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Masterflex+Single-use
Numéro de catalogue:
(BOSSBS-5175R-CY7)
Fournisseur:
Bioss
Description:
Vital cellular functions such as cell proliferation and signal transduction are regulated in part by the balance between the activities of protein tyrosine kinases (PTK) and protein tyrosine phosphatases (PTPs). The protein contains a 121 residue extracellular domain, a single transmembrane segment, and 2 tandem intracytoplasmic catalytic domains. The PTP alpha protein is ubiquitously expressed and may play a fundamental role in the physiology of all cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5175R-CY5)
Fournisseur:
Bioss
Description:
Vital cellular functions such as cell proliferation and signal transduction are regulated in part by the balance between the activities of protein tyrosine kinases (PTK) and protein tyrosine phosphatases (PTPs). The protein contains a 121 residue extracellular domain, a single transmembrane segment, and 2 tandem intracytoplasmic catalytic domains. The PTP alpha protein is ubiquitously expressed and may play a fundamental role in the physiology of all cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8525R-CY7)
Fournisseur:
Bioss
Description:
Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5450R)
Fournisseur:
Bioss
Description:
ICAM proteins are ligands for the leukocyte adhesion LFA-1 protein (Integrin alpha-L/beta-2). Subcellular Located at Membrane; single-pass type I membrane protein. Tissue Specificified Expressed at low level on a subpopulation of lymphocytes, macrophages, and endothelial cells, but is strongly induced on these cells, and on fibroblasts and epithelial cells. [PTM] Monoubiquitinated, which is promoted by MARCH9 and leads to endocytosis (By similarity). It belongs to the immunoglobulin superfamily. ICAM family.
UOM:
1 * 100 µl
Numéro de catalogue:
(ENZOADISAB300J)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Immunoglobulin G (IgG) is an immunoglobulin monomer consisting of two (gamma) heavy chains and two light chains. Each IgG molecule contains two antigen binding domains and a single effector (Fc) domain. Assay designs offers isotyping kits and antibodies in a variety of formats for the detection of human, mouse, rabbit, rat, sheep, and goat IgG.
UOM:
1 * 1 mL
New Product
Numéro de catalogue:
(BOSSBS-5453R-CY3)
Fournisseur:
Bioss
Description:
The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.
UOM:
1 * 100 µl
Numéro de catalogue:
(216-4345)
Fournisseur:
MULTIROIR
Description:
Tiroir empilable en polystyrène idéal pour l'organisation et le stockage de composants de laboratoire, de consommables et de matériaux divers.
UOM:
1 * 1 ST
Numéro de catalogue:
(BOSSBS-6634R-A680)
Fournisseur:
Bioss
Description:
Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognises a wide spectrum of damaged DNA characterised by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognise and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. <i>in vitro</i>, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0290R)
Fournisseur:
Bioss
Description:
The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0290R-A488)
Fournisseur:
Bioss
Description:
The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-0290R-A680)
Fournisseur:
Bioss
Description:
The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9233R)
Fournisseur:
Bioss
Description:
The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF180 (ring finger protein 180), also known as Rines, is a 592 single-pass membrane protein that contains a single RING-type zinc finger. Expressed as three alternatively spliced isoforms, RNF180 is well conserved among vertebrates. RNF180 is expressed in brain, kidney, testis and uterus and localizes to the endoplasmic reticulum. RNF180 is an E3 ubiquitin ligase involved in the ubiquitin-proteasome pathway. RNF180 is encoded by a gene located on human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm, or of chromosome 5 altogether, is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5453R-FITC)
Fournisseur:
Bioss
Description:
The human insulin receptor is a heterotetrameric membrane glycoprotein consisting of disulfide linked subunits in a beta-alpha-alpha-beta configuration. The beta subunit (95 kDa) possesses a single transmembrane domain, whereas the alpha subunit (135 kDa) is completely extracellular. The insulin receptor exhibits receptor tyrosine kinase (RTK) activity. RTKs are single pass transmembrane receptors that possess intrinsic cytoplasmic enzymatic activity, catalyzing the transfer of the gamma phosphate of ATP to tyrosine residues in protein substrates. RTKs are essential components of signal transduction pathways that affect cell proliferation, differentiation, migration and metabolism.Included in this large protein family are the insulin receptor and the receptors for growth factors such as epidermal growth factor, fibroblast growth factor and vascular endothelial growth factor. Receptor activation occurs through ligand binding, which facilitates receptor dimerization and autophosphorylation of specific tyrosine residues in the cytoplasmic portion. The interaction of insulin with the alpha subunit of the insulin receptor activates the protein tyrosine kinase of the beta subunit, which then undergoes an autophosphorylation that increases its tyrosine kinase activity. Three adapter proteins, IRS1, IRS2 and Shc, become phosphorylated on tyrosine residues following insulin receptor activation. These three phosphorylated proteins then interact with SH2 domain containing signaling proteins.
UOM:
1 * 100 µl
Fournisseur:
MIELE
Description:
The PLW 7111 SlimLine laboratory washers offer a comprehensive and systematic solution for analytically pure reprocessing of laboratory glassware.
Numéro de catalogue:
(BOSSBS-11477R-A680)
Fournisseur:
Bioss
Description:
Semaphorins are a family of cell surface and secreted proteins that are conserved from insects to humans. Members of this family of proteins are approximately 750 amino acids in length (including signal sequences) and are defined by a conserved extracellular semaphorin domain of approximately 500 amino acids containing 14-16 cysteines, blocks of conserved sequences and no obvious repeats. The transmembrane semaphorins are characterised by an additional 80 amino acid transmembrane domain and an 80-110 amino acid cytoplasmic domain. Secreted and cell-bound semaphorins chemically attract and repel the growth of neural axons, guiding the development of intricate networks of neural tissue. SEMA4B (semaphorin-4B), also known as SemC or SEMAC, is an 832 amino acid single-pass type I membrane protein that belongs to the semaphorin family and exists as two alternatively spliced isoforms. Containing one Ig-like C2-type (immunoglobulin-like) domain, a PSI domain and a single sema domain, SEMA4B is encoded by a gene located on human chromosome 15.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11477R-CY7)
Fournisseur:
Bioss
Description:
Semaphorins are a family of cell surface and secreted proteins that are conserved from insects to humans. Members of this family of proteins are approximately 750 amino acids in length (including signal sequences) and are defined by a conserved extracellular “semaphorin†domain of approximately 500 amino acids containing 14-16 cysteines, blocks of conserved sequences and no obvious repeats. The transmembrane semaphorins are characterized by an additional 80 amino acid transmembrane domain and an 80-110 amino acid cytoplasmic domain. Secreted and cell-bound semaphorins chemically attract and repel the growth of neural axons, guiding the development of intricate networks of neural tissue. SEMA4B (semaphorin-4B), also known as SemC or SEMAC, is an 832 amino acid single-pass type I membrane protein that belongs to the semaphorin family and exists as two alternatively spliced isoforms. Containing one Ig-like C2-type (immunoglobulin-like) domain, a PSI domain and a single sema domain, SEMA4B is encoded by a gene located on human chromosome 15.
UOM:
1 * 100 µl
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