ITC0050
ITC0050
- Catalog: ITC0050
- Gene/Protein: COL3A1
- Product Description: Immunotag™ Cleaved-COL3A1 (G1221) Polyclonal Antibody
460.0000
Price in reward points: 460
| Antibody Specification | |
| Datasheet | 
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| Target Protein | COL3A1 (G1221) |
| Clonality | Polyclonal |
| Storage/Stability | -20°C/1 year |
| Application | WB,ELISA |
| Recommended Dilution | Western Blot: 1/500 - 1/2000. ELISA: 1/10000. Not yet tested in other applications. |
| Concentration | 1 mg/ml |
| Reactive Species | Human |
| Host Species | Rabbit |
| Immunogen | The antiserum was produced against synthesized peptide derived from human Collagen III alpha1. AA range:1172-1221 |
| Specificity | Cleaved-COL3A1 (G1221) Polyclonal Antibody detects endogenous levels of fragment of activated COL3A1 protein resulting from cleavage adjacent to G1221. |
| Purification | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen |
| Form | Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide. |
| Gene Name | COL3A1 |
| Accession No. | P02461 P08121 |
| Alternate Names | COL3A1; Collagen alpha-1(III) chain |
| Description | collagen type III alpha 1 chain(COL3A1) Homo sapiens This gene encodes the pro-alpha1 chains of type III collagen, a fibrillar collagen that is found in extensible connective tissues such as skin, lung, uterus, intestine and the vascular system, frequently in association with type I collagen. Mutations in this gene are associated with Ehlers-Danlos syndrome types IV, and with aortic and arterial aneurysms. Two transcripts, resulting from the use of alternate polyadenylation signals, have been identified for this gene. [provided by R. Dalgleish, Feb 2008], |
| Cell Pathway/ Category | Focal adhesion,ECM-receptor interaction, |
| Protein Expression | Colon carcinoma,Liver,Placenta,Skin fibroblast, |
| Subcellular Localization | extracellular region,collagen trimer,collagen type III trimer,extracellular space,endoplasmic reticulum lumen,extracellular matrix, |
| Protein Function | disease:Defects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3) [MIM:130020]; also known as benign hypermobility syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS3 is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity.,disease:Defects in COL3A1 are a cause of susceptibility to aortic aneurysm abdominal (AAA) [MIM:100070]. AAA is a common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells.,disease:Defects in COL3A1 are the cause of Ehlers-Danlos syndrome type 4 (EDS4) [MIM:130050]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS4 is the most severe form of the disease. It is characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas.,function:Collagen type III occurs in most soft connective tissues along with type I collagen.,online information:Collagen type III alpha-1 chain mutations,online information:Type-III collagen entry,PTM:O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.,PTM:Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.,similarity:Belongs to the fibrillar collagen family.,similarity:Contains 1 VWFC domain.,subunit:Trimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines., |
| Usage | For Research Use Only! Not for diagnostic or therapeutic procedures. |
| Material Safety Data Sheet | |
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