveness due to extracellular matrix remodeling. Studies have noted interactions between Hsp47 and TGF-beta signaling in fibrotic tissues reinforcing its role in pathological collagen turnover.
We have tested this species and application combination and it works. It is covered by our product promise.
We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
We do not recommend this combination. It is not covered by our product promise.
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