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2,6-Dimethoxy-3-nitropyridine


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Supplier:  Adipogen
Description:   A sensitive reagent for measuring the free sulfhydryl content in proteins, peptides, and tissues. Used to characterize reactive thiol groups and photometric determination of thiols and for measuring low-molecular mass thiols such as glutathione in both pure solutions and biological samples, such as blood. It can also measure the number of thiol groups on proteins. Through reaction with aliphatic thiol groups a mixed disulfide of protein thiol and one mole of 2-nitro-5-thiobenzoate per mole of protein sulfhydryl group is being formed. DTNB has little absorbance. Reaction with -SH groups on proteins (from any solvent accessible Cys) under mild alkaline conditions (pH 7-8) produces the 2-nitro-5-thiobenzoate anion, which gives an intense yellow color with an absorption maximum at 409.5nm (Extinction coefficient: 14150 M-1*cm-1). Sensitive to various buffer ions, therefore, the extinction coefficient used to calculate the number of sulfhydryl groups must be matched to the reaction conditions. In case the thiol groups are in disulfide bonds, they must be reduced under anaerobic conditions prior to reaction with DTNB.
Catalog Number: (10424-770)

Supplier:  Bioss
Description:   ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.
Supplier:  Bioss
Description:   ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier:  VWR International
Description:   Wide variety of VWR® student dissection kits that suit educational needs.
Supplier:  Bioss
Description:   Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
Catalog Number: (102552-890)

Supplier:  BioVendor
Description:   S100A11 (S100C; calgizzarin) was first isolated from chicken gizzard smooth muscle. Human homologue was later identified in human colorectal cancer cells and in colorectal normal mucosa, with much higher expression in the cancer cells. S100A11 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. The polypeptide chain consists of 105 amino acid residues giving molecular weight of unmodified monomeric protein 11.74 kDa. Disulphide bridge linking two monomers in the dimer via Cys-11 residues was found in its structure. The protein can be phosphorylated on some residues from which at least phosphorylation on Thr-10 causes significant structural changes. S100A11 binds to annexins A1 and A2, the DNA-dependent ATPase Rad54B, p53 and RAGE. It was proposed that up-regulated chondrocyte expression of S100A11 (as RAGE ligand) in OA cartilage and RAGE signaling through the p38 MAPK pathway promote inflammation-associated chondrocyte hypertrophy. RAGE signaling mediated by S100A11 thereby might have the potential to contribute to the progression of OA. S100A11 has also been shown to be secreted and to exert RAGE dependent signaling in human keratinocytes. S100A11 was found in many different human both normal and cancer tissues. S100A11 appears to play distinct roles depending on the tumour involved. In bladder carcinoma or renal carcinoma expression is related to tumour suppression however in prostate cancer, breast and pancreatic cancer S100A11 is thought to be a tumour promoter. S100A11 has been also indicated as one of potential biomarkers of infective endocarditis.
Supplier:  AMBEED, INC
Description:   (S)-3-((tert-Butoxycarbonyl)amino)-3-(3-methoxyphenyl)propanoic acid, Purity: 98%, CAS Number: 499995-77-6, Appearance: White to off-white powder or crystals, Storage: Keep in dark place, Inert atmosphere, Room temperature, Size: 100MG
Supplier:  Biotium
Description:   This MAb recognizes a protein of 134 kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This MAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.
Supplier:  Bioss
Description:   ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.

Supplier:  Bioss
Description:   ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.
Supplier:  Bioss
Description:   Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.

Supplier:  Biotium
Description:   This MAb recognizes a protein of 134 kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This MAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.

Supplier:  VWR International
Description:   Wide variety of VWR® student dissection kits that suit educational needs.

Supplier:  Novus Biologicals
Description:   The Bax Antibody (SPM336) - IHC-Prediluted from Novus Biologicals is a mouse monoclonal antibody to Bax. This antibody reacts with human, primate, mouse (negative), rat (negative). The Bax Antibody (SPM336) - IHC-Prediluted has been validated for the following applications: Immunohistochemistry-Paraffin.

Supplier:  Bioss
Description:   ADAM11 was first described as MDC (Metalloproteinase-like disintergin-like cysteine-rich protein) from analysis of human brain libraries, in search of brain-specific proteins. Two splice variants with different carboxyterminal ends were described. The message was found only in the brain in this publication. Another group identified ADAM11 in the human brain, where ADAM11 was thought to be involved in cell migration and spatial patterning. ADAM11 was mapped to 17q21.3, a region of interest for breast cancer, and mutations in ADAM11 are associated with some breast cancers. Retinoic acid caused a doubling in ADAM11 message levels over 24 hours in NT2/D1 cells, a human embryonic carcinoma cell line. ADAM11 null mutant mice have deficits in spatial learning and motor coordination, although they did have normal cell migration and differentiation during development. ADAM11 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full-length ADAM11 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a spacer region, then the transmembrane domain and a short cytoplasmic domain.
Supplier:  Biotium
Description:   This MAb recognizes a protein of 134 kDa, which binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils). Fucosylation is essential for binding to E-selectin. It contains sialic acid residues and 16 Cys-rich GLG1 repeats. This MAb can be used to stain the Golgi complex in cell or tissue preparations and can be used as a Golgi marker in subcellular fractions. It produces a diffuse staining pattern of the Golgi zone in normal and malignant cells. This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. The Golgi apparatus is an organelle present in all eukaryotic cells that forms a part of the endomembrane system. The primary function of the Golgi apparatus is to process and package macromolecules synthesized by the cell for exocytosis or use within the cell. The Golgi is made up of a stack of flattened, membrane-bound sacs known as cisternae, with three functional regions: the cis face, medial region and trans face. Each region consists of various enzymes that selectively modify the macromolecules passing though them, depending on where they are destined to reside. Several spherical vesicles that have budded off of the Golgi are present surrounding the main cisternae. The Golgi tends to be more pronounced and numerous in cells that make and secrete many substances such as plasma B cells.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®568 is a red fluorescent dye (Ex/Em 562/583 nm) with superior brightness and photostability. It also is compatible with super-resolution imaging by STORM and TIRF.
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