B1k chain of laminin and methods of use

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

Reexamination Certificate

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C424S145100, C530S388240

Reexamination Certificate

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06916631

ABSTRACT:
Antibodies directed against laminin B1k are provided.

REFERENCES:
patent: 4834975 (1989-05-01), Siadak et al.
patent: 5003044 (1991-03-01), Hunter et al.
patent: 5610031 (1997-03-01), Burgeson et al.
patent: 5914317 (1999-06-01), Burgeson et al.
patent: WO 92/17498 (1992-10-01), None
Campbell A, General properties and applications of monoclonal antibodies, Elsevier Science Publishers, section 1.1, pp 1-32, 1984.
Harlow E, Lane D., Antibodies a laboratory manual. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press, 198 53-137.
Gerecke et al. cDNAs Encoding for Two of the Chains of Anchoring Filament Proein Kalinin Show Similarity to the Laminin B1 and B2 Chains. Matrix Collagen and Related Research. 13:(1):20-21.
Abaza MS, Atassi MZ. Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: demonstration with region 94-100 (antigenic site 3) of myoglobin.
Colman PM. Effects of amino acid sequence changes on antibody-antigen interactions. Res Immunol. 145(1):33-36, 1994.
Lederman S, et al. A single amino acid substitution in a common African allele of the CD4 molecule ablates binding of the monoclonal antibody, OKT4. Mol Immunol. 28(11):1171-81, 1991.
McMillan et al., “Ultrastructural Orientation of Laminin 5 in the Epidermal Basement Membrane: an Updated Model for Basement Membrane Organization,The Journal of Histochemistry&Cytochemistry”,vol. 51, No. 10, pp. 1299-1306 (2003).
U.S. Appl. No. 08/141,233, filed Oct. 1993, Burgeson et al.
Aratani et al., “Enhanced Synthesis and Secretion of Type IV Collagen and Entactin during Adipose Conversion of 3T3-L1 Cells and Production of Unorthodox Laminin Complex”The Journal of Biological Chemistry,vol. 263, No. 31, pp. 16163-16169, (1988).
Beck et al., “Structure and Function of Laminin: Anatomy of a Multidomain Glycoprotein”The FASEB Journal,vol. 4, pp. 148-160, (1990).
Berger et al. (eds) “Guide to Molecular Cloning Techniques”,Meth. in Enzymology152:316-703 ((1987).
Cooper et al., “Studies on the Biosynthesis of Laminin by Murine Parietal Endoderm Cells”European Journal of Biochemistry,vol. 119, pp. 189-197, (1981).
Davis et al., “Isolation and Characterization of Rat Schwannoma Neurite-promoting Factor. Evidence that the Factor Contains Laminin”The Journal of Neuroscience,vol. 5, No. 10, pp. 2662-2671, (1985).
Edgar et al., “Structural Requirements for the Stimulation of Neurite Outgrowth by Two Variants of Laminin and Their Inhibition by Antibodies”The Journal of Cell Biology,vol. 106, pp. 1299-1306, (1988).
Ehrig et al., “Merosin, A Tissue-Specific Basement Membrane Protein, is a Laminin-Like Protein”Proceedings of the National Academy of Sciences,vol. 87, pp. 3264-3268, (1990).
Engvall et al., “Distribution and Isolation of Four Laminin Variants; Tissue Restricted Distribution of Heterotrimers Assembled From Five Different Subunits”Cell Regulation,vol. 1, pp. 731-740, (1990).
Engvall et al., “Mapping of Domains in Human Laminin Using Monoclonal Antibodies: Localization of the Neurite-promoting Site”The Journal of Cell Biology,vol. 103, No. 6, pp. 2457-2465, (1986).
Frenette et al., “Biosynthesis and Secretion of Laminin and Laminin-associated Glycoproteins by Nonmalignant and Malignant Human Keratinocytes: Comparison of Cell Lines from Primary and Secondary Tumors in the Same Patient”Cancer Res,vol. 48, pp. 5193-5202, (1988).
Gerecke et al., “cDNA's Encoding for the Three Chains of the Anchoring Filament Protein Kalinin Show Similarity to the Laminin A B1 and B2 Chains”,Mol. Biol. Cell,vol. 3, (suppl.), p. # 1A, (1992).
Hunter et al., “Laminin Chain Assembly by Triple and Double Stranded Coiled-Coll Structures”,The Journal of Biological Chemistry,vol. 267, No. 9, pp. 6006-6011, (1992).
Hunter et al., “Expression of S-Laminin and Laminin in the Developing Rat Central Nervous System”The Journal of Comparative Neurology,vol. 323, pp. 238-251, (1992).
Hunter et al., “An LRE (Leucine-Arginine-Glutamate)-dependent Mechanism for Adhesion of Neurons to S-laminin”The Journal of Neuroscience,vol. 11, No. 12, pp. 3960-3671, (1991).
Hunter et al., “Primary Sequence of a Motor Neuron-Selective Adhesive Site in the Synaptic Basal Lamina Protein S-Laminin”Cell,vol. 59, pp. 905-913, (1989).
Liesi et al., “Glial Cells of Mammalian Brain Produce a Variant Form of Laminin”Experimental Neurology,vol. 105, pp. 86-92, 1989.
Marinkovich et al., “The Anchoring Filament Protein Kalinin is Synthesized and Secreted as a High Molecular Weight Precursor”,The Journal of Biological Chemistry,vol. 267, No. 25, pp. 17900-17906, (1992).
Marinkovich et al., “The Dermal-Epidermal Junction of Human Skin Contains a Novel Laminin Variant”The Journal of Cell Biology,vol. 119, No. 3, pp. 695-703, 1992.
Marinkovich et al., “Characterization of a Novel Laminin Isoform Produced by Human KeratinocytesIn Vitro”, Clinical Research,vol. 39, No. 2, pp. # 565A, (1991).
Morita et al., “Post-translational Assembly and Glycosylation of Laminin Subunits in Parietal Endoderm-like F9 Cells”Biochemistry Journal,vol. 229, pp. 259-264, (1985).
Paulsson et al., “Mouse Heart Laminin”The Journal of Biological Chemistry,vol. 264, No. 31, pp. 18726-18732, 1989.
Peters et al., “The Biosynthesis, Processing, and Secretion of Laminin by Human Choriocarcinoma Cells”The Journal of Biological Chemistry,vol. 260, No. 27, pp. 14732-14742, (1985).
Rouselle et al., “Kalinin: An Epithelium-Specific Basement Membrane Adhesion Molecule That is a Component of Anchoring Filaments”Journal Cell Biology,vol. 114, pp. 567-576, (1991).
Sanes et al., “S-Laminin”Cold Spring Harbor Symposia on Quantitative Biology,vol. 55, pp. 419-430, (1990).
Wewer et al., “Human Laminin isolated in a Nearly Intact, Biologically Active Form from Placenta by Limited Proteolysis”The Journal of Biological Chemistry,vol. 258, No. 20, pp. 12654-12660, (1983).
Woodley et al., “Laminin Inhibits Human Keratinocyte Migration”Journal of Cellular Physiology,vol. 136, pp. 140-146, (1988).
Gerecke et al., “cDNAs Encoding for Two of the Chains of the . . . ”, Matrix 13:20-21, Jan. 1993.

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