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Katalogové číslo: (PRSI91-004)
Dodavatel: ProSci Inc.
Popis: At least 23 different variants of IFN- alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN- alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN- alpha subtypes differ in their sequences by only one or two positions. Naturally occurring variants also include proteins that are truncated by 10 amino acids at the carboxyl-terminal end.
Měrná jednotka: 1 * 50 µG


Katalogové číslo: (PRSI91-097)
Dodavatel: ProSci Inc.
Popis: Chemokine (C C Motif) Ligand 26 (CCL26) is a novel small cytokine belonging to the CC chemokine family, which involved in immunoregulatory and inflammatory processes. CCL26 is expressed constitutively in thymus, but only transiently in phytohemagglutinin-stimulated peripheral blood mononuclear cells. It specifically binds and induces chemotaxis in T cells and elicits its effects by interacting with the chemokine receptor CCR4. Eotaxin-3/CCL26, along with Eotaxin-1 and Eotaxin-2, selectively activates the CC chemokine receptor 3 (CCR3). The Eotaxin-3-CCR3 interaction may play an important role in allergic diseases such as atopic dermatitis and bronchial asthma. The full-length cDNA for Eotaxin-3 encodes a protein of 94 amino acids with a putative signal peptide of either 23 or 26 amino acid residues. Both the 71 and 68 amino acid residue variants of recombinant Eotaxin-3 demonstrate equal potency in inducing chemotaxis of a human CCR3-transfected cell line. Unlike most other CC chemokines, Eotaxin-3 maps to human chromosome 7q11.2, within 40 kilobases of the Eotaxin-2 loci. Eotaxin-3 and Eotaxin-2 are unique in that they are the only chemokines identified to date that map to chromosome 7.
Měrná jednotka: 1 * 50 µG


Dodavatel: Thermo Fisher Scientific
Popis: Bisakrylamid 99+% for biochemistry, for electrophoresis
Katalogové číslo: (PRSI91-018)
Dodavatel: ProSci Inc.
Popis: At least 23 different variants of IFN- alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN- alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN- alpha subtypes only differ in their sequences by one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.
Měrná jednotka: 1 * 50 µG


Katalogové číslo: (PRSI91-096)
Dodavatel: ProSci Inc.
Popis: Chemokine Ligand 26 protein (CCL26) is a novel small cytokine belonging to the CC chemokine family which is involved in immunoregulatory and inflammatory processes. CCL26 is constitutively expressed in thymus, but only transiently expressed in phytohemagglutinin-stimulated peripheral blood mononuclear cells. It specifically binds and induces chemotaxis in T cells and elicits its effects by interacting with the chemokine receptor CCR4. CCL26, along with Eotaxin-1 and Eotaxin-2, selectively activates the CC chemokine receptor 3 (CCR3). The Eotaxin-3-CCR3 interaction may play an important role in allergic diseases such as atopic dermatitis and bronchial asthma. The full-length cDNA for CCL26 encodes a protein of 94 amino acids with a putative signal peptide of either 23 or 26 amino acid residues. Both the 71 and 68 amino acid residue variants of recombinant CCL26 demonstrate equal potency in inducing chemotaxis of a human CCR3-transfected cell line. Unlike most other CC chemokines, CCL26 maps to human chromosome 7q11.2, within 40 kilobases of the Eotaxin-2 loci. CCL26 and Eotaxin-2 are unique in that they are the only chemokines identified to date that map to chromosome 7.
Měrná jednotka: 1 * 50 µG


Dodavatel: ENZO LIFE SCIENCES
Popis: The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate-binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

Dodavatel: ENZO LIFE SCIENCES
Popis: The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate binding domain of Hsd70 cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

Dodavatel: Merck
Popis: N-ɑ-Fmoc-N-ε-boc-L-lysine ≥98.0% (by HPLC), Sigma-Aldrich®

Katalogové číslo: (J60461.AP)
Dodavatel: Thermo Fisher Scientific
Popis: 3,3',5,5'-Tetramethylbenzidin solution, standard sensitivity ready-to-use, precipitating
Měrná jednotka: 1 * 500 mL

Katalogové číslo: (1.08475.1000)
Dodavatel: Merck
Popis: 3,3',5,5'-Tetramethylbenzidin solution for the detection of chlorine, Supelco®
Měrná jednotka: 1 * 1 L

Katalogové číslo: (1.08622.0001)
Dodavatel: Merck
Popis: 3,3',5,5'-Tetramethylbenzidin ≥99%, GR for analysis, Supelco®
Měrná jednotka: 1 * 1 g

Dodavatel: Merck
Popis: 3,3',5,5'-Tetramethylbenzidin substrate 1 mg, tablets, Sigma-Aldrich®

Dodavatel: Merck
Popis: 3,3',5,5'-Tetramethylbenzidin ≥98% (by TLC), Sigma-Aldrich®

Dodavatel: MP Biomedicals
Popis: Storage: Store at room temperature (15-30 °C)
L-Lysine monohydrochloride is widely used as nutritional supplements in food and beverage industries. It can also be used in animal feed as source of L-Lysine. L-Lysine Monohydrochloride can be used in a wide variety of industries including: food production, beverage, pharmaceutical, agriculture/animal feed, and various other industries.
L-Lysine monohydrochloride is a key amino acid in calcium absorption.

Dodavatel: ENZO LIFE SCIENCES
Popis: The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate-binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

Katalogové číslo: (ENZOADISPA8136D)
Dodavatel: ENZO LIFE SCIENCES
Popis: The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.
Měrná jednotka: 1 * 50 µG


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