| Product Name | Human Collagen Type IV (COL4) ELISA Kit |
|---|---|
| Description | Type-IV collagen is a type of collagen found primarily in the basal lamina. The C-terminus domain is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. Also, type-IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. This makes the overall arrangement more sloppy with kinks. These two features cause the collagen to form in a sheet, the form of the basal lamina.All of the type IV collagen in mammals is derived from six genetically distinct a-chain polypeptides (a1_a6). The type IV collagen a-chains have similar domain structures and share between 50_70% homology at the amino-acid level. The a-chains can be separated into three domains: an amino-terminal 7S domain, a middle triple-helical domain, and a carboxy-terminal globular non-collagenous (NC)-1 domain (see figure). This assay has high sensitivity and excellent specificity for detection of Human COL4. No significant cross-reactivity or interference between Human COL4 and analogues was observed. |
| Synonyms | Type-IV Collagen |
| Method | Sandwich ELISA |
| Detection Range | 1.56-100 ng/mL |
| Sensitivity | 0.07 ng/mL |
| Reactivity | Human |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background | Type-IV collagen is a type of collagen found primarily in the basal lamina. The C-terminus domain is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel. Also, type-IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. This makes the overall arrangement more sloppy with kinks. These two features cause the collagen to form in a sheet, the form of the basal lamina.All of the type IV collagen in mammals is derived from six genetically distinct a-chain polypeptides (a1_a6). The type IV collagen a-chains have similar domain structures and share between 50_70% homology at the amino-acid level. The a-chains can be separated into three domains: an amino-terminal 7S domain, a middle triple-helical domain, and a carboxy-terminal globular non-collagenous (NC)-1 domain (see figure). |
| Supplier | Abebio |
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