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Masterflex+Single-use+Flow+Sensor
Fournisseur:
Biotium
Description:
This MAb recognizes a single chain, transmembrane, heavily glycosylated protein of 90-120 kDa, which is identified as CD34. Its expression is a hallmark for identifying pluripotent hematopoietic stem or progenitor cells. Its expression is gradually lost as lineage committed progenitors differentiate. CD34 is a marker of choice for staining blasts in acute myeloid leukemia. In addition, CD34 is expressed by soft tissue tumors, such as solitary fibrous tumor and gastrointestinal stromal tumor. Its expression is also found in vascular endothelium. Additionally, it appears that proliferating endothelial cells express this molecule more than the non-proliferating endothelial cells. Anti-CD34 labels > 85% of angiosarcoma and Kaposi's sarcoma, but with a lower specificity.
Fournisseur:
Biotium
Description:
This MAb recognizes a single chain, transmembrane, heavily glycosylated protein of 90-120 kDa, which is identified as CD34. Its expression is a hallmark for identifying pluripotent hematopoietic stem or progenitor cells. Its expression is gradually lost as lineage committed progenitors differentiate. CD34 is a marker of choice for staining blasts in acute myeloid leukemia. In addition, CD34 is expressed by soft tissue tumors, such as solitary fibrous tumor and gastrointestinal stromal tumor. Its expression is also found in vascular endothelium. Additionally, it appears that proliferating endothelial cells express this molecule more than the non-proliferating endothelial cells. Anti-CD34 labels > 85% of angiosarcoma and Kaposi's sarcoma, but with a lower specificity.
Fournisseur:
Biotium
Description:
This MAb recognizes a single chain, transmembrane, heavily glycosylated protein of 90-120 kDa, which is identified as CD34. Its expression is a hallmark for identifying pluripotent hematopoietic stem or progenitor cells. Its expression is gradually lost as lineage committed progenitors differentiate. CD34 is a marker of choice for staining blasts in acute myeloid leukemia. In addition, CD34 is expressed by soft tissue tumors, such as solitary fibrous tumor and gastrointestinal stromal tumor. Its expression is also found in vascular endothelium. Additionally, it appears that proliferating endothelial cells express this molecule more than the non-proliferating endothelial cells. Anti-CD34 labels > 85% of angiosarcoma and Kaposi's sarcoma, but with a lower specificity.
Fournisseur:
Biotium
Description:
Recognizes a protein of 104 kDa-110 kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy.
Numéro de catalogue:
(BOSSBS-13038R-A680)
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) (25). 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 (25). 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-7546R-CY5.5)
Fournisseur:
Bioss
Description:
This gene encodes Lutheran blood group glycoprotein, a member of the immunoglobulin superfamily and a receptor for the extracellular matrix protein, laminin. The protein contains five extracellular immunoglobulin domains, a single transmembrane domain, and a short C-terminal cytoplasmic tail. This protein may play a role in epithelial cell cancer and in vaso-occlusion of red blood cells in sickle cell disease. Polymorphisms in this gene define some of the antigens in the Lutheran system and also the Auberger system. Inactivating variants of this gene result in the recessive Lutheran null phenotype, Lu(a-b-), of the Lutheran blood group. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2012].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7546R-A555)
Fournisseur:
Bioss
Description:
This gene encodes Lutheran blood group glycoprotein, a member of the immunoglobulin superfamily and a receptor for the extracellular matrix protein, laminin. The protein contains five extracellular immunoglobulin domains, a single transmembrane domain, and a short C-terminal cytoplasmic tail. This protein may play a role in epithelial cell cancer and in vaso-occlusion of red blood cells in sickle cell disease. Polymorphisms in this gene define some of the antigens in the Lutheran system and also the Auberger system. Inactivating variants of this gene result in the recessive Lutheran null phenotype, Lu(a-b-), of the Lutheran blood group. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2012].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6204R-CY7)
Fournisseur:
Bioss
Description:
NAP125, also known as NCKAP1 (NCK-associated protein 1), p125Nap1 or membrane-associated protein HEM-2, is a 1,128 amino acid single pass membrane protein that exists as two alternatively spliced isoforms and belongs to the HEM-1/HEM-2 family. While widely expressed, NAP125 is found at highest levels in heart, brain and skeletal muscle where it regulates Rac-dependent actin remodeling as part of a lamellipodial complex with WAVE2, Abi-1 and CYFIP1. NAP125 localizes to the cytoplasmic side of lamellipodium membrane and is encoded by a gene that maps to human chromosome 2q32.1 and mouse chromosome 2 C3. NAP125 expression is markedly reduced in Alzheimer disease (AD)-affected brains, suggesting a possible role in the disease.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12223R-A750)
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 Kr_ppel-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 Kr_ppel 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-13038R-A488)
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-11183R-CY5)
Fournisseur:
Bioss
Description:
Extracellular proteases mediate the digestion of neighboring extracellular matrix components in initial tumor growth, allow desquamation of tumor cells into the surrounding environment, provide the basis for invasion of basement membranes in targeted metastatic organs and are required for release and activation of many growth and angiogenic factors. TMPRSS5 (transmembrane protease, serine 5), also known as spinesin, is a 457 amino acid single-pass type II membrane protein that is expressed specifically in brain and is thought to play a role in hearing. A member of the peptidase S1 family, TMPRSS5 contains one peptidase S1 domain and an SRCR domain, and is encoded by a gene that maps to human chromosome 11q23.2. Defects in the gene encoding TMPRSS5 are associated with deafness.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13038R-FITC)
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-5560R-CY5)
Fournisseur:
Bioss
Description:
Protein kinase C (PKC) zeta is a member of the PKC family of serine/threonine kinases which are involved in a variety of cellular processes such as proliferation, differentiation and secretion. Unlike the classical PKC isoenzymes which are calcium-dependent, PKC zeta exhibits a kinase activity which is independent of calcium and diacylglycerol but not of phosphatidylserine. Furthermore, it is insensitive to typical PKC inhibitors and cannot be activated by phorbol ester. Unlike the classical PKC isoenzymes, it has only a single zinc finger module. These structural and biochemical properties indicate that the zeta subspecies is related to, but distinct from other isoenzymes of PKC. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5343R-A680)
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-12223R-CY5)
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-2672R-A647)
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
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