R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
ECM1 (E3B9A) Rabbit mAb #83458
Filter:
- WB
- IF
Supporting Data
REACTIVITY | H |
SENSITIVITY | Endogenous |
MW (kDa) | 75-100 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Immunofluorescence (Immunocytochemistry) | 1:800 - 1:3200 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
ECM1 (E3B9A) Rabbit mAb recognizes endogenous levels of total ECM1 protein.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of human ECM1 protein.
Background
Extracellular matrix gene 1 (ECM1) is a secreted glycoprotein found primarily in the extracellular matrix. It acts as both a multifunctional binding core and as a scaffolding protein that interacts with a variety of extracellular and structural proteins, including perlecan, fibulin-1C/1D, and MMP-9. (1). Research studies have shown that ECM1 is involved in the maintenance of tissue integrity and homeostasis, T cell immune responses, and angiogenesis (2-5). Its importance in maintaining tissue integrity is demonstrated by reports showing that mutations in the gene encoding ECM1 lead to skin lipoid proteinosis (1). Notably, ECM1 expression is upregulated in a variety of cancers, and during metastasis, suggesting a role for ECM1 in promoting tumor cell proliferation and invasion (6). In this context, research studies have shown that ECM1 can activate various signaling pathways, such as integrin/FAK, MMP-9/galectin-3, and S100A4/RhoA (7-9). In hepatic tissues, it was furthermore shown that ECM1 contributes to maintaining the latency of TGF-β in the extracellular matrix, thereby preventing spontaneous TGF-β activation and liver fibrosis (10,11).
- Chan, I. et al. (2007) Exp Dermatol 16, 881-90.
- Sercu, S. et al. (2008) J Invest Dermatol 128, 1397-408.
- Kong, L. et al. (2010) Matrix Biol 29, 276-86.
- Han, Z. et al. (2001) FASEB J 15, 988-94.
- He, L. et al. (2018) Proc Natl Acad Sci U S A 115, 8621-8626.
- Wang, L. et al. (2003) Cancer Lett 200, 57-67.
- Gan, L. et al. (2018) Oncogene 37, 744-755.
- Lee, K.M. et al. (2014) Breast Cancer Res 16, 479.
- Gómez-Contreras, P. et al. (2017) Clin Exp Metastasis 34, 37-49.
- Fan, W. et al. (2019) Gastroenterology 157, 1352-1367.e13.
- Li, Y. et al. (2022) JHEP Rep 4, 100397.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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