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2-Fluor-4-methylanisol
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2-Fluor-4-methylanisol
Artikel-Nr:
(BOSSBS-12438R-A350)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12438R-A350
Lokale Artikelnummer::
BOSSBS-12438R-A350
Beschreibung:
LRRFIP2 is a 721 amino acid protein that belongs to the LRRFIP family. Ubiquitously expressed, LRRFIP2 acts as an activator of the Wnt signaling pathway and as a positive regulator of NFâ…¹B activity. LRRFIP2 may be involved in regulating cytokine production in macrophages, suggesting a functional role in the TLR4-mediated inflammatory response. Three isoforms of LRRFIP2 exists due to alternative splicing events.
VE:
1 * 100 µl
Lieferant:
FLUOROCHEM
Beschreibung:
2-Amino-4,5-dimethoxybenzonitril
Artikel-Nr:
(ENAMEN300-30883.1G)
Lieferant:
SIA ENAMINE
Hersteller-Artikelnummer::
EN300-30883.1G
Lokale Artikelnummer::
ENAMEN300-30883.1G
Beschreibung:
2-Amino-6-methylbenzamid
VE:
1 * 1 g
 This is a MarketSource item. Additional charges may apply
Lieferant:
Sigma-Aldrich
Beschreibung:
5-Amino-1-naphthol, Sigma-Aldrich®
Artikel-Nr:
(BOSSBS-5855R-CY3)
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
Artikel-Nr:
(BOSSBS-5855R-A680)
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
Artikel-Nr:
(BOSSBS-5855R-CY5.5)
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
Artikel-Nr:
(BOSSBS-5855R-HRP)
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
Artikel-Nr:
(BOSSBS-5855R-FITC)
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
Artikel-Nr:
(BOSSBS-5855R-CY7)
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
Artikel-Nr:
(BSENR-141-100)
Lieferant:
Biosensis
Hersteller-Artikelnummer::
R-141-100
Lokale Artikelnummer::
BSENR-141-100
Beschreibung:
Beclin-1 plays a central role in autophagy. It may also play a role in antiviral host defense. It is ubiquitously expressed and it localises to the cytoplasm, golgi apparatus membrane, and in dendrites and cell bodies of cerbellar Purkinje cells. The unprocessed precursor has a length of 450 amino acids and an estimated molecular weight of 51.89 kDa.
VE:
1 * 100 µl
Lieferant:
Sigma-Aldrich
Beschreibung:
(±)-1-Amino-2-propanol, Sigma-Aldrich®
Artikel-Nr:
(SIAL122513-25G)
Lieferant:
Sigma-Aldrich
Hersteller-Artikelnummer::
122513-25G
Lokale Artikelnummer::
SIAL122513-25G
Beschreibung:
2-Amino-3-hydroxypyridin, Sigma-Aldrich®
VE:
1 * 25 g
Lieferant:
COMBI-BLOCKS
Beschreibung:
3-Amino-5-chlor-2-methylpyridin
Lieferant:
FLUOROCHEM
Beschreibung:
2-Amino-4,4,4-trifluorbuttersäure
Artikel-Nr:
(BOSSBS-13345R-FITC)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13345R-FITC
Lokale Artikelnummer::
BOSSBS-13345R-FITC
Beschreibung:
The GGA family of proteins (Golgi-localized, g-Adaptin ear-containing, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin. Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multi-domain proteins that bind mannose 6-phosphate receptors (MPRs). GGAs have modular structures with an N-terminal VHS (VPS27, Hrs and STAM) domain followed by a GAT (GGA and Tom1) domain, a connecting hinge segment and a C-terminal GAE (g-Adaptin ear) domain. The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences. The human GGA3 gene maps to chromosome 17 and encodes a 723 amino acid protein that shares 46% sequence identity with GGA1 and 38% with GGA2.
VE:
1 * 100 µl
Preis auf Anfrage
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 noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
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
noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
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