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3,3',5,5'-Tetramethylbenzidine (TMB)

Supplier: Roth Carl
Description: 3,3',5,5'-Tetramethylbenzidine (TMB)

Image Unavailable-PRSI91-018

Human recombinant IFN alpha 2a (from E. coli)

Catalog Number: (PRSI91-018)
Supplier: ProSci Inc.
Description: 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.
UOM: 1 * 50 µG
Image Unavailable-PRSI91-097

Human Recombinant CCL26 (from E. coli)

Catalog Number: (PRSI91-097)
Supplier: ProSci Inc.
Description: 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.
UOM: 1 * 50 µG
Image Unavailable-MOLEM88604857

3,3',5,5'-Tetramethylbenzidine (TMB)

Catalog Number: (MOLEM88604857)
Supplier: Molekula
Description: 3,3',5,5'-Tetramethylbenzidine (TMB)
UOM: 1 * 5 g

Market Source Item This is a MarketSource item. Additional charges may apply

Image Unavailable-PRSI91-096

Human Recombinant CCL26 (from E. coli)

Catalog Number: (PRSI91-096)
Supplier: ProSci Inc.
Description: 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.
UOM: 1 * 50 µG
Image Unavailable-ICNA0219469780

L(+)-Lysine monohydrochloride

Supplier: MP Biomedicals
Description: 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.

Image Unavailable-ENZOADISPA819F

Anti-HSPA8 Rabbit Polyclonal Antibody

Supplier: ENZO LIFE SCIENCES
Description: 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.

Image Unavailable-PRSI92-517

Mouse recombinant IL1RA (from E. coli)

Catalog Number: (PRSI92-517)
Supplier: ProSci Inc.
Description: Interleukin-1 receptor antagonist protein (Il1rn), also known as IL-1ra, IRAP or IL1 inhibitor, is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1 alpha (IL1A) and interleukin 1 beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. The mouse Il1rn gene encodes a 178 amino acids (aa) protein with a 26 aa signal peptide. Mouse Il1rn protein shares 26% and 19% identity with its homologues IL-1 beta and IL-1 alpha, respectively. Il1rn can Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signalling, but has no interleukin-1 like activity. Recently, an recombinant human Il1rn protein is used in the treatment of rheumatoid arthritis, an autoimmune disease in which IL-1 plays a key role.
UOM: 1 * 50 µG
Image Unavailable-ENZOADISPA8131F

Anti-HSP70 Mouse Monoclonal Antibody

Supplier: ENZO LIFE SCIENCES
Description: 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.

Image Unavailable-ENZOADISPA8132F

Anti-HSP70 Mouse Monoclonal Antibody

Supplier: ENZO LIFE SCIENCES
Description: 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.

Image Unavailable-ENZOADISPA8133D

Anti-HSP70 Mouse Monoclonal Antibody

Supplier: ENZO LIFE SCIENCES
Description: 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.

Image Unavailable-ENZOADISPA8136D

Anti-HSP70 Mouse Monoclonal Antibody

Catalog Number: (ENZOADISPA8136D)
Supplier: ENZO LIFE SCIENCES
Description: 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.
UOM: 1 * 50 µG
Image Unavailable-BOSSBS-1135R-A680

Anti-SRC Rabbit Polyclonal Antibody (Alexa Fluor® 680)

Catalog Number: (BOSSBS-1135R-A680)
Supplier: Bioss
Description: c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labelling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr --> Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
UOM: 1 * 100 µl
Image Unavailable-J60461.AP

3,3',5,5'-Tetramethylbenzidine (TMB) solution, standard sensitivity ready-to-use, precipitating

Catalog Number: (J60461.AP)
Supplier: Thermo Fisher Scientific
Description: 3,3',5,5'-Tetramethylbenzidine (TMB) solution, standard sensitivity ready-to-use, precipitating
UOM: 1 * 500 mL

MSDS Certificates


Image Unavailable-613548-100

3,3',5,5'-Tetramethylbenzidine (TMB), insoluble, Calbiochem®, Sigma-Aldrich®

Catalog Number: (613548-100)
Supplier: Merck Millipore (Oncogene)
Description: Peroxidase substrate that produces a stable, insoluble, aquamarine blue precipitate at reaction site with little or no background.
UOM: 1 * 100 mL
Image Unavailable-BOSSBS-1135R-CY5

Anti-SRC Rabbit Polyclonal Antibody (Cy5®)

Catalog Number: (BOSSBS-1135R-CY5)
Supplier: Bioss
Description: c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
UOM: 1 * 100 µl
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
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