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Supplier: Thermo Fisher Scientific
Description: Diclofenac sodium salt
Catalog Number: (BSENR-182-250)
Supplier: Biosensis
Description: Ubiquitin is a highly conserved 76 amino acid protein with an estimated molecular weight of 8.56 kDa which has a central role in regulated protein degradation. It is a protein modifier which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Several types of polymeric chains can be formed depending on the lysine used for the assembly. Attachment to proteins as a polymer leads to their degradation by the 26S proteosome; a complex, multicatalytic cytosolic and nuclear protease. Attachment to proteins as a monomer or as an alternatively linked polymer does not lead to proteasomal degradation and may be required for numerous functions, including maintenance of chromatic structure, regulation of gene expression, stress response, ribosome biogenesis and DNA repair. Ubiquitin is synthesized as a polyubiquitin precursor with exact head to tail repeats, the number of repeats of which differ between species and strains. In some species there is a final amino-acid after the last repeat, here in bovine a Cys. Some ubiquitin genes contain a single copy of ubiquitin fused to a ribosomal protein (either L40 or S27a).
UOM: 1 * 250 µG


Catalog Number: (BSENM-1404-100)
Supplier: Biosensis
Description: Ubiquitin is a highly conserved 76 amino acid protein with an estimated molecular weight of 8.56 kDa which has a central role in regulated protein degradation. It is a protein modifier which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Several types of polymeric chains can be formed depending on the lysine used for the assembly. Attachment to proteins as a polymer leads to their degradation by the 26S proteosome; a complex, multicatalytic cytosolic and nuclear protease. Attachment to proteins as a monomer or as an alternatively linked polymer does not lead to proteasomal degradation and may be required for numerous functions, including maintenance of chromatic structure, regulation of gene expression, stress response, ribosome biogenesis and DNA repair. Ubiquitin is synthesized as a polyubiquitin precursor with exact head to tail repeats, the number of repeats of which differ between species and strains. In some species there is a final amino-acid after the last repeat, here in bovine a Cys. Some ubiquitin genes contain a single copy of ubiquitin fused to a ribosomal protein (either L40 or S27a).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12406R-A488)
Supplier: Bioss
Description: SNX2 and SNX4 share a high degree of amino acid similarity with SNX1, as they all contain a characteristic phox homology (PX) domain (4). These proteins are all partially associated with cellular membranes, and they, likewise, associate with EGF, PDGF and insulin receptor tyrosine kinases (2). These nexins are widely expressed and yet have various tissue distribution patterns. Additionally, the sorting nexins can associate with each other and with a variety of other cellular proteins, suggesting that they exist as part of multisubunit complexes (1,5). The related protein, SNX3, comprises a distinct subgroup of nexins that share less sequence similarity outside of the PX domain and have dramatically different binding affinities for the tyrosine kinase receptors (2,6).
UOM: 1 * 100 µl


Supplier: Thermo Fisher Scientific
Description: Rilpivirine

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Catalog Number: (MOLE39643340-25G)
Supplier: Molekula
Description: Diclofenac sodium salt
UOM: 1 * 25 g

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Catalog Number: (287840-1)
Supplier: Merck Millipore (Calbiochem‎)
Description: Diclofenac sodium salt, Millipore®
UOM: 1 * 1 g


Catalog Number: (BOSSBS-9609R)
Supplier: Bioss
Description: Proteins containing RNA recognition motifs, including various hnRNP proteins, are implicated in the regulation of alternative splicing and protein components of snRNPs. The RBM (RNA-binding motif) gene family encodes proteins with an RNA binding motif that have been suggested to play a role in the modulation of apoptosis. RBM26 (RNA binding motif protein 26), whose alternative names include CTCL tumor antigen se70-2, C13orf10, ARRS2, SE70-2, ZC3H17, PRO1777, FLJ20957, RP11-255E21.1, MGC133295 or MGC133296, is a 1,007 amino acid protein with six isoforms which result due to alternative splicing. RBM26 also contains one C3H1-type zinc finger and two RRM (RNA recognition motif) domains. The gene encoding RBM26 maps to human chromosome 13q31.1.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13569R)
Supplier: 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. Zinc finger and BTB domain-containing protein 26 (ZBTB26), also known as ZNF481, is a 441 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB26 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain suggest that ZBTB26 functions as a transcription regulator.
UOM: 1 * 100 µl


Supplier: MP Biomedicals
Description: L-Lysine is an essential proteinogenic α amino acid. It contains an N-butyl amino group in the side chain, and this moiety is protonated at physiological pH. In addition, L-lysine is one of the two amino acids that are degraded to give ketone bodies (a ketogenic amino acid).

Catalog Number: (BOSSBS-1967R-A680)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12406R-A647)
Supplier: Bioss
Description: SNX2 and SNX4 share a high degree of amino acid similarity with SNX1, as they all contain a characteristic phox homology (PX) domain (4). These proteins are all partially associated with cellular membranes, and they, likewise, associate with EGF, PDGF and insulin receptor tyrosine kinases (2). These nexins are widely expressed and yet have various tissue distribution patterns. Additionally, the sorting nexins can associate with each other and with a variety of other cellular proteins, suggesting that they exist as part of multisubunit complexes (1,5). The related protein, SNX3, comprises a distinct subgroup of nexins that share less sequence similarity outside of the PX domain and have dramatically different binding affinities for the tyrosine kinase receptors (2,6).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-12406R-HRP)
Supplier: Bioss
Description: SNX2 and SNX4 share a high degree of amino acid similarity with SNX1, as they all contain a characteristic phox homology (PX) domain (4). These proteins are all partially associated with cellular membranes, and they, likewise, associate with EGF, PDGF and insulin receptor tyrosine kinases (2). These nexins are widely expressed and yet have various tissue distribution patterns. Additionally, the sorting nexins can associate with each other and with a variety of other cellular proteins, suggesting that they exist as part of multisubunit complexes (1,5). The related protein, SNX3, comprises a distinct subgroup of nexins that share less sequence similarity outside of the PX domain and have dramatically different binding affinities for the tyrosine kinase receptors (2,6).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1967R-HRP)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1967R-CY3)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1967R-CY7)
Supplier: Bioss
Description: 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.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
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