R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
COL12A1 (F4D4U) Rabbit mAb #36276
Filter:
- WB
Supporting Data
REACTIVITY | H M |
SENSITIVITY | Endogenous |
MW (kDa) | 333 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
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
COL12A1 (F4D4U) Rabbit mAb recognizes endogenous levels of total COL12A1 protein.
Species Reactivity:
Human, Mouse
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human COL12A1 protein.
Background
The extracellular matrix (ECM) is a complex network of macromolecules that provides structural tissue support to cells in the basement membrane and interstitial matrix. It is composed of many molecules, including proteins, glycoproteins, proteoglycans, and polysaccharides (1,2). One of the major proteins that comprise the ECM, and the human body, is collagen. Collagens are a large family of proteins. They are trimeric molecules composed of three alpha polypeptide chains that form a triple helix structure that is characteristic of all collagens (3). The large family of collagens is divided into three subgroups: fibrillar collagens, non-fibril forming collagens, and fibril-associated collagens. These subgroups differ in their structure and supramolecular assembly (3).
Collagen type XII α1 chain (COL12A1), the largest member of the fibril-associated collagens with interrupted triple helix (FACIT) collagen family, contains fibronectin type III repeats, von Willebrand factor A domains, and two triple-helical domains (4). There are two major isoforms, a long form of 3063 amino acids and a short form of 1899 amino acids. COL12A1 binds to type I collagen fibrils and contributes to tissue biomechanics in the cornea, skeletal muscle, and tendon tissues (reviewed in 5). Mutations in the COL12A1 gene are correlated with myopathapies (6,7). COL12A1 expression is upregulated in several types of cancer; this elevation is thought to enhance tumor migration, invasiveness, and metastasis and, in some cases, correlates with poor prognosis (8-13).
Collagen type XII α1 chain (COL12A1), the largest member of the fibril-associated collagens with interrupted triple helix (FACIT) collagen family, contains fibronectin type III repeats, von Willebrand factor A domains, and two triple-helical domains (4). There are two major isoforms, a long form of 3063 amino acids and a short form of 1899 amino acids. COL12A1 binds to type I collagen fibrils and contributes to tissue biomechanics in the cornea, skeletal muscle, and tendon tissues (reviewed in 5). Mutations in the COL12A1 gene are correlated with myopathapies (6,7). COL12A1 expression is upregulated in several types of cancer; this elevation is thought to enhance tumor migration, invasiveness, and metastasis and, in some cases, correlates with poor prognosis (8-13).
- Barkan, D. et al. (2010) Eur J Cancer 46, 1181-8.
- Hynes, R.O. (2009) Science 326, 1216-9.
- Ricard-Blum, S. (2011) Cold Spring Harb Perspect Biol 3, a004978.
- Gerecke, D.R. et al. (1997) Genomics 41, 236-42.
- Chiquet, M. et al. (2014) Int J Biochem Cell Biol 53, 51-4.
- Hicks, D. et al. (2014) Hum Mol Genet 23, 2353-63.
- Zou, Y. et al. (2014) Hum Mol Genet 23, 2339-52.
- Yan, Y. et al. (2023) Endocr Relat Cancer 30, e230012. doi: 10.1530/ERC-23-0012.
- Papanicolaou, M. et al. (2022) Nat Commun 13, 4587.
- Jiang, X. et al. (2019) Mol Med Rep 20, 3103-3112.
- Wu, Y. and Xu, Y. (2020) Cancer Med 9, 4743-4755.
- Duan, S. et al. (2018) Mol Med Rep 18, 3727-3736.
- Karagiannis, G.S. et al. (2012) Oncotarget 3, 267-85.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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