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Numéro de catalogue: (BOSSBS-0397R-A750)

Fournisseur:  Bioss
Description:   May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin-dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   May play a key role in diverse functions ascribed to CD81 and CD9 such as oocytes fertilization or hepatitis C virus function. May regulate proliferation and differentiation of keratinocytes. May be a negative regulator of cell motility: suppresses T-cell mobility coordinately with CD81, associates with CD82 to suppress prostate cancer cell migration, regulates epidermoid cell reaggregation and motility on laminin-5 with CD9 and CD81 as key linkers. May also play a role on integrin-dependent morphology and motility functions. May participate in the regulation of neurite outgrowth and maintenance of the neural network in the adult brain.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration.Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration.Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-6980R-A750)

Fournisseur:  Bioss
Description:   The type II cAMP-protein kinase (PKA) is a multifunctional kinase with a broad range of substrates (1). Specificity of PKA signaling is thought to be mediated by the compartmentalisation of the kinase to specific sites within the cell. To maintain this specific localisation, the R subunit (RII) of PKA interacts with specific RII-anchoring proteins. This family of proteins has been designated A-kinase anchoring proteins (AKAP) (1-3). Members of this family, including MAP2 (microtubule-associated protein 2), neuronally expressed AKAP 79 and AKAP 150, and the DNA binding AKAP 95, display differential tissue specificity and localisation (4-6). Evidence suggests that AKAP 79 and AKAP 150 are both capable of anchoring PKA to postsynaptic densities (PSD), which are a network of proteins located on the internal surfaces of excitatory synapses.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-6980R-A680)

Fournisseur:  Bioss
Description:   The type II cAMP-protein kinase (PKA) is a multifunctional kinase with a broad range of substrates (1). Specificity of PKA signaling is thought to be mediated by the compartmentalisation of the kinase to specific sites within the cell. To maintain this specific localisation, the R subunit (RII) of PKA interacts with specific RII-anchoring proteins. This family of proteins has been designated A-kinase anchoring proteins (AKAP) (1-3). Members of this family, including MAP2 (microtubule-associated protein 2), neuronally expressed AKAP 79 and AKAP 150, and the DNA binding AKAP 95, display differential tissue specificity and localisation (4-6). Evidence suggests that AKAP 79 and AKAP 150 are both capable of anchoring PKA to postsynaptic densities (PSD), which are a network of proteins located on the internal surfaces of excitatory synapses.
UOM:  1 * 100 µl
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