You Searched For: xpect

Catalog Number: (89336-098)

Supplier: Genetex

Description: Rabbit anti-Bovine IgG Polyclonal antibody

Catalog Number: (10073-060)

Supplier: Prosci

Description: Wnt-7a belongs to the Wnt family of signaling proteins that play a key role in maintaining the integrity of embryonic and adult tissues. It is expressed in placenta, kidney, testis, uterus, fetal lung and fetal and adult brain. Most Wnt proteins can signal though a mechanism called the canonical Wnt pathway, in which Wnt proteins bind to and activate seven-pass transmembrane receptors of the Frizzled family ultimately leading to the disruption of β-Catenein degradation. Intracellular accumulation of β-Catenin increases translocation of the protein into the nucleus where it binds to TCF/LEF transcription factors and induces the expression of numerous genes. Increased Wnt/β-Catenein signaling is associated with tumorigenesis in a diverse set of human cancers. However, Wnt-7a/Frizzled-9 signaling has been shown to act as a tumor suppressor in non-small cell lung cancers. Recombinant human Wnt-7a is a 35.5 kDa glycoprotein containing 318 amino acids. Due to glycosylation, Wnt-7a migrates between 40-55 kDa by SDS-PAGE gel under unreduced conditions.

Catalog Number: (10072-912)

Supplier: Prosci

Description: TRAIL Receptor-1/DR4 and TRAIL Receptor-2/DR5 belong to the TNFR superfamily of transmembrane proteins and contain a cytoplasmic "death domain, " which can activate the cell's apoptotic machinery. These receptors are activated by binding to either membrane anchored or soluble TRAIL/Apo2L. Recombinant human soluble TRAIL Receptor-1/DR4 is a 22.7 kDa protein (215 amino acid residues) consisting of the TNFR homologous, cysteine rich portion of the extracellular domain.

Catalog Number: (10072-534)

Supplier: Prosci

Description: Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Glu-C cleaves at the Carboxyl side of E (can also cleave D under certain conditions). Recombinant Staphylococcus Glu-C is a 28.8 kDa protease consisting of 266 amino acid residues.

Catalog Number: (10072-666)

Supplier: Prosci

Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solublization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in liver and brain and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. It’s interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Compared with E3 and E4, E2 exhibits the lowest receptor binding affinity. E2 allele carriers had significantly lower levels of total cholesterol, low-density lipoprotein cholesterol, and non-high-density lipoprotein cholesterol, as well as increased ApoE levels. Recombinant human ApoE2 is a 34.3 kDa protein containing 300 amino acid residues.

Supplier: Globe Scientific

Description: Diamond® RealSeal™ Plastic Laboratory Bottles from Globe Scientific meet the requirements of the most demanding applications. Rugged and durable, these bottles are a safe, shatterproof alternative to glass bottles for collection, storage, or shipping samples, media, and reagents.

Supplier: Prosci

Description: IL-5 is a hematopoietic growth factor that stimulates the proliferation and activation of eosinophils. Produced by mast cells, T cells, and eosinophils, IL-5 plays an important role in inducing cell-mediated immunity against parasitic infections and certain tumors. Elevated levels of IL-5 lead to Eosinophilia, which may result in the induction of asthma and other allergic diseases. Human and murine IL-5 is cross-species reactive. Recombinant human IL-5 is a 26.0 kDa disulfide-linked homodimeric protein containing two 116 amino acid chains. Recombinant rat IL-5 is a 26.0 kDa disulfide-linked homodimeric protein containing two 113 amino acid chains. Recombinant murine IL-5 is a 26.2 kDa disulfide-linked homodimeric protein containing two 113 amino acid chains.

Supplier: SPEX SAMPLE PREP LLC MS

Description: Accessories for Spex SamplePrep Mills, Presses, and Homogenizers, Spec Caps - Vials and Vial Sets

Catalog Number: (10451-500)

Supplier: Bioss

Description: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.

Catalog Number: (10451-514)

Supplier: Bioss

Description: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.

Catalog Number: (10451-504)

Supplier: Bioss

Description: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.

Catalog Number: (10451-516)

Supplier: Bioss

Description: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.

Catalog Number: (10072-246)

Supplier: Prosci

Description: CNTF is a potent neural factor that was originally characterized as a vital factor for the survival of chick ciliary neurons in vitro. CNTF is also important for the survival of other neural cell types including primary sensory neurons, motor neurons, basal forebrain neurons and type 2 astrocytes. CNTF is highly conserved across species and exhibits cross-species bioactivity. Both human and rat Recombinant CNTF are synthesized as a 199 amino acid polypeptide (22.7 kDa) lacking a hydrophobic N-terminal signal for secretion.

Catalog Number: (10072-928)

Supplier: Prosci

Description: OX40L, a member of the TNF superfamily of structurally related proteins, exists primarily as a type II membrane bound, non-covalently linked homotrimeric protein. It is expressed on antigen presenting cells (APCs), such as dendritic cells and activated B-cells, and also on various other cells such as vascular endothelial cells, mast cells, and natural killer cells. OX40L signals specifically through the OX40 receptor, which is expressed predominantly on CD4+T cells but also on certain activated CD8+T cells. OX40/OX40L functions as a costimulatory signal, which is required for a productive interaction between antigen presenting cells and their target T-cells. It enhances cell proliferation and survival, and increases expression of RANTES, IL-2, IL-3, and IFNγ. OX40/OX40L signaling plays an important role in immuno-regulatory communication, enabling the immune system to distinguish between "friend vs. foe” during activation; a mechanism typically termed immuno-tolerance. Recombinant OX40L is a glycosylated 133 amino acid protein corresponding to the extracellular TNF homologous domain of the full length transmembrane protein. It migrates with an apparent molecular mass of 15.5 - 25.0 kDa on SDS-PAGE.

Catalog Number: (10072-906)

Supplier: Prosci

Description: BAFF Receptor (BAFFR), a member of the TNFR superfamily, is highly expressed in spleen, lymph node, and resting B cells and to some extent in activated B cells, resting CD4+ cells and peripheral blood leukocytes. BAFFR is a type III transmembrane protein that binds with high specificity to BAFF (TNFSF13B). BAFFR/BAFF signaling plays a critical role in B cell survival and maturation. Recombinant human BAFFR is a 76 amino acid polypeptide (7.7 kDa) corresponding to the extracellular portion of the full BAFFR protein.

Catalog Number: (470028-890)

Supplier: JAROSLAW KUDAY

Description: Enhance Your Lessons and Labs with Full Color Digital Images.