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3-Chloro-4-(ethoxycarbonyl)benzeneboronic+acid,+pinacol+ester


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Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-11959R-A488
Lokale Artikelnummer:: BOSSBS-11959R-A488
Beschreibung:   The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. SLITRK5 (SLIT and NTRK-like family, member 5), also known as LRRC11 (leucine-rich repeat-containing protein 11), is a 958 amino acid single-pass type I membrane protein that contains 16 LRR repeats and belongs to the SLITRK family. Expressed at high levels in the cerebral cortex, but also present in areas of the spinal cord and medulla, SLITRK5 functions to suppress neurite outgrowth, thereby playing a regulatory role in neuronal function. The gene encoding SLITRK5 maps to human chromosome 13, which houses over 400 genes, such as BRCA2 and RB1, and comprises nearly 4% of the human genome. Trisomy 13, also known as Patau syndrome, is deadly and the few who survive past one year suffer from permanent neurologic defects, difficulty eating and vulnerability to serious respiratory infections.
VE:  1 * 100 µl
Artikel-Nr: (BOSSBS-12252R)

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-12252R
Lokale Artikelnummer:: BOSSBS-12252R
Beschreibung:   ZFP57 is a 452 amino acid protein that contains one KRAB domain and seven C2H2-type zinc fingers and is a member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZFP57 functions as a transcriptional repressor that inhibits the expression of Schwann cell-specific proteins, thereby playing a role in the development of the peripheral nervous system. ZFP57 exists as two isoforms that are produced from alternative splicing events.
VE:  1 * 100 µl
Artikel-Nr: (BOSSBS-11691R)

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-11691R
Lokale Artikelnummer:: BOSSBS-11691R
Beschreibung:   FLAD1 is a 587 amino acid protein where its N-terminus belongs to the moaB/mog family and its C-terminus belongs to the PAPS reductase family. Existing as five alternatively spliced isoforms, FLAD1 localizes to the cytoplasm and utilizes magnesium as a cofactor. FLAD1 is a key enzyme in the metabolic pathway that converts riboflavin into the redox cofactor flavin adenine dinucleotide (FAD). It is suggested that the molybdenum cofactor biosynthesis protein-like region of FLAD1 may not be functional.
VE:  1 * 100 µl
Artikel-Nr: (BOSSBS-9348R)

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-9348R
Lokale Artikelnummer:: BOSSBS-9348R
Beschreibung:   ACLP2 (acid phosphatase-like 2), also known as UNQ370 or PRO706, is a 480 amino acid secreted protein that functions to catalyze the H2O-dependent conversion of a phosphate monoester to an alcohol and a phosphate. Expressed as two alternatively spliced isoforms, ACPL2 is encoded by a gene that maps to chromosome 3, which houses over 1,100 genes, including a chemokine receptor (CKR) gene cluster and a variety of human cancer-related gene loci. Key tumor suppressing genes on chromosome 3 include those that encode the apoptosis mediator RASSF1, the cell migration regulator HYAL1 and the angiogenesis suppressor SEMA3B. Marfan Syndrome, porphyria, von Hippel-Lindau syndrome, osteogenesis imperfecta and Charcot-Marie-Tooth Disease are a few of the numerous genetic diseases associated with chromosome 3.
VE:  1 * 100 µl
Lieferant:  Thermo Scientific
Beschreibung:   2-Amino-3-brom-5-methylbenzoesäure
Lieferant:  US Biological
Hersteller-Artikelnummer:: F4150-25-HRP
Lokale Artikelnummer:: USBIF4150-25-HRP
Beschreibung:   Anti-FKBP10 Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))
VE:  1 * 200 µl
Lieferant:  SIGMA ALDRICH MICROSCOPY
Beschreibung:   Hämatoxylin, Sigma-Aldrich®
Artikel-Nr: (MHS80-2.5L)

Lieferant:  SIGMA ALDRICH MICROSCOPY
Hersteller-Artikelnummer:: MHS80-2.5L
Lokale Artikelnummer:: SIAMMHS80-2.5L
Beschreibung:   Hämatoxylin
VE:  1 * 2,5 L

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-5855R-CY3
Lokale Artikelnummer:: BOSSBS-5855R-CY3
Beschreibung:   ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-5855R-A680
Lokale Artikelnummer:: BOSSBS-5855R-A680
Beschreibung:   ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilisation. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-5855R-CY5.5
Lokale Artikelnummer:: BOSSBS-5855R-CY5.5
Beschreibung:   ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
VE:  1 * 100 µl
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-5855R-HRP
Lokale Artikelnummer:: BOSSBS-5855R-HRP
Beschreibung:   ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
VE:  1 * 100 µl
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-5855R-FITC
Lokale Artikelnummer:: BOSSBS-5855R-FITC
Beschreibung:   ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-5855R-CY7
Lokale Artikelnummer:: BOSSBS-5855R-CY7
Beschreibung:   ADAM32 was first discovered in a search for testis-specific proteinases. ADAM32 was identified in human, rat, mouse, macaque and chimp, and thus far has been found only in testis. In mice, ADAM32 is found on the sperm surface, where it may play a role in fertilization. ADAM32 is a member of the ADAMs family (A Disintegrin And Metalloproteinase), but does not contain the canonical HExxHxxxxH zinc-binding metalloproteinase catalytic site. The domain structure of the full length ADAM32 includes a signal sequence, propeptide domain, metalloproteinase-like domain, disintegrin-like domain, cys-rich domain, EGF-like domain, a short spacer region, then the transmembrane domain and a cytoplasmic domain. Like many of the reproductive-specific ADAMS, ADAM32 plays a non-enzymatic role, or (as is the case for ADAMs 1 & 2 (fertilin alpha and beta)), the protein acts in concert with a proteolytically active ADAM to process proteins. Little is known about interactions between ADAM32 and other ADAMs. Several different sequences for human ADAM32 are published; 787, 688, 649, 629, and 279 amino acids in length. The 688 amino acid form is identical to the 787 AA form until the EGF-like domain, and lacks the TM and cytoplasmic domains. The 649 AA form is likewise identical to the longer form, just to the start of the TM domain, and also lacks the TM and cytoplasmic domains. The 629 AA form has a deletion of 107 residues midway into the MP-like domain, and lacks the amino end of the disintegrin domain, but contains the rest of the domains found in the full-length ADAM32. The predicted masses for the different versions are 87.8, 76.9, 72.9, 70.9 and 32.1, respectively, for the 786, 688, 649, 629 and 279 AA forms.
VE:  1 * 100 µl

Lieferant:  Sigma-Aldrich
Hersteller-Artikelnummer:: 248118-25G
Lokale Artikelnummer:: SIAL248118-25G
Beschreibung:   4-Amino-3-nitrobenzoesäure, Sigma-Aldrich®
VE:  1 * 25 g
Lieferant:  FLUOROCHEM
Beschreibung:   4-Amino-3-fluorbenzoesäure
Preis auf Anfrage
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Lager für diesen Artikel ist begrenzt, kann aber in einem Lagerhaus in Ihrer Nähe zur Verfügung. Bitte stellen Sie sicher, dass Sie in sind angemeldet auf dieser Seite, so dass verfügbare Bestand angezeigt werden können. Wenn das call noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
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