Human Collagen type III 100 % (solid phase RIA at 1/500 dilution). Type III Collagen, MW 95 kDa, can be observed in skin, cartilage, human placenta and vitreous body. Cross Reactions: Human Collagen I, II, IV and V: < 0,1 % Human Fibronectin and Laminin: < 0,1 %. Does not react with Mouse, Rat, Bovine and Pig.
ELISA. RIA (> 1/1000). Immunflourescence assay: 1/80Immunohistochemistry on Paraffin Sections: 1/1000 (60 min at RT or 2-8 °C over night). Immunohistochemistry on Frozen Sections. Pretreatment for IHC: After de-waxing the tissue slices they are treated with 0.2 % hyaluronidase (app.300 U/mg) in TBS 15 min at 37 °C. There after non-specific binding isblocked by blocking serum or 3 % BSA in TBS. For peroxidase systems blocking with 1 %peroxide solution in TBS for 30 min at RT is recommended. Positive Control: Human skin and placenta.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Rekonstitution
Restore by adding 0.1 mL distilled water.
Konzentration
1.0 mg/mL
Buffer
PBS without preservatives or BSA.
Konservierungsmittel
Without preservative
Handhabung
Avoid repeated freezing and thawing.
Lagerung
4 °C/-20 °C
Informationen zur Lagerung
Store the antibody at 2-8 °C for one month or (in aliquots) at -20 °C for longer. Do not freeze working dilutions
EDS4A antikoerper, AW550625 antikoerper, Col3a-1 antikoerper, MMS10-W antikoerper, Ms10w antikoerper, mKIAA4231 antikoerper, col3a1 antikoerper, collagen type III alpha 1 chain antikoerper, collagen, type III, alpha 1 antikoerper, collagen, type III, alpha 1 (Ehlers-Danlos syndrome type IV, autosomal dominant) S homeolog antikoerper, COL3A1 antikoerper, Col3a1 antikoerper, col3a1 antikoerper, col3a1.S antikoerper
Hintergrund
Collagens consist in a family of highly specialized glycoproteins of which at least 16 genetically distinct types are known to date. The basal unit of a collagen molecule cosists in a tripel-helical structure formed by 3 alpha-chains. Predominant amino acids are glycine, proline and hydroxproline. Regularly also lysines and hydroxylysines occur, which are responsible for cross-linkage and glycosylation of the protein chains. Different composition of alpha-chains and different glycosylation contribute to the high variability of collagens in different tissues and organs. Type III collagen is an alpha1(III)-trimer, MW 95 kDa, which forms 67 nm cross-banded fibrils. Typically it can be observed in skin, cartilage, vitreous body, and human placenta.Synonyms: COL3A1