Esta buscando: Beckman Coulter

Numero del catalogo: (BOSSBS-8341R-FITC)

Proveedor: Bioss

Descripción: CPXM (carboxypeptidase X, member 1) belongs to the peptidase M14 family. However, no carboxypeptidase activity has yet been detected. It may be involved in cell-cell interactions.Members of the M14 metallocarboxypeptidase protein family serve many diverse functions and are divided into three subfamilies based on structure, function and amino acid sequence similarity. Belonging to the N/E subfamily, CPXM (metallocarboxypeptidase CPX-1) is a 734 amino acid protein that contains a F5/8 type C domain and likely binds one zinc ion per subunit. Most members of the N/E subfamily contain several domains, including an active carboxypeptidase domain and signal peptide, and are thought to function mostly in protein-protein interactions and/or protein-membrane interactions, thereby targeting the protein to specific locations within the secretory pathway. CPXM is a unique member of this subfamily in that it does not appear to exhibit any enzymatic activity due to lack of several active-site residues that are present in the catalytic domain of other members of the N/E subfamily. Studies showing that CPXM expression is regulated during osteoclastogenesis suggest that CPXM may play a role in osteoclast differentiation. There are two isoforms of CPXM which are a result of alternative splicing events.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8341R-A555)

Proveedor: Bioss

Descripción: CPXM (carboxypeptidase X, member 1) belongs to the peptidase M14 family. However, no carboxypeptidase activity has yet been detected. It may be involved in cell-cell interactions.Members of the M14 metallocarboxypeptidase protein family serve many diverse functions and are divided into three subfamilies based on structure, function and amino acid sequence similarity. Belonging to the N/E subfamily, CPXM (metallocarboxypeptidase CPX-1) is a 734 amino acid protein that contains a F5/8 type C domain and likely binds one zinc ion per subunit. Most members of the N/E subfamily contain several domains, including an active carboxypeptidase domain and signal peptide, and are thought to function mostly in protein-protein interactions and/or protein-membrane interactions, thereby targeting the protein to specific locations within the secretory pathway. CPXM is a unique member of this subfamily in that it does not appear to exhibit any enzymatic activity due to lack of several active-site residues that are present in the catalytic domain of other members of the N/E subfamily. Studies showing that CPXM expression is regulated during osteoclastogenesis suggest that CPXM may play a role in osteoclast differentiation. There are two isoforms of CPXM which are a result of alternative splicing events.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-8341R-A750)

Proveedor: Bioss

Descripción: CPXM (carboxypeptidase X, member 1) belongs to the peptidase M14 family. However, no carboxypeptidase activity has yet been detected. It may be involved in cell-cell interactions.Members of the M14 metallocarboxypeptidase protein family serve many diverse functions and are divided into three subfamilies based on structure, function and amino acid sequence similarity. Belonging to the N/E subfamily, CPXM (metallocarboxypeptidase CPX-1) is a 734 amino acid protein that contains a F5/8 type C domain and likely binds one zinc ion per subunit. Most members of the N/E subfamily contain several domains, including an active carboxypeptidase domain and signal peptide, and are thought to function mostly in protein-protein interactions and/or protein-membrane interactions, thereby targeting the protein to specific locations within the secretory pathway. CPXM is a unique member of this subfamily in that it does not appear to exhibit any enzymatic activity due to lack of several active-site residues that are present in the catalytic domain of other members of the N/E subfamily. Studies showing that CPXM expression is regulated during osteoclastogenesis suggest that CPXM may play a role in osteoclast differentiation. There are two isoforms of CPXM which are a result of alternative splicing events.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-12860R-A555)

Proveedor: Bioss

Descripción: Crystallins are separated into two classes:taxon-specific, or enzyme, and ubiquitous. The latter classconstitutes the major proteins of vertebrate eye lens and maintainsthe transparency and refractive index of the lens. Since lenscentral fiber cells lose their nuclei during development, thesecrystallins are made and then retained throughout life, making themextremely stable proteins. Mammalian lens crystallins are dividedinto alpha, beta, and gamma families; beta and gamma crystallinsare also considered as a superfamily. Alpha and beta families arefurther divided into acidic and basic groups. Seven protein regionsexist in crystallins: four homologous motifs, a connecting peptide,and N- and C-terminal extensions. Gamma-crystallins are ahomogeneous group of highly symmetrical, monomeric proteinstypically lacking connecting peptides and terminal extensions. Theyare differentially regulated after early development. This geneencodes a protein initially considered to be a beta-crystallin butthe encoded protein is monomeric and has greater sequencesimilarity to other gamma-crystallins. This gene encodes the mostsignificant gamma-crystallin in adult eye lens tissue. Whether dueto aging or mutations in specific genes, gamma-crystallins havebeen involved in cataract formation. [provided by RefSeq, Jul2008].

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-12860R-CY5)

Proveedor: Bioss

Descripción: Crystallins are separated into two classes:taxon-specific, or enzyme, and ubiquitous. The latter classconstitutes the major proteins of vertebrate eye lens and maintainsthe transparency and refractive index of the lens. Since lenscentral fiber cells lose their nuclei during development, thesecrystallins are made and then retained throughout life, making themextremely stable proteins. Mammalian lens crystallins are dividedinto alpha, beta, and gamma families; beta and gamma crystallinsare also considered as a superfamily. Alpha and beta families arefurther divided into acidic and basic groups. Seven protein regionsexist in crystallins: four homologous motifs, a connecting peptide,and N- and C-terminal extensions. Gamma-crystallins are ahomogeneous group of highly symmetrical, monomeric proteinstypically lacking connecting peptides and terminal extensions. Theyare differentially regulated after early development. This geneencodes a protein initially considered to be a beta-crystallin butthe encoded protein is monomeric and has greater sequencesimilarity to other gamma-crystallins. This gene encodes the mostsignificant gamma-crystallin in adult eye lens tissue. Whether dueto aging or mutations in specific genes, gamma-crystallins havebeen involved in cataract formation. [provided by RefSeq, Jul2008].

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-12860R-HRP)

Proveedor: Bioss

Descripción: Crystallins are separated into two classes:taxon-specific, or enzyme, and ubiquitous. The latter classconstitutes the major proteins of vertebrate eye lens and maintainsthe transparency and refractive index of the lens. Since lenscentral fiber cells lose their nuclei during development, thesecrystallins are made and then retained throughout life, making themextremely stable proteins. Mammalian lens crystallins are dividedinto alpha, beta, and gamma families; beta and gamma crystallinsare also considered as a superfamily. Alpha and beta families arefurther divided into acidic and basic groups. Seven protein regionsexist in crystallins: four homologous motifs, a connecting peptide,and N- and C-terminal extensions. Gamma-crystallins are ahomogeneous group of highly symmetrical, monomeric proteinstypically lacking connecting peptides and terminal extensions. Theyare differentially regulated after early development. This geneencodes a protein initially considered to be a beta-crystallin butthe encoded protein is monomeric and has greater sequencesimilarity to other gamma-crystallins. This gene encodes the mostsignificant gamma-crystallin in adult eye lens tissue. Whether dueto aging or mutations in specific genes, gamma-crystallins havebeen involved in cataract formation. [provided by RefSeq, Jul2008].

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-12860R-FITC)

Proveedor: Bioss

Descripción: Crystallins are separated into two classes:taxon-specific, or enzyme, and ubiquitous. The latter classconstitutes the major proteins of vertebrate eye lens and maintainsthe transparency and refractive index of the lens. Since lenscentral fiber cells lose their nuclei during development, thesecrystallins are made and then retained throughout life, making themextremely stable proteins. Mammalian lens crystallins are dividedinto alpha, beta, and gamma families; beta and gamma crystallinsare also considered as a superfamily. Alpha and beta families arefurther divided into acidic and basic groups. Seven protein regionsexist in crystallins: four homologous motifs, a connecting peptide,and N- and C-terminal extensions. Gamma-crystallins are ahomogeneous group of highly symmetrical, monomeric proteinstypically lacking connecting peptides and terminal extensions. Theyare differentially regulated after early development. This geneencodes a protein initially considered to be a beta-crystallin butthe encoded protein is monomeric and has greater sequencesimilarity to other gamma-crystallins. This gene encodes the mostsignificant gamma-crystallin in adult eye lens tissue. Whether dueto aging or mutations in specific genes, gamma-crystallins havebeen involved in cataract formation. [provided by RefSeq, Jul2008].

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-12876R-CY7)

Proveedor: Bioss

Descripción: POU domain proteins contain a bipartite DNA-binding domain divided by a flexible linker that enables them to adopt various monomer configurations on DNA. The versatility of POU protein operation is additionally conferred at the dimerization level. The POU dimer from the OCT1 gene formed on the palindromic OCT factor recognition element, or PORE (ATTTGAAATGCAAAT), could recruit the transcriptional coactivator OBF1. Studies of tissue-specific expression of immunoglobulin promoters demonstrate the importance of an octamer, ATTTGCAT, and the proteins that bind to it. This is a regulatory element important for tissue- and cell-specific transcription as well as for transcription of a number of housekeeping genes. Oct-1 encodes one protein, NF-A1, which is found in nuclear extracts from all cell types and thus is not specific to lymphoid cells as is the protein NF-A2, which is encoded by Oct-2. A novel protein designated Bob 1 (B cell Oct binding protein 1), alternatively called OBF-1, specifically interacts with Oct-1 and Oct-2, enhancing their transcriptional efficacy. Bob 1 is expressed at highest levels in spleen and peripheral blood leukocytes and represents an Oct co-factor capable of conferring cell-specific activation of Oct-1 and Oct-2. Although having no intrinsic capacity for DNA binding, Bob 1 associates tightly with the octamer motif in the presence of Oct-1 and/or Oct-2. The gene which encodes Bob 1 maps to human chromosome 11q23.1.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (BOSSBS-7719R-A680)

Proveedor: Bioss

Descripción: DNA helicase involved in cellular proliferation. Possesses DNA-dependent ATPase and helicase activities. This helicase translocates on single-stranded DNA in the 5' to 3' direction in the presence of ATP and, to a lesser extent, dATP. Its unwinding activity requires a 5'-single-stranded region for helicase loading, since flush-ended duplex structures do not support unwinding. The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended to 500 bp by RPA or the cohesion establishment factor, the Ctf18-RFC (replication factor C) complex activities. Stimulates the flap endonuclease activity of FEN1. Required for normal sister chromatid cohesion. Required for recruitement of bovine papillomavirus type 1 regulatory protein E2 to mitotic chrmosomes and for viral genome maintenance. Required for maintaining the chromosome segregation and is essential for embryonic development and the prevention of aneuploidy. May function during either S, G2, or M phase of the cell cycle. Binds to both single- and double-stranded DNA.Tissue specificity: Highly expressed in spleen, B-cells, thymus, testis, ovary, small intestine, and pancreas. Very low expression seen in the brain. Expressed in dividing cells and/or cells undergoing high levels of recombination. No expression is seen in cells signaled to terminally differentiate. Expressed in keratinocyte growth factor-stimulated cells but not in serum, EGF and IL1-beta-treated keratinocytes.

UOM: 1 * 100 µl

Promoción

Numero del catalogo: (PRSI3467)

Proveedor: ProSci Inc.

Descripción: Caspase-7 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-7 is an executioner caspase that was identified based on its homology with caspases 1 and 3, as well as the C. elegans cell death protein CED-3. Alternative splicing of Caspase-7 mRNA results in the production of 3 distinct isoforms. Caspase-7 activity can be directly inhibited by XIAP expression.

UOM: 1 * 100 µG

Promoción

Numero del catalogo: (PRSI3475)

Proveedor: ProSci Inc.

Descripción: Caspase-8 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-8 is an initiator caspase that was identified as a member of the Fas/APO-1 death-inducing signaling complex. The adaptor molecule FADD couples procaspase-8 to the Fas receptor death domain; subsequent oligomerization promotes procaspase-8 autoactivation. FLIP, a catalytically inactive caspase-8-like molecule inhibits these interactions and thus can inhibit apoptosis. This antibody will only detect isoform E of caspase-8.

UOM: 1 * 100 µG

Promoción

Proveedor: Corning

Descripción: Cajas de policarbonato reutilizables.

Certificados

Proveedor: HEATHROW

Descripción: These reagent reservoirs offer a fresh and modern design with enhanced features to streamline pipetting procedures. They are designed for multi-channel pipettes and accommodate most common brands. A full range of volumes and styles is available to accommodate required volume of reagents and reduce waste.

Numero del catalogo: (PRSI92-471)

Proveedor: ProSci Inc.

Descripción: Ephrin type-B receptor 2(EPHB2) belongs to the protein kinase superfamily and Ephrin receptor subfamily. EPHB2 contains 1 Eph LBD domain, 2 fibronectin type-III domains, 1 protein kinase domain and 1 SAM domain. Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family.

UOM: 1 * 50 µG

Promoción

Numero del catalogo: (PRSI5987)

Proveedor: ProSci Inc.

Descripción: KPNA4 Antibody: Karyopherin, a cytosolic and heterodimeric protein complex consisting of alpha and beta subunits, is responsible for targeting proteins with nuclear localization signals to the nuclear pore complex by an energy requiring, Ran-dependent mechanism. The alpha subunit and imported substrate enter the nucleus and accumulate in the nucleoplasm, while the beta subunit accumulates at the NPC. Molecules containing the classical nuclear localization signal (NLS) are transported into the nucleus by alpha/beta heterodimers. KPNA3 has been shown to be important in the TNF-alpha -induced nuclear import of NF-kappa B. It is also involved in the stress-mediated nuclear stabilization of p53 and the nuclear import and replication of HIV-1 in both dividing and non-dividing cells.

UOM: 1 * 100 µG

Promoción

Numero del catalogo: (GLWAB175B)

Proveedor: GLW

Descripción: Estas cajas criogénicas están diseñadas para tubos de ensayo de 5,0 ml y tubos eppendorf® (5,0 ml).

UOM: 1 * 1 UN

Promoción