124512 Results for: "3+ml+k2edta"

Supplier: Biosensis

Apolipoprotein E (ApoE) is a lipoprotein involved in fat metabolism and acts as cholesterol carrier between cells and across tissues. On a genetic level, three APOE alleles are described, APOE2, APOE3 and APOE4. These alleles give rise to six APOE isoforms, which are differentially implicated in various diseases. In the peripheral system, APOE4 is linked to increased risk of atherosclerosis. In the CNS, the ability of APOE4 in clearing beta-amyloid is impaired, while APOE3 and APOE2 are more efficient in performing this task. The APOE4 genotype in particular has been linked to increased risk for developing Alzheimer's Disease.

Supplier: ReVacc Scientific

This pseudotyped virus uses recombinant Vesicular Stomatitis Virus (rVSV) to carry the S protein mutated from D (Asp) to G (Gly) at site of 614 of SARS-CoV-2 (GenBank: MN908947), with 18-aa cytoplasmic tail truncation for optimal infection.

Supplier: Rockland Immunochemical

Inaba et al. (1992) used murine cDNA clones for 3 cyclin D genes that are normally expressed during the G1 phase of the cell cycle to clone the cognate human genes. D-type cyclins (cyclins D1, D2, and D3) are regarded as essential links between cell environment and the core cell cycle machinery. cyclin D2(CCND2) gene ia assigned to 12p13. This antibody is suitable for researchers interested in cancer research, autoimmune disease, neurodegenerative disease, MAP Kinase Signaling, AKT Signaling, Ubiquitin research, and Cell Cycle research.

Supplier: Prosci

The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator.The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Prosci

FBXO8 is a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. FBXO8 belongs to the Fbxs class. It contains a C-terminal amino acid sequence that bears a significant similarity with a portion of yeast Sec7p, a critical regulator of vesicular protein transport. This human protein may interact with ADP-ribosylation factor (s) (ARFs) and exhibit ARF-GEF (guanine nucleotide exchange factor) activity.This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. It contains a C-terminal amino acid sequence that bears a significant similarity with a portion of yeast Sec7p, a critical regulator of vesicular protein transport. This human protein may interact with ADP-ribosylation factor (s) (ARFs) and exhibit ARF-GEF (guanine nucleotide exchange factor) activity.

Supplier: Prosci

PTBP1 belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. This protein binds to the intronic polypyrimidine tracts that requires pre-mRNA splicing and acts via the protein degradation ubiquitin-proteasome pathway. It may also promote the binding of U2 snRNP to pre-mRNAs.This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has four repeats of quasi-RNA recognition motif (RRM) domains that bind RNAs. This protein binds to the intronic polypyrimidine tracts that requires pre-mRNA splicing and acts via the protein degradation ubiquitin-proteasome pathway. It may also promote the binding of U2 snRNP to pre-mRNAs. This protein is localized in the nucleoplasm and it is also detected in the perinucleolar structure. Alternatively spliced transcript variants encoding different isoforms have been described.

Supplier: Prosci

RXRB is a member of the retinoid X receptor (RXR) family of nuclear receptors which are involved in mediating the effects of retinoic acid (RA). This receptor forms homodimers with the retinoic acid, thyroid hormone, and vitamin D receptors, increasing both DNA binding and transcriptional function on their respective response elements. This gene encodes a member of the retinoid X receptor (RXR) family of nuclear receptors which are involved in mediating the effects of retinoic acid (RA). This receptor forms homodimers with the retinoic acid, thyroid hormone, and vitamin D receptors, increasing both DNA binding and transcriptional function on their respective response elements. The gene lies within the major histocompatibility complex (MHC) class II region on chromosome 6. An alternatively spliced transcript variant has been described, but its full length sequence has not been determined. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.This gene encodes a member of the retinoid X receptor (RXR) family of nuclear receptors which are involved in mediating the effects of retinoic acid (RA). This receptor forms homodimers with the retinoic acid, thyroid hormone, and vitamin D receptors, increasing both DNA binding and transcriptional function on their respective response elements. The gene lies within the major histocompatibility complex (MHC) class II region on chromosome 6. An alternatively spliced transcript variant has been described, but its full length sequence has not been determined. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Prosci

SSB is involved in diverse aspects of RNA metabolism, including binding and protecting 3-prime UUU (OH) elements of newly RNA polymerase III-transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs associated with hepatitis C virus. SSB protein was originally defined by its reactivity with autoantibodies from patients with Sjogren syndrome and systemic lupus erythematosus.La is involved in diverse aspects of RNA metabolism, including binding and protecting 3-prime UUU (OH) elements of newly RNA polymerase III (see MIM 606007)-transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs associated with hepatitis C virus. La protein was originally defined by its reactivity with autoantibodies from patients with Sjogren syndrome (MIM 270150) and systemic lupus erythematosus La is involved in diverse aspects of RNA metabolism, including binding and protecting 3-prime UUU (OH) elements of newly RNA polymerase III (see MIM 606007)-transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs associated with hepatitis C virus. La protein was originally defined by its reactivity with autoantibodies from patients with Sjogren syndrome (MIM 270150) and systemic lupus erythematosus (SLE; MIM 152700) (Teplova et al., 2006 [PubMed 16387655]).[supplied by OMIM]. Sequence Note: removed 1 base from the 3' end that did not align to the reference genome assembly. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications. PRIMARYREFSEQ_SPAN PRIMARY_IDENTIFIER PRIMARY_SPAN COMP 1-1673 BC020818.1 1-1673

Supplier: Prosci

TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. TAF6 is one of the smaller subunits of TFIID that binds weakly to TBP but strongly to TAF1,the largest subunit of TFIID. One of the isoforms has been shown to preclude binding of one of the other TFIID subunits, thereby reducing transcription and initiating signals that trigger apoptosis.Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the smaller subunits of TFIID that binds weakly to TBP but strongly to TAF1, the largest subunit of TFIID. Four isoforms have been identified but complete transcripts have been determined for only three isoforms. One of the isoforms has been shown to preclude binding of one of the other TFIID subunits, thereby reducing transcription and initiating signals that trigger apoptosis.

Supplier: Prosci

SPRY2 is a protein belonging to the sprouty family. It contains a carboxyl-terminal cysteine-rich domain essential for the inhibitory activity on receptor tyrosine kinase signaling proteins and is required for growth factor stimulated translocation of the protein to membrane ruffles. In primary dermal endothelial cells this gene is transiently upregulated in response to fibroblast growth factor two. SPRY2 is indirectly involved in the non-cell autonomous inhibitory effect on fibroblast growth factor two signaling. The protein interacts with Cas-Br-M (murine) ectropic retroviral transforming sequence, and can function as a bimodal regulator of epidermal growth factor receptor/mitogen-activated protein kinase signaling. SPRY2 may play a role in alveoli branching during lung development as shown by a similar mouse protein.This gene encodes a protein belonging to the sprouty family. The encoded protein contains a carboxyl-terminal cysteine-rich domain essential for the inhibitory activity on receptor tyrosine kinase signaling proteins and is required for growth factor stimulated translocation of the protein to membrane ruffles. In primary dermal endothelial cells this gene is transiently upregulated in response to fibroblast growth factor two. This protein is indirectly involved in the non-cell autonomous inhibitory effect on fibroblast growth factor two signaling. The protein interacts with Cas-Br-M (murine) ectropic retroviral transforming sequence, and can function as a bimodal regulator of epidermal growth factor receptor/mitogen-activated protein kinase signaling. This protein may play a role in alveoli branching during lung development as shown by a similar mouse protein. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Biotix

Biotix disposable reagent reservoirs are designed for use in multi-channel pipetting applications and can accommodate up to 12-channel pipettors. Angled sides and a V-shaped bottom allow for maximum recovery of reagents. All reservoirs feature internal graduated volume lines and pour-spouts on the corners. Choose from opaque white polyvinyl chloride (PVC) or high clarity polystyrene (PS) in several packaging configurations.

Supplier: Adipogen

Alcian blue 8GX is primarily used for demonstrating acid mucopolysaccharides, which it does quite selectively. In recent years there has been some difficulty obtaining the dye. Alcian Blue 8GX is also suitable for detection of glycoproteins on nitrocellulose and in PAGE gels. There are other dyes similar to alcian blue, although not necessarily belonging to the same class of dyes. Alcian green has gained some popularity, and alcian yellow has been suggested, especially in a method for demonstrating Helicobacter. They are used for acid mucopolysaccharides in the same way as alcian blue. They have no particular advantage for demonstrating mucin. According to the Merck Index the groups marked X split off during staining.

Supplier: STEMCELL Technologies

Thrombopoietin (TPO) is a key regulator of megakaryocytopoiesis and thrombopoiesis in vitro and in vivo. TPO stimulates the proliferation and maturation of megakaryocytes and has an important role in regulating the level of circulating platelets in vivo (Bartley et al.; de Sauvage et al.; Foster et al.; Sohma et al.). TPO also promotes the survival, self-renewal, and expansion of hematopoietic stem cells and primitive multilineage progenitor cells. It is commonly used with other cytokines such as stem cell factor (SCF) and Flt3/Flk-2 ligand to promote expansion of primitive hematopoietic cells in culture (Hitchcock and Kaushansky). The TPO receptor, c-Mpl, is expressed at all stages of megakaryopoiesis, from hematopoietic stem and progenitor cells to mature platelets (Ng et al.).

Supplier: Genetex

TRF2 is a ubiquitously expressed protein that is implicated in the control of telomere length. TRF2, like TRF1, contains a Myb-related DNA binding motif. It binds to duplex TTAGGG repeats and is localized to all human telomeres in metaphase chromosomes. TRF2 is thought to protect chromosome ends by maintaining the correct structure at telomere termini. The use of mutant forms of TRF2 has implicated a role for TRF2 in the prevention of senescence in primary human cells. Recently, it has been shown that inhibition of TRF2 resulted in apoptosis in a subset of mammalian cell types.

Supplier: Prosci

RC3H1 Antibody: The ring finger protein RC3H1, also known as Roquin, is a highly conserved member of the RING type ubiquitin ligase protein family whose M199R mutation leads to the excessive production of follicular helper T cells and germinal centers in the sanroque strain of mice, a strain with excessive IL-21 production and high titers of autoantibodies. The complete loss of RC3H1 induces early death and immune deregulation but not autoimmunity in RC3H1-null mice, suggesting that the mutant RC3H1 is more disruptive to the immune system than its complete loss.

Supplier: Prosci

TLX1 Antibody: The Hox proteins play a role in patterns of embryonic development and cellular differentiation by regulating downstream target genes. TLX1, also called homeobox11 (HOX11), as it is located outside of the four mammalian Hox clusters, is a DNA-binding nuclear transcription factor. TLX1 encodes a homeobox-domain containing protein and is containing a glycine and proline-rich amino terminus. TLX1 is required for maintenance of the developing spleen and cell survival. TLX1 is highly expressed in T-cell leukemia and lymphoid neoplasias as a result of translocation. TLX1-deficient mice have no spleen.

Supplier: Prosci

The THAP domain-contining protein 11 (THAP11), also known as Ronin, is an essential factor involved in embryonic stem (ES) cell pluripotency and cell growth. THAP 11 contains a THAP domain, a conserved DNA-binding domain common to many proteins associated with chromatin modification and gene expression silencing, and has striking similarity to the site-specific DNA-binding domain (DBD) of Drosophila P element transposases. THAP11 can also negatively regulate CD44 v6 expression through its interaction with the poly(rC) binding protein PCBP1.

Supplier: Prosci

KHDC1 Antibody: KHDC1 family members are K-homology (KH) domain-containing RNA binding proteins that are involved in various aspects of RNA metabolism, ranging from transcription to RNA splicing, transportation, translation, and stability. KHDC1 is highly expressed in oocytes and interacts with cytoplasmic polyadenylation element-binding protein 1 (CPEB1), a key translational regulator controlling the polyA length of mRNAs. KHDC1 functions as a global translational repressor and induces apoptosis through an ER-dependent signaling pathway and that the C-terminal putative trans-membrane motif (TMM) is critical for its activities.

Supplier: Rockland Immunochemical

AIMP2 was initially identified as a part of an aminoacyl-tRNA synthesase complex (1). It was later discovered to be a cofactor and substrate of Parkin, a Ring-type E3 ubiquitin ligase that is important for the survival of dopamine neurons in Parkinson’s disease; accumulation of AIMP2 in these cells lead to catecholaminergic cell death (2). AIMP2 can also bind to TRAF2, a key player in the TNF-alpha signaling pathway, causing the ubiquitination of TRAF2 by cIAP1, leading to TNF-alpha-dependent apoptosis (3). Finally, AIMP2 has been suggested to function as a tumor suppressor (4).

Supplier: Rockland Immunochemical

Calcineurin, the Ca(2+)/calmodulin-regulated protein phosphatase, first detected in skeletal muscle and brain, has been found in all cells from yeast to mammals. Calcineurin A alpha (PPP3CA),is located on human chromosomes 4, Chromosomal mapping of the human genes for the calmodulin-dependent protein phosphatase (calcineurin) catalytic subunit. Calcineurin regulates bone formation by the osteoblast. This antibody is suitable for researchers interested in apoptosis, transcription factors, nuclear receptors, cancer research, Immune Response, cardiovascular disease, MAK Kinase Signaling, and AKT Signaling.

Supplier: MP Biomedicals

100× Non-essential Amino Acids for Minimum Essential Medium Eagle Contains 19 amino acids. The essential amino acids and the non-essential amino acids; L-ala; L-asn; L-asp; L-glu; L-gly; L-pro and L-ser.

Supplier: Electron Microscopy Sciences

In-Situ mounting medium is a unique mounting medium designed for permanent preservation of tissue sections and cell smear with alkaline phosphatase chromogens like NBT/BCIP and red stain. It is ideal for mounting tissues and cell smears.

Supplier: STEMCELL Technologies

Semi-solid methylcellulose-based hybridoma selection and cloning medium without HAT (serum-containing).

Supplier: Globe Scientific

These 24-hour urine collection containers offer sizes, configurations and features required to meet most 24-hour collection needs.

Supplier: Leica Microsystems

The Leica DM500 microscope is a user-friendly educational tool, perfect for classrooms. It provides clear imaging, fostering a deeper understanding of the microscopic world for students. Designed for educational institutions seeking a reliable and versatile microscope.

Supplier: VistaLab

Revolutionary ergonomic design addresses the issues of posture, repetition, and force to significantly reduce strain and pain that occur from pipetting.

Supplier: Jackson Immunoresearch Lab

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The whole IgG form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on antigen-binding assay and/or ELISA, the antibody reacts with the Fc portion of mouse IgG2c but not with other mouse IgG subclasses, mouse IgM, or the Fab portion of mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and rabbit serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The whole IgG form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with the Fc portion of human IgG heavy chain but not with the Fab portion of human IgG. No antibody was detected against human IgM or IgA, or against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine, horse and mouse serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The whole IgG form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on immunoelectrophoresis and/or ELISA, the antibody reacts with whole molecule goat IgG. It also reacts with the light chains of other goat immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine, chicken, guinea pig, syrian hamster, horse, human, mouse, rabbit and rat serum proteins, but it may cross-react with immunoglobulins from other species.

Supplier: Jackson Immunoresearch Lab

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The whole IgG form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective. Based on antigen-binding assay and/or ELISA, the antibody reacts with the Fc portion of mouse IgG3 but not with other mouse IgG subclasses, mouse IgM, or the Fab portion of mouse immunoglobulins. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with human, bovine and rabbit serum proteins, but it may cross-react with immunoglobulins from other species.