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Numer katalogowy: (BOSSBS-8682R-A488)
Producent: Bioss
Opis: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.
j.m.: 1 * 100 µl


Producent: Genscript
Opis: GenBox Gel electrophoresis system is designed to run 1 or 2 mini gels at the same time. GenBox mini tank is designed for ultimate convenience and consistent performance compared to traditional electrophoresis tanks. Discover the versatile and easy to use GenBox mini tank for your gel electrophoresis and blotting needs.

Numer katalogowy: (BSENM-1657-100)
Producent: Biosensis
Opis: Visinin (sometimes known as hippocalcin-like protein 3, HLP3, HPCAL3, HUVISL1, VLP-1, VILIP and VILIP-1) was originally isolated biochemically from chicken retina as a major protein of about 24kDa on SDS-PAGE. Following cloning and sequencing of visinin, several visinin like proteins were discovered by homology screening. One of these, Visinin-like protein 1 is a small Calcium binding protein which is very abundant in the nervous system and is found only in neurons, though different neurons have different levels of expression. It is particularly concentrated in cerebellar Purkinje cells, and tends to be most abundant in perikarya and dendrites. The protein belongs to the large superfamly of calmodulin and paravalbumin type proteins which function by binding Calcium ions. Calcium binding alters the confomation of these proteins and allow them to interact with other binding partners, the properties of which they may alter. Visinin-like protein 1 has four 'EF hand' domains, which are negatively charged helix-turn-helix peptides which are responsible for Calcium binding. Visinin-like protein 1 is 191 amino acids in size and has a molecular weight on SDS-PAGE of 22kDa.
j.m.: 1 * 100 µG


Numer katalogowy: (BOSSBS-1864R-A488)
Producent: Bioss
Opis: SerpinB2 is a serine proteinase inhibitor of the ovalbumin like B clade of serpins. It was first discovered in the placenta, and given the name PAI-2 because of the ability to inhibit urokinase plasminogen activator (u-PA) at low micromolar efficiency. SerpinB2 also inhibits tissue plasminogen activator (t-PA), but with micromolar efficiency, and PAI-1 is much more efficient that SerpinB2 on both forms of plasminogen activator. The structure of PAI-2 is not terribly similar to PAI-1, however, which is an E clade serpin. SerpinB2 is made by many cell types, and is found intracellularly as an unglycosylated kDa protein, and secreted as a 60 kDa protein. SerpinB2 is found in saliva, secreted by gingival fibroblasts, and in the skin. SerpinB2 levels are elevated in serum during pregnancy, and in leukemia, breast cancer and ovarian cancer, although it was lowered in some cancers.A shorter SerpinB2 isoform of 382 amino acids, has been reported, with a predicted mass of 43.1 kDa and a pI of 5.69. The shorter form has a deletion just after the start of the mature protein, but it is unclear what the relative production and distribution is for the shorter sequence.
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-1967R-CY5)
Producent: Bioss
Opis: Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-1864R-A350)
Producent: Bioss
Opis: SerpinB2 is a serine proteinase inhibitor of the ovalbumin like B clade of serpins. It was first discovered in the placenta, and given the name PAI-2 because of the ability to inhibit urokinase plasminogen activator (u-PA) at low micromolar efficiency. SerpinB2 also inhibits tissue plasminogen activator (t-PA), but with micromolar efficiency, and PAI-1 is much more efficient that SerpinB2 on both forms of plasminogen activator. The structure of PAI-2 is not terribly similar to PAI-1, however, which is an E clade serpin. SerpinB2 is made by many cell types, and is found intracellularly as an unglycosylated kDa protein, and secreted as a 60 kDa protein. SerpinB2 is found in saliva, secreted by gingival fibroblasts, and in the skin. SerpinB2 levels are elevated in serum during pregnancy, and in leukemia, breast cancer and ovarian cancer, although it was lowered in some cancers.A shorter SerpinB2 isoform of 382 amino acids, has been reported, with a predicted mass of 43.1 kDa and a pI of 5.69. The shorter form has a deletion just after the start of the mature protein, but it is unclear what the relative production and distribution is for the shorter sequence.
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-1864R-CY3)
Producent: Bioss
Opis: SerpinB2 is a serine proteinase inhibitor of the ovalbumin like B clade of serpins. It was first discovered in the placenta, and given the name PAI-2 because of the ability to inhibit urokinase plasminogen activator (u-PA) at low micromolar efficiency. SerpinB2 also inhibits tissue plasminogen activator (t-PA), but with micromolar efficiency, and PAI-1 is much more efficient that SerpinB2 on both forms of plasminogen activator. The structure of PAI-2 is not terribly similar to PAI-1, however, which is an E clade serpin. SerpinB2 is made by many cell types, and is found intracellularly as an unglycosylated kDa protein, and secreted as a 60 kDa protein. SerpinB2 is found in saliva, secreted by gingival fibroblasts, and in the skin. SerpinB2 levels are elevated in serum during pregnancy, and in leukemia, breast cancer and ovarian cancer, although it was lowered in some cancers.A shorter SerpinB2 isoform of 382 amino acids, has been reported, with a predicted mass of 43.1 kDa and a pI of 5.69. The shorter form has a deletion just after the start of the mature protein, but it is unclear what the relative production and distribution is for the shorter sequence.
j.m.: 1 * 100 µl


Numer katalogowy: (PRSI29-555)
Producent: ProSci Inc.
Opis: MSH2 was identified as a locus frequently mutated in hereditary nonpolyposis colon cancer (HNPCC). When cloned, it was discovered to be a human homolog of the E. coli mismatch repair gene mutS, consistent with the characteristic alterations in microsatellite sequences (RER+ phenotype) found in HNPCC.
j.m.: 1 * 100 µG


Numer katalogowy: (PRSI55-920)
Producent: ProSci Inc.
Opis: MSH2 was identified as a locus frequently mutated in hereditary nonpolyposis colon cancer (HNPCC). When cloned, it was discovered to be a human homolog of the E. coli mismatch repair gene mutS, consistent with the characteristic alterations in microsatellite sequences (RER+ phenotype) found in HNPCC. [provided by RefSeq].
j.m.: 1 * 400 µl

New Product


Numer katalogowy: (PRSI92-456)
Producent: ProSci Inc.
Opis: TIGIT (also called T cell immunoreceptor with Ig and ITIM domains) is one newly discovered immune receptor on some percentage of T cells and Natural Killer Cells(NK). It is also identified as WUCAM and Vstm3. TIGIT could bind to CD155(PVR) on dendritic cells(DCs), macrophages, etc. with high affinity, and also to CD112(PVRL2) with lower affinity.
j.m.: 1 * 50 µG


Numer katalogowy: (BOSSBS-1967R)
Producent: Bioss
Opis: Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-13157R-CY3)
Producent: Bioss
Opis: Src is the human homolog of the v-Src gene of the rous sarcoma virus, also designated avian sarcoma virus or ASV. Src was the first proto-oncogenic non-receptor tyrosine kinase characterized in human. The Src family, which has common structural motifs, is composed of nine members in vertebrates, including Src, Yes, Fgr, Frk, Fyn, Lyn, Hck, Lck and Blk. Src-family kinases transduce signals that are involved in the control of a variety of cellular processes, including proliferation, differentiation, motility and adhesion. Src-family ki-nases contain an amino-terminal cell membrane anchor followed by an SH3 domain and an SH2 domain, which are involved in modular association and activation, respectively. Src-family kinases, which are normally maintained in an inactive state and can be activated transiently during cellular events such as mitosis. Different subcellular localizations of Src-family kinases may be important for the regulation of specific cellular processes such as mitogenesis, cytoskeletal organization and membrane trafficking. c-Fgr is a human non-receptor tyrosine kinase family member that was discovered by using a probe toward the v-Fgr portion of the cell-derived domain of Gardner-Rasheed feline sarcoma virus. The human c-Fgr gene encodes a 529 amino acid protein.
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-13157R-CY7)
Producent: Bioss
Opis: Src is the human homolog of the v-Src gene of the rous sarcoma virus, also designated avian sarcoma virus or ASV. Src was the first proto-oncogenic non-receptor tyrosine kinase characterized in human. The Src family, which has common structural motifs, is composed of nine members in vertebrates, including Src, Yes, Fgr, Frk, Fyn, Lyn, Hck, Lck and Blk. Src-family kinases transduce signals that are involved in the control of a variety of cellular processes, including proliferation, differentiation, motility and adhesion. Src-family ki-nases contain an amino-terminal cell membrane anchor followed by an SH3 domain and an SH2 domain, which are involved in modular association and activation, respectively. Src-family kinases, which are normally maintained in an inactive state and can be activated transiently during cellular events such as mitosis. Different subcellular localizations of Src-family kinases may be important for the regulation of specific cellular processes such as mitogenesis, cytoskeletal organization and membrane trafficking. c-Fgr is a human non-receptor tyrosine kinase family member that was discovered by using a probe toward the v-Fgr portion of the cell-derived domain of Gardner-Rasheed feline sarcoma virus. The human c-Fgr gene encodes a 529 amino acid protein.
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-1967R-A488)
Producent: Bioss
Opis: Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-0022R-A750)
Producent: Bioss
Opis: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localised in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis.
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-1967R-CY7)
Producent: Bioss
Opis: Kallikrein 9, also known as Kallikrein-Like 3 (KLK-L3), is a chymotrypsin-like serine proteinase. Kallikrein 9 was discovered as the locus for kallikreins on chromosome 19 was more fully mapped and found by similarity to the other tissue kallikreins. Kallikrein 9 has been found in the ovary, thymus, testis, prostate, skin, breast and neuronal tissues and is made by many cell lines in culture. Kallikrein 9 levels in breast cancer and uterine cancer patients have been reported to drop as the disease progresses, thus hK9 might be considered a favorable prognostic marker. Different splice variants of hK9 have been reported, although it is not yet known if they produce functional proteins. The full length Kallikrein 9 encodes for a 250 amino acid protein, with a predicted mass of 27.5 kDa and a pI of 7.53. The 234 amino acid form predicts a protein of 26 kDa with a pI of 9.76 and this quite basic pI might give the shorter form a very different function or localization. The shorter sequence also diverges before the catalytic serine residue, making it unlikely to be proteolytically active. Pre-pro-kallikrein 9 has the 17 amino acid signal sequence is removed before secretion, and the Pro-kallikrein 9 is activated to Kallikrein 9 by removal of the 5 amino acid propeptide domain.
j.m.: 1 * 100 µl


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