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Single-use+Temperature+Sensor
Numéro de catalogue:
(BOSSBS-13038R-CY3)
Fournisseur:
Bioss
Description:
Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13038R-A555)
Fournisseur:
Bioss
Description:
Dynamin I is a GTPase enzyme required for the retrieval of synaptic vesicles after exocytosis and functions in endocytosis by stimulating assembly of invaginating synaptic vesicles (1). Dynamin I is phosphorylated in nerve terminals exclusively in the cytosolic compartment and in vitro by protein kinase C (PKC) (2–5). The phosphorylation site in PKC-phosphorylated Dynamin I is a single site at Serine 795, which is located near a binding site for the SH3 domain of p85, the regulatory subunit of phosphatidylinositol 3-kinase (2–5). Dephosphorylation is required for synaptic vesicle retrieval, suggesting that phosphorylation affects the subcellular localization of Dynamin I (5). Mouse, rat and human Dynamin I are phosphorylated on serine residues, including Ser 778, by Cdk5, regulating PACSIN1 recruitment and enabling synaptic vesicle endocytosis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2672R-FITC)
Fournisseur:
Bioss
Description:
The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that appears to be a central coordinator for activation of many serine proteinases in immune/inflammatory cells. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor, and a residual portion of the propeptide acts as an intramolecular chaperone for the folding and stabilization of the mature enzyme. This enzyme requires chloride ions for activity and can degrade glucagon. Defects in the encoded protein have been shown to be a cause of Papillon-Lefevre syndrome, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2672R-CY5.5)
Fournisseur:
Bioss
Description:
The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that appears to be a central coordinator for activation of many serine proteinases in immune/inflammatory cells. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor, and a residual portion of the propeptide acts as an intramolecular chaperone for the folding and stabilization of the mature enzyme. This enzyme requires chloride ions for activity and can degrade glucagon. Defects in the encoded protein have been shown to be a cause of Papillon-Lefevre syndrome, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2672R-CY3)
Fournisseur:
Bioss
Description:
The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that appears to be a central coordinator for activation of many serine proteinases in immune/inflammatory cells. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor, and a residual portion of the propeptide acts as an intramolecular chaperone for the folding and stabilization of the mature enzyme. This enzyme requires chloride ions for activity and can degrade glucagon. Defects in the encoded protein have been shown to be a cause of Papillon-Lefevre syndrome, an autosomal recessive disorder characterized by palmoplantar keratosis and periodontitis. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11110R)
Fournisseur:
Bioss
Description:
Protocadherins are a large family of cadherin-like cell adhesion proteins that are involved in the establishment and maintenance of neuronal connections in the brain. There are three protocadherin gene clusters, designated alpha, beta and gamma, all of which contain multiple tandemly arranged genes. PCDH17 is a 1,159 amino acid single-pass type I membrane protein that contains six cadherin domains. Expressed as multiple alternatively spliced isoforms, PCDH17 is thought to function as a calcium-dependent cell adhesion protein that may play a role in establishing cell-cell connections within brain tissue. The gene encoding PCDH17 maps to human chromosome 13, which houses over 400 genes, such as BRCA2 and RB1, and comprises nearly 4% of the human genome.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-15458R-CY3)
Fournisseur:
Bioss
Description:
Hephaestin is a single-pass type I membrane protein that belongs to the multicopper oxidase family of proteins. Hephaestin, a copper-dependant ferroxidase protein, is crucial for iron exiting intestinal enterocytes into the circulation. It mediates the movement of iron across the basolateral membrane in conjunction with ferroportin 1. This is an important link between iron and copper metabolism in mammalian systems, as copper deficiency leads to reduced hephaestin and reduced iron absorption resulting in anemia. Hephaestin can bind six copper ions per monomer and is regulated by the homeobox transcription factor CDX2. Increased levels of iron leads to an increase in CDX2 expression and thus Hephaestin. Hephaestin is primarily detected in the intestine, but is also expressed in colon, breast, bone trabecural cells and fibroblasts.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12223R-CY3)
Fournisseur:
Bioss
Description:
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. ZNF786 (zinc finger protein 786) is a 782 amino acid protein that belongs to the Krüppel C2H2-type zinc-finger protein family and is thought to function in transcriptional regulation. Localizing to nucleus, ZNF786 contains sixteen C2H2-type zinc fingers, a single KRAB domain and is encoded by a gene that maps to human chromosome 7q36.1.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5342R-A750)
Fournisseur:
Bioss
Description:
This gene is a member of the Tyr protein kinase family and the epidermal growth factor receptor subfamily. It encodes a single-pass type I membrane protein with multiple cysteine rich domains, a transmembrane domain, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins and other factors and induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. Mutations in this gene have been associated with cancer. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterised.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-15482R-A350)
Fournisseur:
Bioss
Description:
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilise XPC. May protect XPC from proteasomal degradation. 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. In vitro, 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-15482R-CY3)
Fournisseur:
Bioss
Description:
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilise XPC. May protect XPC from proteasomal degradation. 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. In vitro, 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-15482R-HRP)
Fournisseur:
Bioss
Description:
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilise XPC. May protect XPC from proteasomal degradation. 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. In vitro, 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-1677R-A647)
Fournisseur:
Bioss
Description:
Efficiently joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5990R-FITC)
Fournisseur:
Bioss
Description:
This gene encodes a member of the ALEX family of proteins which may play a role in tumor suppression. The encoded protein contains a potential N-terminal transmembrane domain and a single Armadillo (arm) repeat. Other proteins containing the arm repeat are involved in development, maintenance of tissue integrity, and tumorigenesis. This gene is closely localized with other family members on the X chromosome. Three transcript variants encoding the same protein have been identified for this gene. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5990R-HRP)
Fournisseur:
Bioss
Description:
This gene encodes a member of the ALEX family of proteins which may play a role in tumor suppression. The encoded protein contains a potential N-terminal transmembrane domain and a single Armadillo (arm) repeat. Other proteins containing the arm repeat are involved in development, maintenance of tissue integrity, and tumorigenesis. This gene is closely localized with other family members on the X chromosome. Three transcript variants encoding the same protein have been identified for this gene. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1226R-CY7)
Fournisseur:
Bioss
Description:
The glycoprotein encoded by this gene is a cell surface antigen that is expressed in greater than 95% of human colon cancers. The open reading frame encodes a 319 amino acid polypeptide having a putative secretory signal sequence and 3 potential glycosylation sites. The predicted mature protein has a 213 amino acid extracellular region, a single transmembrane domain, and a 62 amino acid intracellular tail. The sequence of the extracellular region contains 2 domains characteristic of the CD2 subgroup of the immunoglobulin (Ig) superfamily.
UOM:
1 * 100 µl
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