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Katalogové číslo: (BOSSBS-9238R-CY5)
Dodavatel: Bioss
Popis: 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. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11966R-A488)
Dodavatel: Bioss
Popis: The Testican family, also designated the BM-40/SPARC/osteonectin family, is composed of highly conserved, extracellular, calcium-binding, sulfate proteoglycans. Expression of Testicans is detected in a variety of tissues, but is most abundant in brain. Family members include Testican-1, Testican-2, Testican-3 and an amino-terminal splice variant of Testican-3, designated N-Tes. Most Testicans inhibit MT-MMPs, thereby inhibiting the activity of pro-MMP-2. Testican-2 is expressed in the central nervous system (CNS), with widespread expression in the olfactory bulb, cerebral cortex, thalamus, hippocampus, cerebellum and medulla, and is also found in lung and testis. Testican-2 is unique in that it actually abolishes the inhibition of MT-MMPs by other testican family members and specifically inactivates N-Tes by binding to its COOH-terminal extracellular calcium-binding domain. Testican-2 halts neurite growth from cerebellar neurons and may be involved in regu-lating the development of the CNS.
Měrná jednotka: 1 * 100 µl


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Katalogové číslo: (BOSSBS-11966R-CY3)
Dodavatel: Bioss
Popis: The Testican family, also designated the BM-40/SPARC/osteonectin family, is composed of highly conserved, extracellular, calcium-binding, sulfate proteoglycans. Expression of Testicans is detected in a variety of tissues, but is most abundant in brain. Family members include Testican-1, Testican-2, Testican-3 and an amino-terminal splice variant of Testican-3, designated N-Tes. Most Testicans inhibit MT-MMPs, thereby inhibiting the activity of pro-MMP-2. Testican-2 is expressed in the central nervous system (CNS), with widespread expression in the olfactory bulb, cerebral cortex, thalamus, hippocampus, cerebellum and medulla, and is also found in lung and testis. Testican-2 is unique in that it actually abolishes the inhibition of MT-MMPs by other testican family members and specifically inactivates N-Tes by binding to its COOH-terminal extracellular calcium-binding domain. Testican-2 halts neurite growth from cerebellar neurons and may be involved in regu-lating the development of the CNS.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11966R-HRP)
Dodavatel: Bioss
Popis: The Testican family, also designated the BM-40/SPARC/osteonectin family, is composed of highly conserved, extracellular, calcium-binding, sulfate proteoglycans. Expression of Testicans is detected in a variety of tissues, but is most abundant in brain. Family members include Testican-1, Testican-2, Testican-3 and an amino-terminal splice variant of Testican-3, designated N-Tes. Most Testicans inhibit MT-MMPs, thereby inhibiting the activity of pro-MMP-2. Testican-2 is expressed in the central nervous system (CNS), with widespread expression in the olfactory bulb, cerebral cortex, thalamus, hippocampus, cerebellum and medulla, and is also found in lung and testis. Testican-2 is unique in that it actually abolishes the inhibition of MT-MMPs by other testican family members and specifically inactivates N-Tes by binding to its COOH-terminal extracellular calcium-binding domain. Testican-2 halts neurite growth from cerebellar neurons and may be involved in regu-lating the development of the CNS.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-7613R-FITC)
Dodavatel: Bioss
Popis: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se.Tissue specificity: Broadly expressed, with lowest levels in brain and thymus, and highest levels detectable in heart, ovary and testis.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1967R-A488)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-9238R-A680)
Dodavatel: Bioss
Popis: 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. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localises to cytosol but shifts to mitochondria upon co-localisation with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-9238R-A488)
Dodavatel: Bioss
Popis: 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. RNF23 (RING finger protein 23), also known as tripartite motif-containing protein 39 (TRIM39) or testis-abundant finger protein, is a 518 amino acid protein belonging to the TRIM/RBCC family that is known to interact with MOAP1. Ubiquitously expressed and existing as two alternatively spliced isoforms, RNF23 is found at highest levels in spleen, testis, brain, kidney, liver, heart and skeletal muscle. RNF23 typically localizes to cytosol but shifts to mitochondria upon co-localization with MOAP1, a short-lived, pro-apoptotic protein which RNF23 prevents from becoming poly-ubiquitinated and degraded, thereby facilitating apoptosis. RNF23 contains one B box-type zinc finger, a B30.2/SPRY domain and a single RING-type zinc finger.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1967R-CY3)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1967R-CY7)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1967R-A647)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-11966R-A647)
Dodavatel: Bioss
Popis: The Testican family, also designated the BM-40/SPARC/osteonectin family, is composed of highly conserved, extracellular, calcium-binding, sulfate proteoglycans. Expression of Testicans is detected in a variety of tissues, but is most abundant in brain. Family members include Testican-1, Testican-2, Testican-3 and an amino-terminal splice variant of Testican-3, designated N-Tes. Most Testicans inhibit MT-MMPs, thereby inhibiting the activity of pro-MMP-2. Testican-2 is expressed in the central nervous system (CNS), with widespread expression in the olfactory bulb, cerebral cortex, thalamus, hippocampus, cerebellum and medulla, and is also found in lung and testis. Testican-2 is unique in that it actually abolishes the inhibition of MT-MMPs by other testican family members and specifically inactivates N-Tes by binding to its COOH-terminal extracellular calcium-binding domain. Testican-2 halts neurite growth from cerebellar neurons and may be involved in regu-lating the development of the CNS.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1967R-CY5.5)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1967R-A750)
Dodavatel: Bioss
Popis: 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 localisation. 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1967R-A350)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


Katalogové číslo: (BOSSBS-1967R-FITC)
Dodavatel: Bioss
Popis: 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.
Měrná jednotka: 1 * 100 µl


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Omezené množství produktu na skladě. Zboží může být k dispozici v jiném skladě poblíž vašeho sídla. Přesvědčte se, že jste přihlášení na stránky, abyste mohli vidět dostupné položky na skladě. Pokud je stále zobrazeno call a potřebujete asistenci, volejte na číslo 321 570 321.
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