Anti-Collagen I + II + III + IV + V antibody (ab24117)
- Product nameAnti-Collagen I + II + III + IV + V antibodySee all Collagen I + II + III + IV + V primary antibodies ...
- DescriptionRabbit polyclonal to Collagen I + II + III + IV + V
- Specificityab24117 recognises collagen I, II, III, IV and V. Antisera to specific collagen types were blended so to achieve equal reaction to any of the collagen types used.
- Tested applicationsIHC-Fr, Dot Blot, ELISA more details
- Species reactivityReacts with: Human
Full length protein. Immunogens are extensively purified native collagen type I, II, III, IV and V.
- Positive controlHuman kidney, liver, skin and heart
- Storage instructionsStore at +4°C short term (1-2 weeks). Aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
- Storage bufferPreservative: None
- Concentration information loading...
- PurityIgG fraction
- Purification notesAmmonium sulfate precipitation + DEAE cellulose chromatography + Cross-absorption with immobilized human serum proteins.
- Clonality Polyclonal
- Research Areas
Our Abpromise guarantee covers the use of ab24117 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|Dot Blot||Dot: Use at an assay dependent dilution.|
- RelevanceCollagen I is a member of group I collagen (fibrillar forming collagen), it forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. Collagen II is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces. High expression of isoform 2 in juvenile chondrocyte and low in fetal chondrocyte. Collagen III occurs in most soft connective tissues along with collagen I. Collagen IV is the major structural component of glomerular basement membranes, forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Collagen V is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Collagen V binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.
- Cellular localizationExtracellular
- Entrez Gene: 1277 Human
- Entrez Gene: 1280 Human
- Entrez Gene: 1281 Human
- Entrez Gene: 1282 Human
- Entrez Gene: 1289 Human
- Omim: 120150 Human
- Omim: 120140 Human
- Omim: 120180 Human
- Omim: 120130 Human
- Omim: 120215 Human
- SwissProt: P02452 Human
- SwissProt: P02458 Human
- SwissProt: P02461 Human
- SwissProt: P02462 Human
- SwissProt: P20908 Human
- Unigene: 172928 Human
- Unigene: 408182 Human
- Unigene: 443625 Human
- Unigene: 17441 Human
- Unigene: 210283 Human
- COL11A3 antibodyCOL1A1 antibodyCOL2A1 antibody
- COL3A1 antibodyCOL4A1 antibodyCOL5A1 antibodyCollagen alpha 1 chain antibodyCollagen alpha 1 II chain precursor contains chondrocalcin antibodyCollagen alpha 1 III chain precursor antibodyCollagen alpha 1 V chain precursor antibodyCollagen alpha 1(I) chain antibodyCollagen alpha 1(II) chain antibodyCollagen alpha 1(III) chain antibodyCollagen alpha 1(IV) chain antibodyCollagen alpha 1(V) chain antibodyCollagen alpha 2 I chain precursor antibodyCollagen alpha 2 V chain precursor antibodyCollagen I alpha 1 polypeptide antibodyCollagen II alpha 1 polypeptide antibodyCollagen IV alpha 1 polypeptide antibodyCollagen type I alpha 1 antibodyCollagen type I alpha 2 antibodyCollagen type II alpha 1 antibodyCollagen type III alpha 1 antibodyCollagen type IV alpha 1 antibodyCollagen type V alpha 1 antibodyCollagen type V alpha 2 antibodyEDS4A antibodyEhlers Danlos syndrome type IV autosomal dominant antibodyOI4 antibodyPrimary osteoarthritis spondyloepiphyseal dysplasia congenital antibodySEDC antibody
References for Anti-Collagen I + II + III + IV + V antibody (ab24117)
This product has been referenced in:
- Demidova-Rice TN et al. Bioactive peptides derived from vascular endothelial cell extracellular matrices promote microvascular morphogenesis and wound healing in vitro. Wound Repair Regen 19:59-70 (2011). IP ; Human . Read more (PubMed: 21134032) »
- Layton BE et al. Collagen's triglycine repeat number and phylogeny suggest an interdomain transfer event from a Devonian or Silurian organism into Trichodesmium erythraeum. J Mol Evol 66:539-54 (2008). Read more (PubMed: 18521530) »