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Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-9616R-A488
Lokale Artikelnummer:: BOSSBS-9616R-A488
Beschreibung:   Ubr7 is a 425 amino acid protein that contains one UBR-type zinc finger and one PHD zinc finger. Participating in protein modification events within the N-end rule pathway, Ubr7 functions as an E3 ubiquitin-protein ligase that recognizes and binds proteins that contain destabilizing N-terminal residues, thereby leading to their ubiquitination and subsequent degradation.
VE:  1 * 100 µl

Lieferant:  US Biological
Hersteller-Artikelnummer:: 133513
Lokale Artikelnummer:: USBI133513
Beschreibung:   Anti-SLC7A1 Mouse Polyclonal Antibody
VE:  1 * 50 µG
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-12438R-FITC
Lokale Artikelnummer:: BOSSBS-12438R-FITC
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:  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:  US Biological
Hersteller-Artikelnummer:: 031670-AP
Lokale Artikelnummer:: USBI031670-AP
Beschreibung:   Anti-AES Rabbit Polyclonal Antibody (AP (Alkaline Phosphatase))
VE:  1 * 200 µl

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:  Bioss
Hersteller-Artikelnummer:: BS-11468R-A750
Lokale Artikelnummer:: BOSSBS-11468R-A750
Beschreibung:   Nogo is an oligodendrocyte-specific member of the Reticulon family and is a component of CNS white matter that inhibits axon outgrowth, induces collapse of growth cones of chick dorsal root ganglion cells, and inhibits the spreading of 3T3 fibroblasts. Nogo is expressed by oligodendrocytes but not by Schwann cells and associates primarily with the endoplasmic reticulum. Nogo exists in three different splice forms, Nogo A, B and C. NgBR (Nogo-B receptor), also known as nuclear undecaprenyl pyrophosphate synthase 1 homolog, is a 293 amino acid single-pass type I membrane protein that acts as a specific receptor for the amino-terminus of Nogo-B. Through this interaction, NgBR is involved in the regulation of vascular remodeling and angiogenesis. NgBR also enhances Niemann-Pick type C2 protein (NPC2) stabilisation. Knockdown of NgBR mRNA leads to decreased NPC2 levels, which results in the hallmarks of NPC2 mutation: increased intracellular cholesterol accumulation and a loss of sterol sensing.
VE:  1 * 100 µl
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
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-11956R-HRP
Lokale Artikelnummer:: BOSSBS-11956R-HRP
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. SLITRK3 (SLIT and NTRK-like family, member 3) is a 977 amino acid single-pass type I membrane protein that contains 20 LRR repeats and belongs to the SLITRK family. Expressed at highest levels in cerebral cortex, SLITRK3 is also found in adult and fetal neural tissues and some astrocytic brain tumors. SLITRK3 functions to suppress neurite outgrowth and plays a role in the regulation of neuronal function. SLITRK3 is encoded by a gene that maps to human chromosome 3, which houses over 1,100 genes, including a chemokine receptor (CKR) gene cluster and a variety of human cancer-related gene loci.
VE:  1 * 100 µl
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-11956R-FITC
Lokale Artikelnummer:: BOSSBS-11956R-FITC
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. SLITRK3 (SLIT and NTRK-like family, member 3) is a 977 amino acid single-pass type I membrane protein that contains 20 LRR repeats and belongs to the SLITRK family. Expressed at highest levels in cerebral cortex, SLITRK3 is also found in adult and fetal neural tissues and some astrocytic brain tumors. SLITRK3 functions to suppress neurite outgrowth and plays a role in the regulation of neuronal function. SLITRK3 is encoded by a gene that maps to human chromosome 3, which houses over 1,100 genes, including a chemokine receptor (CKR) gene cluster and a variety of human cancer-related gene loci.
VE:  1 * 100 µl
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-1603R-HRP
Lokale Artikelnummer:: BOSSBS-1603R-HRP
Beschreibung:   The protein encoded by this gene belongs to the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases play critical roles in mRNA translation by charging tRNAs with their cognate amino acids. The encoded protein is a mitochondrial enzyme that specifically aminoacylates alanyl-tRNA. Mutations in this gene are a cause of combined oxidative phosphorylation deficiency 8.
VE:  1 * 100 µl
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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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