CC076 | Human Collagen Type IV

CC076
100 µg  
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      Overview

      Key Spec Table

      Key Applications
      CULT
      Description
      Catalogue Number CC076
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      Description Human Collagen Type IV
      Overview Collagen type IV is the major structural element of basal membranes. Human collagen type IV is a native triple helix. Collagen was extracted from washed dissected tissue into dilute acetic acid after mild pepsin treatment. The Collagen type IV was purified by using differential salt precipitation. Purity and retention of native helical structure was controlled by SDS-PAGE and by reaction with anti-collagen type specific monoclonal antibodies. Molecular weight: 300kDa; Solubility: 10mg/mL
      References
      Product Information
      Presentation Liquid purified protein. In 100 μL of 0.5M acetic acid solution, pH 2.5. Salt-free, no preservative.
      Applications
      Key Applications
      • Cell Culture
      Application Notes Coating material for cell culture studies

      Formation of collagen gels

      Optimal working dilutions must be determined by end user.
      Biological Information
      Concentration 1 mg/mL
      Purity Human collagen type IV: 95% pure by SDS-PAGE.

      Human collagen types I-III, V, VI, and non-collagen proteins:<5%. Retention of native structure was confirmed by ability to form microfibrils.
      Source Human placenta, negative for HBsAg and HIV antibodies
      Species Human
      Entrez Gene Number
      Entrez Gene Summary This gene encodes the major type IV alpha collagen chain of basement membranes. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter.
      Gene Symbol
      • arresten
      • COL4A1
      • Arresten
      UniProt Number
      UniProt Summary FUNCTION: SwissProt: P02462 # Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Potently inhibits endothelial cell proliferation and angiogenesis. Inhibits angiogenesis potentially via mechanisms involving cell surface proteoglycans and the alpha and beta integrins of endothelial cells.
      SIZE: 1669 amino acids; 160615 Da
      SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)- alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.
      SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane.
      TISSUE SPECIFICITY: Highly expressed in placenta.
      DOMAIN: SwissProt: P02462 Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G- X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.
      PTM: Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates. & Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. & Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. & The trimeric structure of the NC1 domains may be stabilized by covalent bonds between Lys and Met residues.
      DISEASE: SwissProt: P02462 # Defects in COL4A1 are a cause of brain small vessel disease with hemorrhage [MIM:607595]. Brain small vessel diseases underlie 20 to 30 percent of ischemic strokes and a larger proportion of intracerebral hemorrhages. Inheritance is autosomal dominant. & Defects in COL4A1 are a cause of porencephaly type 1 [MIM:175780]; also known as encephaloclastic porencephaly. Porencephaly is a term used for any cavitation or cerebrospinal fluid-filled cyst in the brain. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma. Inheritance is autosomal dominant.
      SIMILARITY: Belongs to the type IV collagen family. & Contains 2 COL4C (collagen IV C-terminal) domains.
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage Conditions Store at -20ºC for up to 12 months. Avoid repeated freeze/thaw cycles.
      Packaging Information
      Material Size 100 µg
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      Certificates of Analysis

      TitleLot Number
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN - 2101977 2101977
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN - 2387742 2387742
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN - 2388840 2388840
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN 2470383
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN - 1994359 1994359
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN - 2005362 2005362
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN - 2042763 2042763
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN - 2193272 2193272
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN - 2278481 2278481
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN - 2280293 2280293
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN - 2325740 2325740

      References

      Reference overviewPub Med ID
      Isolation and partial characterization of a new human collagen with an extended triple-helical structural domain.
      Bentz, H, et al.
      Proc. Natl. Acad. Sci. U.S.A., 80: 3168-72 (1983) 1983

      6574478
      Isolation and characterization of a native placental basement-membrane collagen and its component alpha chains.
      Glanville, R W, et al.
      Eur. J. Biochem., 95: 383-9 (1979) 1979

      Show Abstract
      456357
      Characterization of a novel collagen chain in human placenta and its relation to AB collagen.
      Sage, H and Bornstein, P
      Biochemistry, 18: 3815-22 (1979) 1979

      Show Abstract
      224919

      Brochure

      Title
      Human Stem Cell Systems

      Data Sheet

      Title
      HUMAN COLLAGEN TYPE IV PURIFIED PROTEIN
      Reprogramming Cell Fate and Function Novel Strategies for iPSC Generation, Characterization, and Differentiation