207 results about "Sequence homology" patented technology

Polymerases from the Pol I family which are able to efficiently use ddNTPs have demonstrated a much improved performance when used to sequence DNA. A number of mutations have been made to the gene coding for the Pol II family DNA polymerase from the archaeon Pyrococcus furiosus with the aim of improving ddNTP utilisation. "Rational" alterations to amino acids likely to be near the dNTP binding site (based on sequence homologies and structural information) did not yield the desired level of selectivity for ddNTPs. However, alteration at four positions (Q472, A486, L490 and Y497) gave rise to variants which incorporated ddNTPs better than the wild type, allowing sequencing reactions to be carried out at lowered ddNTP:dNTP ratios. Wild type Pfu-Pol required a ddNTP:dNTP ratio of 30:1; values of 5:1 (Q472H), 1:3 (L490Y), 1:5 (A486Y) and 5:1 (Y497A) were found with the four mutants; A486Y representing a 150-fold improvement over the wild type. A486, L490 and Y407 are on an alpha-helix that lines the dNTP binding groove, but the side chains of the three amino acids point away from this groove; Q472 is in a loop that connects this alpha-helix to a second long helix. None of the four amino acids can contact the dNTP directly. Therefore, the increased selectivity for ddNTPs is likely to arise from two factors: 1) Small overall changes in conformation that subtly alter the nucleotide triphosphate binding site such that ddNTPs become favoured; 2) interference with a conformational change that may be critical both for the polymerisation step and discrimination between different nucleotide triphosphates.

The present invention relates to a novel peptide and use thereof, more particularly to an isolated peptide comprising 21-41 contiguous amino acids selected from the amino acid sequence of SEQ ID NO: 1 or the amino acid sequence having at least 90% sequence homology to the amino acid sequence of SEQ ID NO: 1 and methods for promoting fibroblast proliferation and wound healing, which comprise administering to a subject in need thereof an effective amount of the peptide.

Specific anti-heparanase antibodies which bind specifically to heparanase having sequence homology to human heparanase, which can be used to treat and diagnose conditions associated with heparanase catalytic activity, for purification of heparanase, and for drug development in heparanase associated conditions are disclosed.

A search of the public human genome database identified a human EST, GenBank accession number AW293249, which has high homology to known pufferfish urocortin sequences. The full length sequence was amplified from human genomic DNA and sequenced. Sequence homology comparisons of the novel sequence with human urocortin I and urocortin II revealed that the sequence encoded a novel human urocortin, which was designated urocortin III (UcnIII). While urocortin III does not have high affinity for either CRF-R1 or CRF-R2, the affinity for CRF-R2 is greater than the affinity for CRF-R1. Urocortin III is capable stimulating cyclic AMP production in cells expressing CRF-R2α or β. Thus, the affinity is high enough that urocortin III could act as a native agonist of CRF-R2. However, it is also likely that urocortin III is a stronger agonist of a yet to be identified receptor.

A novel peptide sequence having the general formula AB wherein each of A and B represent a chain of amino acid residues and wherein said A chain is capable of binding with a major histocompatibility complex on an antigen presenting cell, and wherein said B chain is capable of binding with a Signal-2 receptor on an antigen presenting cell. Preferred forms of the peptide sequence further include an X chain positioned intermediate the A chain and the B chain. Moreover, preferred forms include an A chain which has at least about 10% sequence homology with a Signal-1 moiety, or is a peptidomimetic of a Signal-1 moiety, said B chain has at least 10% sequence homology with a Signal-2 receptor moiety, or is a peptidomimetic of a Signal-2 receptor moiety, and wherein the X chain has at least one amino acid residue, or is a peptidomimetic of that amino acid residue. Advantageously, the novel peptide sequence is capable of shifting a type-1 immune response to a type-2 immune response or from a type-2 immune response to a type-1 immune response.

The invention discloses a bactrian camel heavy-chain (HC) variable-domain antibody resisting a porcine circovirus 2 as well as a preparation method and an application thereof, and belongs to the field of a biotechnology. A PCV2 (Porcine Circovirus Virus) inactivated vaccine immunized bactrian camel is firstly utilized and a phage display technology is utilized to establish a PCV2 immune VHH antibody base; and a high-specificity variable domain antibody of heavy chains of HCAbs (VHH) which has a good affinity with the PCV, particularly a PCV2 virus antigen; and the antibody disclosed by the invention has an amino acid sequence shown as SEQ (sequence) ID NO.1 or an amino acid sequence which is shown as SEQ ID NO.2 and has the sequence isogeny being more than 95%. The PCV2 heavy-chain variable-domain antibody disclosed by the invention has the very important meanings on researching porcine circovirus, particularly researching a porcine circovirus 2-type infection mechanism and establishing rapid antigen detection with high sensitivity and specificity or diagnosing a reagent.

Expressed Sequence Tags (ESTs) isolated from maize are disclosed. The ESTs provide a unique molecular tool for the targeting and isolation of novel genes for plant protection and improvement. The disclosed ESTs have utility in the development of new strategies for understanding critical plant developmental and metabolic pathways. The disclosed ESTs have particular utility in isolating genes and promoters, identifying and mapping the genes involved in developmental and metabolic pathways, and determining gene function. Sequence homology analyses using the ESTs provided in the present invention, will result in more efficient gene screening for desirable agronomic traits. An expanding database of these select pieces of the plant genomics puzzle will quickly expand the knowledge necessary for subsequent functional validation, a key limitation in current plant biotechnology efforts.

An alcohol dehydrogenase (ADH) from hyperthermophilic archaeon Thermococcus guaymasensis was purified to homogeneity and was found to be a homotetramer with a subunit size of 40±1 kDa. The gene encoding the enzyme was cloned and sequenced, and found to have significant sequence homology to known zinc-containing ADHs and L-threonine dehydrogenases with both binding motifs of catalytic zinc and NADP⁺. The wild-type enzyme is a primary-secondary ADH that exhibits a substrate preference for secondary alcohols and corresponding ketones, and exhibits unusual stereoselectivity. The wild-type enzyme was found to have outstanding thermostability, demonstrating 60% activity after incubation at 80° C. for 40 hours. Site-directed mutagenesis was used to substitute the cyteine residue at position 56 with a serine, to provide the TgADH(C56S) mutant. In the assays that we carried out, we found virtually no difference in enzyme activity and oxygen-sensitivity between the mutant TgADH (C56S) and wild type TgADH.

The present invention relates to a computation method for detecting remote sequence homologies. The method comprises the following steps: First, a training sequence set of positive and negative examples each having a corresponding binary label is provided together with a database query sequence set (typically large) of unlabeled sequences. Second, each sequence in the training set is converted into a fixed-length vector of real values by computing pairwise sequence similarity scores with respect to the vectorization set to obtain vectorized training sequences each having corresponding binary labels. Third, the vectorized training sequences (along with their binary labels) are used to train a discriminative classification algorithm to obtain a trained discriminative classification algorithm. Fourth, the the database of unlabeled sequences are converted into pairwise score vectors, using the vectorization set to obtain vectorized database sequences. Finally, each vectorized database query sequence is presented to the trained discriminative classification algorithm to produce predicted classifications for the database query sequence.

Disclosed are: a composition for organ, tissue or cell transplantation, containing, as an active ingredient, a peptide comprising the amino acid sequence of SEQ ID NO: 1, a peptide having at least 80% sequence homology with the amino acid sequence, or a peptide which is a fragment thereof; a kit comprising the composition; or a method using the composition. By using the composition, the kit, or the method, the viability and/or function of an organ, tissue, or cell after transplantation are strengthened and an organ, tissue or cell isolated from a living body is preserved temporarily without damage.

The present invention provides nucleic acid and amino acid sequences useful as the immunogenic portion of vaccines or immunogenic compositions effective for lessening the severity of the clinical symptoms associated with Lawsonia intracellularis infection or conferring protective immunity to an animal susceptible to such infection. Preferred amino acid sequences are selected from the group consisting of 1) a polypeptide comprising a sequence selected from the group consisting of SEQ ID Nos.: 1-455, SEQ ID No 466, or the polypeptide encoded by SEQ ID No: 456, SEQ ID No: 457 or SEQ ID No: 466; 2) any polypeptide that has at least 85% sequence homology, more preferably at least about 90% sequence homology, still more preferably at least about 95% sequence homology, even more preferably at least about 97% sequence homology, still even more preferably at least about 98% sequence homology, and even more preferably at least about 99% sequence homology to the polypeptide of 1); 3) any immunogenic portion of the polypeptides of 1) and/or 2) 4) the immunogenic portion of 3), comprising at least 300, 290, 280, 270, 260, 250, 240, 230, 220, 210, 200, 190, 180, 170, 160, 150, 140, 130, 120, 110, 100, 90, 80, 70, 60, 50, 45, 40, 35, 30, 25, 20, 18, 15, 13, 10, or most preferably 9 contiguous amino acids included in the sequences of SEQ ID No: 1-455, SEQ ID No: 456, or the amino acid sequence encoded by SEQ ID No: 457 or SEQ ID No: 466; and/or 5) a polypeptide that is encoded by a DNA that codes for a peptide comprising the sequence of SEQ ID No: 1-455 or SEQ ID No: 466. Thus, the nucleic acid sequences encoding such proteins, or the proteins themselves are included in vaccine compositions, together with veterinary-acceptable carrier and administered to an animal in need thereof.

The invention relates to improved transaminase, an encoding gene and application thereof in preparation of (R)-3-aminobutanol. The improved transaminase is higher than wild transaminase in enzymatic activity. The amino acid sequence of the wild transaminase is shown in SEQ ID No.2 and is rooted in Aspergillus terreus NIH2624. The improved transaminase comprises an amino acid sequence with at least 95% sequence homology as the amino acid sequence shown in the SEQ ID No.2, and the 215th bit corresponding to the amino acid sequence shown in SEQ ID No.2 is a proline residue. The reaction conditions are mild when the improved transaminase is used for preparing (R)-3-aminobutanol, the product is high in chirality purity and yield, the concentration of a substrate reaches up to 50 g/L, and the good industrial application prospect is achieved.

The invention discloses a recombinant human-like collagen protein-human original cell growth factor fusion protein and a preparation method and application thereof. The prepared fusion protein is provided with a special fibrous structure and good biological tissue compatibility, and can promote proliferation and differentiation of epidermis cells, endothelial cells and fibroblast cells. The preparation method comprises the following steps: obtaining encoded DNA sequence of the fusion protein, reconstructing and recombining fusion protein expressed by an expression vectors in escherichia coli, pichia pastoris or chinese hamster ovary cells. The fusion protein comprises a first zone and a second zone, wherein the first zone has at least 85% of sequence homology with human collagen protein and has the function of the human collagen protein, and the second zone has at least 85% of human original cell growth factor and has the function of the human original cell growth factor; connecting peptide is arranged between the first zone and the second zone; the general formula of the connecting peptide is (GGGS)n; preferably, the amino acid sequence of the fusion protein is SEQ ID NO. 15.

Expressed Sequence Tags (ESTs) isolated from cotton are disclosed. The ESTs provide a unique molecular tool for the targeting and isolation of novel genes for plant protection and improvement. The disclosed ESTs have utility in the development of new strategies for understanding critical plant developmental and metabolic pathways. The disclosed ESTs have particular utility in isolating genes and promoters, identifying and mapping the genes involved in developmental and metabolic pathways, and determining gene function. Sequence homology analyses using the ESTs provided in the present invention, will result in more efficient gene screening for desirable agronomic traits. An expanding database of these select pieces of the plant genomics puzzle will quickly expand the knowledge necessary for subsequent functional validation, a key limitation in current plant biotechnology efforts.

The present invention relates to methods and apparatus for rapid assessment of genomic sequences using the difference set model. The invention provides methods to determine the presence and identity of similarities and differences in genomic sequences. In particular, the invention provides methods and apparatus to assess homology, the presence and identity of insertion and deletion segments and the presence and identity of single nucleotide polymorphisms in genomic sequences.

Expressed Sequence Tags (ESTs) isolated from soybean are disclosed. The ESTs provide a unique molecular tool for the targeting and isolation of novel genes for plant protection and improvement. The disclosed ESTs have utility in the development of new strategies for understanding critical plant developmental and metabolic pathways. The disclosed ESTs have particular utility in isolating genes and promoters, identifying and mapping the genes involved in developmental and metabolic pathways, and determining gene function. Sequence homology analyses using the ESTs provided in the present invention, will result in more efficient gene screening for desirable agronomic traits. An expanding database of these select pieces of the plant genomics puzzle will quickly expand the knowledge necessary for subsequent functional validation, a key limitation in current plant biotechnology efforts.

The invention relates to the field of medicine, and discloses a high-throughput screening method for active polypeptides based on tandem mass spectrometry and molecular docking. The invention uses modern biochemical technology to extract and prepare mixed polypeptides from marine molluscs, fish and other animals. After preliminary activity separation, the active site/component group is determined, and the amino acid sequence of all polypeptides in the active site/component group is identified by LC-MS/MS method. In the molecular docking software, all polypeptide sequences are homologously modeled, and then imported Molecular docking software docks with the target protein, analyzes the binding rate of the polypeptide and the target protein, and evaluates its inhibitory/activating activity, and screens the confirmed active polypeptide through solid-phase synthesis combined with in vitro activity evaluation to verify the accuracy of the screening. The invention has the advantages of fast and efficient search for marine active polypeptides, strong operability and important application value.