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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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HSP47 Antibody / Collagen Chaperone Antibody recognizes HSP47, also known as SERPINH1, a collagen-specific molecular chaperone that resides primarily within the endoplasmic reticulum. Unlike many members of the heat shock protein family that assist with the folding of diverse client proteins, HSP47 displays remarkable substrate specificity by binding newly synthesized procollagen molecules during their maturation. This interaction promotes correct collagen folding, stabilizes the characteristic triple-helical structure, and helps prevent aggregation before secretion into the extracellular matrix. Because collagen is the most abundant structural protein in the human body, HSP47 is essential for normal connective tissue development, tissue integrity, wound healing, and organ function. An HSP47 Antibody is therefore widely used to investigate collagen biosynthesis, extracellular matrix organization, and diseases characterized by abnormal collagen production.
HSP47 expression is closely linked to tissues with active collagen synthesis, including fibroblasts, osteoblasts, chondrocytes, hepatic stellate cells, vascular smooth muscle cells, and many epithelial cell populations undergoing remodeling or repair. During collagen maturation, HSP47 binds procollagen within the endoplasmic reticulum and releases its cargo as environmental conditions change during transport toward the Golgi apparatus. Loss or dysfunction of HSP47 disrupts collagen assembly, resulting in defective extracellular matrix formation and impaired tissue architecture. Researchers studying connective tissue biology frequently examine HSP47 alongside collagen types I, II, III, and IV, as well as additional extracellular matrix proteins involved in tissue remodeling. Because of its highly specialized biological role, the protein has become an important marker for studies focused on collagen homeostasis rather than general cellular stress responses.
Numerous studies have demonstrated that elevated HSP47 expression accompanies pathological fibrosis affecting the lung, liver, kidney, heart, and other organs. Increased collagen deposition is a defining feature of many chronic fibrotic disorders, making HSP47 an attractive biomarker for understanding disease progression and evaluating potential anti-fibrotic therapies. Altered expression has also been reported in multiple cancers, where remodeling of the extracellular matrix contributes to tumor growth, invasion, angiogenesis, and metastatic spread. Investigators continue to explore how HSP47 influences tumor-associated fibroblasts, stromal interactions, epithelial-to-mesenchymal transition, and the formation of collagen-rich tumor microenvironments. An HSP47 Antibody is therefore valuable for both basic research and translational studies investigating fibrosis, cancer biology, tissue regeneration, and extracellular matrix remodeling.
HSP47 is commonly analyzed using Western blot, immunohistochemistry, immunofluorescence, immunocytochemistry, immunoprecipitation, and flow cytometry to evaluate protein expression, intracellular localization, and changes associated with disease or experimental treatment. Its predominately endoplasmic reticulum localization and tight relationship with collagen synthesis make it an informative marker for studies examining secretory pathway function and matrix production. When combined with complementary collagen, fibrosis, or extracellular matrix biomarkers, HSP47 provides additional insight into tissue remodeling and cellular differentiation. NSJ Bioreagents offers carefully validated antibodies to support these applications across diverse research models. An HSP47 Antibody / Collagen Chaperone Antibody provides researchers with a reliable tool for investigating collagen maturation, extracellular matrix biology, and the molecular mechanisms underlying fibrosis, connective tissue disorders, and cancer progression.
Browse our Cell Biology Antibodies page to find validated antibodies for HSP47 and other proteins involved in protein folding, collagen biosynthesis, endoplasmic reticulum function, and cellular homeostasis.
The stated application concentrations are suggested starting amounts. Titration of the HSP47 Antibody / Collagen Chaperone Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
Human partial recombinant protein (AA 247-418) was used as the immunogen for this HSP47 antibody.
After reconstitution, the HSP47 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
HSP47 antibody, SERPINH1 antibody, Serpin Family H Member 1 antibody, Heat Shock Protein 47 antibody, Collagen Chaperone antibody
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