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Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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96-Well Plate
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48-602MAG
Buffer Detection Kit for Magnetic Beads
1 Kit
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Human Collagen Type IV: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
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
HS Code
3504 00 90
Presentation
Liquid purified protein. In 100 μL of 0.5M acetic acid solution, pH 2.5. Salt-free, no preservative.
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.
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.
Stem Cell Type
Human Embryonic Stem Cells
Mesenchymal Stem Cells
Neural Stem Cells
Hematopoietic Stem Cells
Epithelial Cells
Pancreatic Stem Cells
Induced Pluripotent Stem Cells
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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.
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)
1982
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
A novel collagen chain, termed alpha C, has been isolated from human placenta by limited pepsin digestion. The collagen containing the alpha C chain copurifies with placental AB collagen during selective salt precipitation but is virtually absent from fetal birth membranes, which contain relatively larger amounts of AB. Both native AB and alpha C-containing collagens are resistant to human skin collagenase under conditions that support cleavage of type I by greater than 90%. The alpha C chain was separated from alpha B by phosphocellulose chromatography and subsequently from alpha P by chromatography on CM-cellulose. Its amino acid composition is distinct from alpha A and alha B although all three chains posses compositional features in common; the carbohydrate content of the alpha C chain was intermediate between those of alpha A and alpha B. Analysis by NaDodSO4-polyacrylamide gel electrophoresis of peptides produced by CNBr cleavage and by limited digestion with the enzyme mast cell protease indicated different and unique products for the alpha A, alpha B, and alpha C chains. The data support the existence of another collagen chain which is related to the alpha A and alpha B chains but which is structurally unique. The proteins containing these chains may in turn comprise a subfamily of collagen isotypes which represents a divergence from and/or specialization of the type IV basement membrane collagens.
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
Native type IV collagen was isolated from human placenta using pepsin solubilisation followed by fractional salt precipitation and chromatogarphic purification. The native preparation was characterised using amino acid analyses, disc gel electrophoresis, segment-long-spacing crystallites and immunological methods. Two component alpha chains were isolated with molecular weights of approximately 95000 and 70000. Cyanogen bromide digests of these chains indicated that they are not related to any of the known alpha chains of interstitial collagens or to the recently described collagen containing alphaA and alphaB chains. They are also not related to one another and are therefore probably fragments of two genetically distinct type IV collagen alpha chains.
ECM coated plates that meet cell type-specific needs for growth and adhesion. Weitere Informationen >>
Collagen Antibodies
Millipore offer Collagen antibodies, proteins and kits for your ECM and adhesion research. See below for a list of Collagen related products, based on the expertise of Upstate & Chemicon. Weitere Informationen >>