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Image Unavailable-10671-480

Anti-IQCG Rabbit Polyclonal Antibody (Cy5.5®)

Catalog Number: (10671-480)
Supplier: Bioss
Description: IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.
Image Unavailable-10671-482

Anti-IQCG Rabbit Polyclonal Antibody (Cy7®)

Catalog Number: (10671-482)
Supplier: Bioss
Description: IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.
Image Unavailable-10671-478

Anti-IQCG Rabbit Polyclonal Antibody (Cy5®)

Catalog Number: (10671-478)
Supplier: Bioss
Description: IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.
Image Unavailable-10774-430

Human Recombinant IGF-BP4 (from (BTI-Tn-5B1-4) Hi-5 Insect cells)

Supplier: Peprotech
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF-independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant Human IGF-BP4 is a 25.7 kDa protein consisting of 237 amino acid residues including, the IGF-BP domain and thyroglobulin type-I domain.

Image Unavailable-10072-930

Human Recombinant IGFBP4

Catalog Number: (10072-930)
Supplier: Prosci
Description: IGF-BPs control the distribution, function and activity of IGFs in various cell tissues and body fluids. IGF-BP4 is the major IGF-BP produced by osteoblasts, and is also found in the epidermis, ovarian follicles, and other tissues. IGF-BP4 inhibits the activity of IGF-I and IGF-II by binding in a manner that results in the formation of complexes with reduced ability to signal through cell surface IGF receptors. IGF-BP4 can inhibit the growth of chick pelvis cartilage and HT29 colon adenocarcinoma cells by blocking the mitogenic actions of IGFs, and has also been shown to reduce colony formation by colorectal cancer cells via an IGF independent pathway. The biological effects of IGF-BP4 can be regulated by Pregnancy Associated Plasma Protein A (PAPP-A), which reduces IGF-BP4/IGF binding affinity by proteolytically cleaving IGF-BP4. The modulation of IGF-BP4 activity by PAPP-A is an important component in the regulation of ovarian folliculogenesis and in the growth inhibition of responding ovarian cancer cells. Recombinant human IGF-BP4 is a 25.8 kDa protein consisting of 237 amino acid residues including the IGF-BP domain and thyroglobulin type-I domain.
Image Unavailable-10429-358

Anti-FGFRL1 Rabbit Polyclonal Antibody (Cy5®)

Catalog Number: (10429-358)
Supplier: Bioss
Description: FGFRL1 is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. A marked difference between FGFRL1 and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found.
Product Image-10093-222

Anti-RAB6B Rabbit Polyclonal Antibody

Catalog Number: (10093-222)
Supplier: Proteintech
Description: The human RAB genes share structural and biochemical properties with the Ras gene superfamily. Accumulating data suggests an important role for RAB proteins either in endocytosis or in biosynthetic protein transport. The transport of newly synthesized proteins from endoplasmic reticulum to the Golgi complex and to secretory vesicles involves the movement of carrier vesicles, a process that appears to involve RAB protein function. Rab6A has been shown to be a regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Rab6B is encoded by an independent gene which is located on chromosome 3 region q21-q23. In contrast to Rab6A whose expression is ubiquitous, Rab6B is expressed in a tissue and cell-type specific manner. Rab6B is predominantly expressed in brain and the neuroblastoma cells. In brain, Rab6B was found to be specifically expressed in microglia, pericytes and Purkinje cells. Endogenous Rab6B localises to the Golgi apparatus and to ERGIC-53-positive vesicles. Comparable studies between Rab6A and Rab6B revealed distinct biochemical and cellular properties. Rab6B displays lower GTP-binding activities and is distributed over Golgi and ER membranes, whereas Rab6A is more restricted to the Golgi apparatus. Since the GTP-bound form of Rab6B does interact with all known Rab6A effectors, including Rabkinesin-6, the results suggest a cell-type specific role for Rab6B in retrograde membrane traffic at the level of the Golgi complex.
Product Image-77392-554

AASTY 6-55

Supplier: CUBE BIOTECH
Description: AASTYs (Acrylic acid-co-styrenes) - like AASTY 6-55 - are highly-alternating copolymers, well-suited for generating native lipid nanodiscs. They are a 2022 novel developed series for membrane protein solubilization & stabilization. AASTY 6-55 gets its name from its molecular weight and Acrylic Acid : Styrene Ratio. These varying ratios of acrylic acid to styrene contribute to the hydrophilic properties of our AASTYs. In general, lighter AASTYs, like 6-55 tend to be more aggressive, while heavier AASTYs, such as 11-45 show higher thermodynamic stability.

The exact composition of AASTY copolymers shows different extraction efficiency, depending on the lipid composition of the lipid bilayers being formulated into nanodiscs. As AASTY is made by controlled radical polymerization techniques, the dispersity of polymer molecular weight distribution is low, and the molecular weights are controlled. This means that excess AASTY copolymer can be removed by dialysis after nanodisc formation. Based on previous findings on SMA, it is the expectation that AASTY of different molecular weights will display different rates of nanodisc formation, extraction efficacy, and stability of resulting nanodiscs.

Every membrane protein solubilization needs to undergo a screening process before. The characteristic phospholipid environment surrounding the different membrane proteins in question performs differently well with each polymer. To support you in this process, we offer a handy Screening Kit for AASTYs to test them all. Additionally, we recommend the two following publications if you would like to get further information: Smith et al. 2020 & Timcenko et al. 2022

Image Unavailable-77392-560

AASTY 11-55

Supplier: CUBE BIOTECH
Description: AASTYs (Acrylic acid-co-styrenes) - like AASTY 11-55 - are highly alternating copolymers, well-suited for generating native lipid nanodiscs. They are a 2022 novel developed series for membrane protein solubilization & stabilization. AASTY 11-55 is named from its molecular weight and Acrylic Acid : Styrene Ratio. These varying ratios of acrylic acid to styrene contribute to the hydrophilic properties of our AASTYs. In general lighter AASTYs, like 6-45 tend to be more aggressive, while heavier AASTYs, such as 11-55 show higher thermodynamic stability.

The exact composition of AASTY copolymers shows different extraction efficiencies, depending on the lipid composition of the lipid bilayers being formulated into nanodiscs. As AASTY is made by controlled radical polymerization techniques, the dispersity of polymer molecular weight distribution is low, and the molecular weights are controlled. This means that excess AASTY copolymer can be removed by dialysis after nanodisc formation. Based on previous findings on SMA, it is the expectation that AASTY of different molecular weights will display different rates of nanodisc formation, extraction efficacy, and stability of resulting nanodiscs.

Every membrane protein solubilization needs to undergo a screening process before. The characteristic phospholipid environment surrounding the different membrane proteins in question performs differently well with each polymer. To support you in this process we offer a handy Screening Kit for AASTYs to test them all. Additionally, we recommend the two following publications if you would like to get further information: Smith et al. 2020 & Timcenko et al. 2022

Image Unavailable-CAPIPA5-14651

Anti-FGFR2 Rabbit Polyclonal Antibody

Catalog Number: (CAPIPA5-14651)
Supplier: Thermo Scientific
Description: FGFR2 is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein consists of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. This particular family member is a high-affinity receptor for acidic, basic and/or keratinocyte growth factor, depending on the isoform. Mutations in the gene are associated with many craniosynostotic syndromes and bone malformations. The genomic organization of the gene encompasses 20 exons. Alternative splicing in multiple exons, including those encoding the Ig-like domains, the transmembrane region and the carboxyl terminus, results in varied isoforms which differ in structure and specificity. Isoform 1 has equal affinity for aFGF and bFGF but does not bind KGF.
Product Image-77392-528

AASTY 6-45

Supplier: CUBE BIOTECH
Description: AASTYs (Acrylic acid-co-styrenes) - like AASTY 6-45 - are highly alternating copolymers, well-suited for generating native lipid nanodiscs. They are a 2022 novel developed series for membrane protein solubilization & stabilization. AASTY 6-45 gets it's name from its molecular weight and Acrylic Acid : Styrene Ratio. These varying ratios of acrylic acid to styrene contribute to the hydrophilic properties of our AASTYs. In general lighter AASTYs, like 6-45 tend to be more aggressive, while heavier AASTYs, such as 11-45 show higher thermodynamic stability.

The exact composition of AASTY copolymers shows different extraction efficiency, depending on the lipid composition of the lipid bilayers being formulated into nanodiscs. As AASTY is made by controlled radical polymerization techniques, the dispersity of polymer molecular weight distribution is low, and the molecular weights are controlled. This means that excess AASTY copolymer can be removed by dialysis after nanodisc formation. Based on previous findings on SMA, it is the expectation that AASTY of different molecular weights will display different rates of nanodisc formation, extraction efficacy, and stability of resulting nanodiscs.

Every membrane protein solubilization needs to undergo a screening process before. The characteristic phospholipid environment surrounding the different membrane proteins in question performs differently well with each polymer. To support you in this process we offer a handy Screening Kit for AASTYs to test them all. Additionally, we recommend the two following publications if you would like to get further information: Smith et al. 2020 & Timcenko et al. 2022

Image Unavailable-77392-542

AASTY 6-50

Supplier: CUBE BIOTECH
Description: AASTYs (Acrylic acid-co-styrenes) - like AASTY 6-50 - are highly-alternating copolymers, well-suited for the generation of native lipid nanodiscs. They are a 2022 novel developed series for membrane protein solubilization & stabilization. AASTY 6-50 gets its name from its molecular weight and Acrylic Acid : Styrene Ratio. These varying ratios of acrylic acid to styrene contribute to the hydrophilic properties of our AASTYs. In general lighter AASTYs, like 6-50 tend to be more aggressive, while heavier AASTYs, such as 11-45 show higher thermodynamic stability.

The exact composition of AASTY copolymers shows different extraction efficiency, depending on the lipid composition of the lipid bilayers being formulated into nanodiscs. As AASTY is made using controlled radical polymerization techniques, the dispersity of polymer molecular weight distribution is low, and the molecular weights are controlled. This means that excess AASTY copolymer can be removed by dialysis after nanodisc formation. Based on previous findings on SMA, it is the expectation that AASTY of different molecular weights will display different rates of nanodisc formation, extraction efficacy, and stability of resulting nanodiscs.

Every membrane protein solubilization needs to undergo a screening process before. The characteristic phospholipid environment surrounding the different membrane proteins in question performs differently well with each polymer. To support you in this process we offer a handy Screening Kit for AASTYs to test them all. Additionally, we recommend the two following publications if you would like to get further information: Smith et al. 2020 & Timcenko et al. 2022

Image Unavailable-77392-534

AASTY 11-45

Supplier: CUBE BIOTECH
Description: AASTYs (Acrylic acid-co-styrenes) - like AASTY 11-45 - are highly alternating copolymers, well-suited for the generation of native lipid nanodiscs. They are a 2022 novel developed series for membrane protein solubilization & stabilization. AASTY 11-45 gets its name from its molecular weight and Acrylic Acid : Styrene Ratio. These varying ratios of acrylic acid to styrene contribute to the hydrophilic properties of our AASTYs. In general lighter AASTYs, like 6-45 tend to be more aggressive, while heavier AASTYs, such as 11-45 show higher thermodynamic stability.

The exact composition of AASTY copolymers shows different extraction efficiency, depending on the lipid composition of the lipid bilayers being formulated into nanodiscs. As AASTY is made by controlled radical polymerization techniques, the dispersity of polymer molecular weight distribution is low, and the molecular weights are controlled. This means that excess AASTY copolymer can be removed by dialysis after nanodisc formation. Based on previous findings on SMA, it is the expectation that AASTY of different molecular weights will display different rates of nanodisc formation, extraction efficacy, and stability of resulting nanodiscs.

Every membrane protein solubilization needs to undergo a screening process before. The characteristic phospholipid environment surrounding the different membrane proteins in question performs differently well with each polymer. To support you in this process, we offer a handy Screening Kit for AASTYs to test them all. Additionally, we recommend the two following publications if you would like to get further information: Smith et al. 2020 & Timcenko et al. 2022

Product Image-10102-592

Anti-CLEC4M Rabbit Polyclonal Antibody

Catalog Number: (10102-592)
Supplier: Prosci
Description: CLEC4M is a transmembrane receptor and is often referred to as L-SIGN because of its expression in the endothelial cells of the lymph nodes and liver. It is involved in the innate immune system and recognizes numerous evolutionarily divergent pathogens ranging from parasites to viruses, with a large impact on public health. The protein is organized into three distinct domains: an N-terminal transmembrane domain, a tandem-repeat neck domain and C-type lectin carbohydrate recognition domain. The extracellular region consisting of the C-type lectin and neck domains has a dual function as a pathogen recognition receptor and a cell adhesion receptor by binding carbohydrate ligands on the surface of microbes and endogenous cells. The neck region is important for homo-oligomerization which allows the receptor to bind multivalent ligands with high avidity. Variations in the number of 23 amino acid repeats in the neck domain of this protein are common and have a significant impact on ligand binding ability. This gene is closely related in terms of both sequence and function to a neighboring gene (GeneID 30835; often referred to as DC-SIGN or CD209). DC-SIGN and L-SIGN differ in their ligand-binding properties and distribution. Alternative splicing results in multiple variants.This gene encodes a type II integral membrane protein that is 77% identical to CD209 antigen, a HIV gp120-binding protein. This protein, like CD209, efficiently binds both intercellular adhesion molecule 3 (ICAM3) and HIV-1 gp120, and enhances HIV-1 infection of T cells. This gene is mapped to 19p13.3, in a cluster with the CD209 and CD23/FCER2 genes. Multiple alternatively spliced transcript variants have been found for this gene, but the biological validity of some variants has not been determined.
Product Image-470228-484

ProPette™ Electronic Pipette Controller

Supplier: MTC BIO, INC.
Description: ProPette™ features an ergonomic body design, with computer-balanced weight distribution and low pressure fingertip control buttons that combine to provide a more comfortable pipetting experience.

Product Image-89358-864

Anti-SFPQ Mouse Monoclonal Antibody [clone: B92]

Catalog Number: (89358-864)
Supplier: Genetex
Description: The RNAs that direct protein synthesis in animals and plant cells are synthesized in the nucleus as large precursors (pre-mRNAs). The protein coding sequences in pre-mRNA molecules are arranged in discontinuous segments - exons interspersed with noncoding sequences - introns. In a process termed splicing, these introns are efficiently removed before the pre-mRNA is transported from the nucleus to the cytoplasm, where it is translated into protein. Studies have shown that nuclear pre-mRNA splicing takes place in a multi-component structure termed a spliceosome. The polypyrimidine tract-binding (PTB) protein-associated splicing factor (PSF), which plays an essential role in mammalian spliceosomes, is a ubiquitous nuclear matrix protein. A complex between PTB and PSF is necessary for pre-mRNA splicing. PSF contains two consensus RNA-binding domains and an unusual amino terminus rich in proline and glutamine residues. The RNA-binding properties of PSF are apparently identical to those of PTB. Both proteins, together and independently, bind the polypyrimidine tract of mammalian introns. However, the nuclear localization of PSF and PTB and their distribution in subnuclear fractions differ markedly: isolated nuclear matrices contain a bulk of PSF, but only minor amounts of PTB. In confocal microscopy both proteins appear in speckles, the majority of which do not co-localize. These PTB/PSF complexes, as well as the observed PSF-PTB interaction, may reflect the presence of PTB and PSF in spliceosomal complexes during RNA processing, although other data point to different cellular distribution and nuclear matrix association of the majority of PSF and PTB. The cleavage of PSF during lysis of immature myeloid cells is accompanied by digestion of the PTB splicing regulator but not other proteins tested. In contrast, during apoptosis PTB is degraded while PSF remains intact. Proteolytic degradation of PSF specifically occurs in intact myeloid cells and this process is enhanced upon immature myeloid cell lysis; PSF is completely cleaved to a 47 kDa proteolytic cleavage product (p47), due to potent proteolytic activity found in these cells but rare in other cells and tissues. Furthermore, p47 is abundant in intact normal and tumor myeloid cells while in other cell types it is undetectable. The bone marrow 47 kDa protein is a fragment constituting the N-terminal, protease-resistant half of the splicing factor PSF. PSF is highly basic and migrates anomalously on SDS gels. The 47 kDa protein of mouse cells of immature myeloid origin (bone marrow and acute myeloid leukemia) exhibits a gel migration pattern corresponding to a 49 kDa molecule. In other cell types such as lymphoid cells and in peripheral blood cells, PSF appears as approx. 100 kDa or 75 kDa molecules. The sequence of a fragment of mouse PSF was found to be remarkably similar to that of human PSF ( > 98% homology). Also, the sequences of PSF and the human (h) 100 kDa DNA-pairing protein (hPOMp100) reveals identity. Homologous pairing is a fundamental biological reaction implicated in various cellular processes such as DNA recombination and repair, chromosome pairing, sister chromatid cohesion and chromosome condensation, gene inactivation and initiation of replication. The base pairing is also involved in spliceosome assembly resulting in formation of a dynamic Holliday-like structure within which splicing occurs. Indeed, PSF/hPOMp100 bind both singlestranded (ss) and double-stranded (ds) DNA and facilitates the renaturation of complementary ssDNA molecules. Importantly, PSF/hPOMp100 promotes the formation of D-loops in superhelical duplex DNA. PSF/hPOMp100 also serves as an efficient substrate for protein kinase C (PKC) in vitro. PKC phosphorylation of PSF/hPOMp100 stimulates its DNA binding and D-loop formation activity suggesting a possible regulatory mechanism. PSF has been demonstrated to interact with a variety of cellular targets including the human pro-oncoproteins EWS, hPOMp75/TLS and calmodulin, the RNA/DNAbinding nuclear protein p54nrb/NonO (the homolog of PSF) and DNA topoisomerase. A direct interaction has been observed, between PSF and topoisomerase I which has been implied in DNA recombination, DNA repair, and chromosome formation and may act as a transcription factor and a protein kinase. PSF is also expressed by differentiating neurons in developing mouse brain. Both the expression of PSF mRNA in cortex and cerebellum and PSF immunoreactivity in all brain areas has been found to be high during embryonic and early postnatal life. In adult tissue, only various neuronal populations in the hippocampus and olfactory bulb express PSF. PSF is expressed by differentiating neurons but not by astrocytic cells including radial glia; however oligodendrocytes differentiating in vitro were found to express it. The restricted expression of PSF suggests that it is involved in the control of neuronal-specific splicing events occurring at particular stages of neuronal differentiation and maturation. Monoclonal antibodies reacting specifically with PSF are useful tools for the molecular identification and characterization of the functional activity of PSF.
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