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Numer katalogowy: (BOSSBS-7594R-FITC)
Producent: Bioss
Opis: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-7594R-CY7)
Producent: Bioss
Opis: Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].
j.m.: 1 * 100 µl


Numer katalogowy: (BOSSBS-0022R-A647)
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 localized 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-8682R-CY3)
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


Numer katalogowy: (PRSI48-383)
Producent: ProSci Inc.
Opis: Also known as LRRN6A (leucine-rich repeat neuronal 6A), LINGO1 is a newly discovered gene that is expressed primarily in the central nervous system during early embro development, and may be an essential protein in the development of the nervous system.
j.m.: 1 * 50 µG


Numer katalogowy: (BOSSBS-0022R-HRP)
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 localized 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-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: (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-1864R-HRP)
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


Producent: EPPENDORF
Opis: Discover the PCR Plates BioBased made of bio-based polymer (mass balance approach). These plates allow you to significantly reduce your consumable-related carbon footprint and yet to maintain the identical technical performance. The new bio-based plates have the identical material properties and technical specifications as the legacy plates.

Numer katalogowy: (PRSI2447)
Producent: ProSci Inc.
Opis: MTBP Antibody: The p53 tumor-suppressor gene integrates numerous signals that control cell life and death. Several novel molecules involved in p53 network, including Chk2, p53R2, p53AIP1, Noxa, PIDD, PID/MTA2 and MTBP, were recently discovered. The transcriptional activity of p53 is modulated by posttranslational regulations of the p53 protein including stabilization and acetylation. P53 transcriptionally activates MDM2 gene then the translated MDM2 protein binds to p53 and promotes the degradation of p53 leading to lowering the concentration of p53 protein. MDM2 inhibits both p53 mediated G1 arrest and apoptosis. A recently discovered protein termed MTBP was found to bind to MDM2 and to inhibit the modulation effect of MDM2 on p53. MTBP is expressed in a variety of normal tissues.
j.m.: 1 * 100 µG


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-CY3)
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-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


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


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