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Goat Anti-Collagen, type VII Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q02388 |
| Other Accession | NP_000085, 1294, 12836 (mouse) |
| Reactivity | Rat |
| Predicted | Human, Mouse, Pig, Dog |
| Host | Goat |
| Clonality | Polyclonal |
| Concentration | 100ug/200ul |
| Isotype | IgG |
| Calculated MW | 295220 Da |
| Gene ID | 1294 |
|---|---|
| Other Names | Collagen alpha-1(VII) chain, Long-chain collagen, LC collagen, COL7A1 |
| Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Goat Anti-Collagen, type VII Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | COL7A1 |
|---|---|
| Function | Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen. |
| Cellular Location | Secreted, extracellular space, extracellular matrix, basement membrane |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes the alpha chain of type VII collagen. The type VII collagen fibril, composed of three identical alpha collagen chains, is restricted to the basement zone beneath stratified squamous epithelia. It functions as an anchoring fibril between the external epithelia and the underlying stroma. Mutations in this gene are associated with all forms of dystrophic epidermolysis bullosa. In the absence of mutations, however, an acquired form of this disease can result from an autoimmune response made to type VII collagen.
References
Type VII collagen: the anchoring fibril protein at fault in dystrophic epidermolysis bullosa. Chung HJ, et al. Dermatol Clin, 2010 Jan. PMID 19945621.
Forty-two novel COL7A1 mutations and the role of a frequent single nucleotide polymorphism in the MMP1 promoter in modulation of disease severity in a large European dystrophic epidermolysis bullosa cohort. Kern JS, et al. Br J Dermatol, 2009 Nov. PMID 19681861.
Long-term follow-up of patients with recessive dystrophic epidermolysis bullosa in the Netherlands: expansion of the mutation database and unusual phenotype-genotype correlations. van den Akker PC, et al. J Dermatol Sci, 2009 Oct. PMID 19665875.
Increased invasive behaviour in cutaneous squamous cell carcinoma with loss of basement-membrane type VII collagen. Martins VL, et al. J Cell Sci, 2009 Jun 1. PMID 19435799.
Collagen mRNA levels changes during colorectal cancer carcinogenesis. Skovbjerg H, et al. BMC Cancer, 2009 May 7. PMID 19422682.
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