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1000 results found for “peroxisomal biogenesis factor”
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Name :
GAGA-POZDescription:
GAGA-POZ Drosophila Melanogaster Recombinant
Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.
Product # :
PRO-435Price :
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Shipped with Ice Packs
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Description
GAGA-POZ Drosophila Melanogaster Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids & having a molecular mass of 14 kDa.
Source
Escherichia Coli.
Formulation
The protein containing 10mM HEPES (pH-7.4) and 25mM NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
The GAGA factor is a sequence-specific DNA-binding protein, which participates in the regulation of the expression of a variety of different classes of genes in Drosophila such as many developmentally regulated genes, stress induced genes, and cell cycle regulated genes, as well as housekeeping genes. GAGA contains a C-terminal glutamine-rich domain and a highly conserved N-terminal POZ domain which reported to be involved in self-oligomerization in a number of other POZ domain containing proteins. In case of GAGA protein, the N-terminal POZ domain mediates the formation of oligomers both in vitro and in vivo.
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Synonyms
Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLLDLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQTVTKDDYTTH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GMFB AntibodyDescription:
Glia Maturation Factor Beta, Mouse Anti Human
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.
Product # :
ANT-680Price :
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
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Introduction
Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.
Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines. -
Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human GMFB mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GMFB amino acids 1-142 purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and Kappa light chain.
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Clone
PAT44D8AT.
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Applications
GMFB antibody has been tested by ELISA, Western blot and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
GMFB antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MIF Human, GSTDescription:
Macrophage Migration Inhibitor Factor Human Recombinant, GST tag
Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.
Product # :
CYT-401Price :
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Description
MIF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 345 amino acids (1-115 a.a) and having a molecular mass of 39.2kDa. MIF is fused to a 230 amino acid GST-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIF protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSPEFA MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SDF 1b MouseDescription:
Stromal Cell Derived Factor-1 Beta Mouse Recombinant (CXCL12)
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Product # :
CHM-326Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stromal Cell-Derived Factor-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8513 Dalton. The SDF-1b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CXCL12 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by its ability to chemoattract human monocytes at 50-100ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.More Info
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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Stromal Cell-Derived Factor-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Lys-Pro-Val-Ser-Leu.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PRSS3 Human, HEKDescription:
Protease Serine 3 Human Recombinant, HEK
Protease, Serine, 3, Protease, Serine, 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Mesotrypsin, Trypsin III, EC 3.4.21.4 4, Trypsin IV, PRSS4, TRY3, TRY4 Protease, Serine, 3 (Mesotrypsin), Pancreatic Trypsinogen III, Serine Protease 3, Serine Protease 4, Trypsinogen IV, Trypsinogen 4, Trypsinogen 5, EC 3.4.21, MTG, T9.
Product # :
ENZ-1194Price :
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Description
PRSS3 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 238 amino acids (16-247 a.a.) and having a molecular mass of 26kDa. PRSS3 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
PRSS3 protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 10,000pmol/min/ug, and is defined as the amount of enzyme that cleaves 1pmol of McaRPKPVE-Nval-WRK(Dnp)-NH2 per minute at pH 8.0 at 37℃.
More Info
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Synonyms
Protease, Serine, 3, Protease, Serine, 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Mesotrypsin, Trypsin III, EC 3.4.21.4 4, Trypsin IV, PRSS4, TRY3, TRY4 Protease, Serine, 3 (Mesotrypsin), Pancreatic Trypsinogen III, Serine Protease 3, Serine Protease 4, Trypsinogen IV, Trypsinogen 4, Trypsinogen 5, EC 3.4.21, MTG, T9.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
VPFDDDDKIV GGYTCEENSL PYQVSLNSGS HFCGGSLISE QWVVSAAHCY KTRIQVRLGE HNIKVLEGNE QFINAAKIIR HPKYNRDTLD NDIMLIKLSS PAVINARVST ISLPTAPPAA GTECLISGWG NTLSFGADYP DELKCLDAPV LTQAECKASY PGKITNSMFC VGFLEGGKDS CQRDSGGPVV CNGQLQGVVS WGHGCAWKNR PGVYTKVYNY VDWIKDTIAA NSHHHHHH.
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Background
PRSS3 is a member of the serine protease family, characterized by its specific enzymatic activity mediated by the serine residue in the catalytic triad. PRSS3's structure consists of a catalytic domain, a substrate-binding site, and disulfide bridges that help maintain its stability. Understanding the molecular characteristics of PRSS3 is crucial for elucidating its functions.
Physiological Functions: PRSS3 is primarily expressed in the pancreas, where it plays a vital role in the digestion of dietary proteins. It contributes to the breakdown of proteins into smaller peptides, facilitating their absorption in the small intestine. PRSS3 is part of a complex enzymatic network that ensures proper digestion and nutrient absorption.
Pathological Implications: Research has shown that abnormal PRSS3 activity or expression can be associated with various diseases. For example, alterations in PRSS3 have been linked to pancreatic diseases, including pancreatitis and pancreatic cancer. Investigating PRSS3's role in disease pathogenesis can provide valuable insights into the development and progression of these conditions.
Biomedical Research: PRSS3 human recombinant proteins are valuable tools in biomedical research. Researchers use these recombinant proteins to study PRSS3's enzymatic properties, interactions with other molecules, and potential therapeutic applications. They can perform controlled experiments to gain a deeper understanding of PRSS3's functions.
Therapeutic Potential: PRSS3's involvement in diseases like pancreatitis and pancreatic cancer has raised interest in its therapeutic potential. Researchers explore the development of inhibitors or modulators targeting PRSS3 as potential treatments for these diseases. Additionally, PRSS3's role in protein digestion has implications for digestive disorders and enzyme replacement therapies.
Diagnostic Markers: PRSS3 levels or activity may serve as diagnostic markers for certain diseases. Changes in PRSS3 expression in pancreatic tissue or serum may be indicative of pancreatic disorders. Research in this area aims to establish PRSS3 as a diagnostic tool for early disease detection.
Future Directions: Continued research on PRSS3 human recombinant and its roles in health and disease is essential. This includes investigating its regulation, substrate specificity, and potential interactions with other proteins. Such studies may uncover novel therapeutic targets and diagnostic strategies.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PYCRL HumanDescription:
Pyrroline-5-Carboxylate Reductase Like Human Recombinant
Pyrroline-5-carboxylate reductase 3, P5C reductase 3, P5CR 3, Pyrroline-5-carboxylate reductase-like protein, PYCRL.
Product # :
ENZ-678Price :
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Description
PYCRL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (1-274) and having a molecular mass of 31kDa.PYCRL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PYCRL solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Pyrroline-5-Carboxylate Reductase Like (PYCRL) is a member of the pyrroline-5-carboxylate reductase family and acts as a homodecamer. PYCRL plays a key role in proline bio-synthesis. Proline serves as a non-enzymatic antioxidant to reduce damage caused by reactive oxygen species (ROS) in microorganisms, animals and plants. In the final stage of proline biosynthesis, PYCRL catalyzes the reduction of aldehyde dehydrogenase 4A1 (ALDH4A1) to proline with NAD(P)H as the cofactor.
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Synonyms
Pyrroline-5-carboxylate reductase 3, P5C reductase 3, P5CR 3, Pyrroline-5-carboxylate reductase-like protein, PYCRL.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAAEPS PRRVGFVGAG RMAGAIAQGL IRAGKVEAQH ILASAPTDRN LCHFQALGCR TTHSNQEVLQ SCLLVIFATK PHVLPAVLAE VAPVVTTEHI LVSVAAGVSL STLEELLPPN TRVLRVLPNL PCVVQEGAIV MARGRHVGSS ETNLLQHLLE ACGRCEEVPE AYVDIHTGLS GSGVAFVCAF SEALAEGAVK MGMPSSLAHR IAAQTLLGTA KMLLHEGQHP AQLRSDVCTP GGTTIYGLHA LEQGGLRAAT MSAVEAATCR AKELSRK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Leptin-A TilapiaDescription:
Leptin-A Tilapia Recombinant
Product # :
CYT-1109Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin-A Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 16,491 Dalton. The Leptin-A Tilapia is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.
More Info
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Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin-A Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-A Tilapia should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin-A Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin A are Ala-Pro-Leu-Pro-Val-Glu.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.33 for 1 mg/ml Leptin-A Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NUBP1 HumanDescription:
Nucleotide Binding Protein 1 Human Recombinant
Cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 , NBP, NBP1, NBP35, Nucleotide-binding protein 1.
Product # :
PRO-2203Price :
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Shipped with Ice Packs
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Description
NUBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a) and having a molecular mass of 36.9kDa.NUBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques
Source
Escherichia Coli.
Formulation
NUBP1protein solution (1mg/ml) in Phosphate buffered saline (pH7.4),10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 (NUBP1) is Involved in the regulation of centrosome duplication similarity. NUBP1 is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. NUBP1 is necessary for maturation of extra mitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer constructs a Fe-S scaffold complex, mediating the de novo compilation of a Fe-S cluster and its transfer to target apoproteins.
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Synonyms
Cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 , NBP, NBP1, NBP35, Nucleotide-binding protein 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEEVPHD CPGADSAQAG RGASCQGCPN QRLCASGAGA TPDTAIEEIK EKMKTVKHKI LVLSGKGGVG KSTFSAHLAH GLAEDENTQI ALLDIDICGP SIPKIMGLEG EQVHQSGSGW SPVYVEDNLG VMSVGFLLSS PDDAVIWRGP KKNGMIKQFL RDVDWGEVDY LIVDTPPGTS DEHLSVVRYL ATAHIDGAVI ITTPQEVSLQ DVRKEINFCR KVKLPIIGVV ENMSGFICPK CKKESQIFPP TTGGAELMCQ DLEVPLLGRV PLDPLIGKNC DKGQSFFIDA PDSPATLAYR SIIQRIQEFC NLHQSKEENL ISS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CEBP Gamma HumanDescription:
CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
Product # :
PRO-434Price :
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Description
CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.
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Synonyms
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HPGDS HumanDescription:
Hematopoietic Prostaglandin D Synthase Human Recombinant
Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.
Product # :
ENZ-616Price :
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Description
HPGDS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-199 a.a.) and having a molecular mass of 25.9kDa.HPGDS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HPGDS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the sigma class glutathione-S-transferase family. The HPGDS enzyme catalyzes the conversion of PGH2 to PGD2 and has a role in the production of prostanoids in the immune system and mast cells. The presence of the HPGDS enzyme can be utilized to identify the differentiation stage of human megakaryocytes. Furthermore, HPGDS is a prostaglandin involved in smooth muscle contraction/relaxation and an effective inhibitor of platelet aggregation, and the conjugation of glutathione with a extensive range of aryl halides and organic isothiocyanates. In addition, HPGDS displays low glutathione-peroxidase activity towards cumene hydroperoxide. HPGDS is expressed in a number of megakaryocytic cell lines but not in platelets. HPGDS is highly expressed in the adipose tissue, macrophages and placenta; however it is expressed at lower levels in the lung, heart, lymph nodes, appendix, bone marrow and fetal liver.
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Synonyms
Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPNYKL TYFNMRGRAE IIRYIFAYLD IQYEDHRIEQ ADWPEIKSTL PFGKIPILEV DGLTLHQSLA IARYLTKNTD LAGNTEMEQC HVDAIVDTLD DFMSCFPWAE KKQDVKEQMF NELLTYNAPH LMQDLDTYLG GREWLIGNSV TWADFYWEIC
STTLLVFKPD LLDNHPRLVT LRKKVQAIPA VANWIKRRPQ TKL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GSTZ1 HumanDescription:
Glutathione Transferase Zeta 1 Human Recombinant
MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.
Product # :
ENZ-494Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GSTZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 26.2 kDa. The GSTZ1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The GSTZ1 protein solution contains 1x PBS pH-7.4 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GSTZ1 is part of the glutathione S-transferase super-family which encodes multifunctional enzymes vital in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. GSTZ1 is a bifunctional protein which has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 has low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. GSTZ1 catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.
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Synonyms
MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQAGKPILYS YFRSSCSWRV RIALALKGID YETVPINLIK DGGQQFSKDF QALNPMKQVP TLKIDGITIH QSLAIIEYLE ETRPTPRLLP QDPKKRASVR MISDLIAGGI QPLQNLSVLK QVGEEMQLTW AQNAITCGFN ALEQILQSTA GIYCVGDEVT MADLCLVPQV ANAERFKVDL TPYPTISSIN KRLLVLEAFQ VSHPCRQPDT PTELRA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ATF4 HumanDescription:
Activating Transcription Factor-4 Human Recombinant
Cyclic AMP-dependent transcription factor ATF-4, cAMP-dependent transcription factor, ATF-4, Activating transcription factor 4, Cyclic AMP-responsive element-binding protein 2, CREB-2, cAMP-responsive element-binding protein 2, DNA-binding protein, TAXREB67, Tax-responsive enhancer element-binding protein 67, TaxREB67, ATF4, CREB2, TXREB.
Product # :
PKA-006Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ATF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 510 amino acids (1-351 a.a.) and having a molecular mass of 56.6kDa.ATF4 is fused to a 159 amino acid His-Calmodulin-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ATF4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Activating transcription factor 4 (ATF4) is a member of a family of DNA-binding proteins which includes the AP-1 family of transcription factors, cAMP-response element binding proteins and CREB-like proteins. The ATF4 gene encodes a transcription factor which was initially identified as a widely expressed mammalian DNA binding protein that could bind a tax-responsive enhancer element in the LTR of HTLV-1.
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Synonyms
Cyclic AMP-dependent transcription factor ATF-4, cAMP-dependent transcription factor, ATF-4, Activating transcription factor 4, Cyclic AMP-responsive element-binding protein 2, CREB-2, cAMP-responsive element-binding protein 2, DNA-binding protein, TAXREB67, Tax-responsive enhancer element-binding protein 67, TaxREB67, ATF4, CREB2, TXREB.
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Physical Appearance
ATF4 is supplied as a sterile filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MHHHHHHMAD QLTEEQIAEF KEAFSLFDKD GDGTITTKEL GTVMRSLGQN PTEAELQDMI NEVDADGNGT IDFPEFLTMM ARKMKDTDSE EEIREAFRVF DKDGNGYISA AELRHVMTNL GEKLTDEEVD EMIREADIDG DGQVNYEEFV QMMTAKGSHM TEMSFLSSEV LVGDLMSPFD
QSGLGAEESL GLLDDYLEVA KHFKPHGFSS DKAKAGSSEW LAVDGLVSPS NNSKEDAFSG TDWMLEKMDL KEFDLDALLG IDDLETMPDD LLTTLDDTCD LFAPLVQETN KQPPQTVNPI GHLPESLTKP DQVAPFTFLQ PLPLSPGVLS STPDHSFSLE LGSEVDITEG DRKPDYTAYV
AMIPQCIKEE DTPSDNDSGI CMSPESYLGS PQHSPSTRGS PNRSLPSPGV LCGSARPKPY DPPGEKMVAA KVKGEKLDKK LKKMEQNKTA ATRYRQKKRA EQEALTGECK ELEKKNEALK ERADSLAKEI QYLKDLIEEV RKARGKKRVP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TGFB1 HumanDescription:
Transforming Growth Factor-beta 1 Human
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.
Product # :
CYT-561Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Transforming Growth Factor-beta 1 purified from Human Platelets having a molecular mass of 25kDa.The TGF-b 1 is purified by proprietary chromatographic techniques.
Source
Human Platelets.
Formulation
TGF-Beta1 protein was lyophilized from a solution containing 30% acetonitrile and 0.1% trifluoroacetic acid.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
Stimulates the growth of NRK-1 cells in soft agar at concentrations ranging from 0.1 to 5ng/ml corresponding to a specific activity of 200,000-10,000,000IU/mg. Effective concentration ranges must be experimentally determined. Purified EGF and/or TGF- must be present for observation of the biological activity.More Info
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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
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Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Lyophilized TGF-beta 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-beta 1 should be stored at 4°C between 2-7 days and for future use below -18°C.DO NOT RECONSTITE WITH NEUTRAL BUFFERS.DO NOT USE GLASS IMPLEMENTS OR EXTENSIVE MANIPULATIONS.PREVENT FREEZE THAW CYCLES.
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Solubility
It is recommended to reconstitute lyophilized TGF-beta 1 in 0.5% BSA in 0.1N acetic acid, which can then be further diluted to the desired aliquot with 30% acetonitrile and 0.1% trifluoroacetic acid.
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Background
Title: Transforming Growth Factor-Beta 1 Human: An Insight into its Role in Cellular Regulation
Abstract:
Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a critical role in various cellular processes, including cell growth, differentiation, apoptosis, and immune regulation. This research paper aims to provide a comprehensive overview of the structure, synthesis, signaling pathways, and biological functions of TGF-β1 in human cells. Additionally, this article highlights the relevance of TGF-β1 in various physiological and pathological conditions, including cancer, fibrosis, and immune disorders. Furthermore, potential therapeutic strategies targeting TGF-β1 signaling are also discussed. The information presented in this paper consolidates the current understanding of TGF-β1 and its significance in cellular regulation.Introduction:
Transforming Growth Factor-Beta 1 (TGF-β1) belongs to a superfamily of growth factors that regulate various cellular processes. It is synthesized as a precursor protein and undergoes proteolytic cleavage to generate the biologically active form. TGF-β1 exerts its effects by binding to specific cell surface receptors, leading to the activation of downstream signaling cascades. These signaling pathways involve Smad-dependent and Smad-independent mechanisms, which ultimately regulate gene expression and cellular responses.Biological Functions:
TGF-β1 regulates cell proliferation by exerting both stimulatory and inhibitory effects, depending on the cellular context. It plays a crucial role in tissue development, wound healing, and tissue repair by promoting extracellular matrix synthesis and modulating the immune response. TGF-β1 also has immunomodulatory functions, influencing the differentiation and function of immune cells. However, dysregulation of TGF-β1 signaling is associated with various pathologies, including cancer progression, fibrosis, and autoimmune disorders.Role in Cancer:
TGF-β1 acts as a tumor suppressor in early stages of cancer by inhibiting cell proliferation and inducing apoptosis. However, in advanced stages, it promotes tumor progression by enhancing tumor cell migration, invasion, and angiogenesis. The dual role of TGF-β1 in cancer highlights its complex involvement in tumorigenesis.Therapeutic Implications:
Given the significant role of TGF-β1 in various diseases, targeting its signaling pathways has emerged as a potential therapeutic strategy. Several approaches, including small molecule inhibitors, antibodies, and gene therapies, are being explored to modulate TGF-β1 activity in a controlled manner. These interventions hold promise in the treatment of cancer, fibrosis, and other TGF-β1-related disorders.Conclusion:
Transforming Growth Factor-Beta 1 is a versatile cytokine with diverse functions in cellular regulation. Its role in physiological processes and disease pathogenesis underscores its importance as a therapeutic target. Further investigations into the precise mechanisms and downstream effects of TGF-β1 signaling will contribute to the development of novel therapies for various human disorders.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Activin-A, CHO HumanDescription:
Activin-A Human Recombinant, CHO
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-1258Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Activin-A Human Recombinant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 26.0kDa. The Active form Activin-A is purified by standard chromatographic techniques.
Source
CHO cells.
Formulation
Human Activin-A was lyophilized from a concentrated filtered solution in 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.
Purity
Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
Assessed by the ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 for this effect is < 2.0 ng/ml, corresponding to a specific activity of ≥5.0 × 105 units/mg.
More Info
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
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Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Human INHBA protein should be reconstituted in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26 kDa.
What is the source or expression system of Activin A Protein?
CHO Cells.
What is the Purity of Activin A Protein?
Activin A Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
Assessed by the ability to inhibit the proliferation of mouse MPC-11 cells. The expected ED50 for this effect is < 2.0 ng/ml, corresponding to a specific activity of ≥5.0 × 105 units/mg.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?
GLECDGKVNI CCKKQFFVSF KDIGWNDWII APSGYHANYC EGECPSHIAG TSGSSLSFHS TVINHYRMRG HSPFANLKSC CVPTKLRPMS MLYYDDGQNI IKKDIQNMIV EECGCS
What applications can ACTIVIN A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NIP7 HumanDescription:
Nuclear Import 7 Homolog Human Recombinant
Nuclear Import 7 Homolog, 60S ribosome subunit biogenesis protein NIP7 homolog KD93, CGI-37, HSPC031, FLJ10296, NIP7.
Product # :
PRO-780Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
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Description
NIP7 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-180 a.a.) and having a molecular mass of 21.5kDa. NIP7 is fused to 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NIP7 protein solution contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
60S ribosome subunit biogenesis protein NIP7 homolog (NIP7) belongs to NIP7 family and contains 1 PUA domain. NIP7 interacts with pre-ribosome complex and may bind to RNA. NIP7 is vital for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
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Synonyms
Nuclear Import 7 Homolog, 60S ribosome subunit biogenesis protein NIP7 homolog KD93, CGI-37, HSPC031, FLJ10296, NIP7.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRPLTEEETR VMFEKIAKYI GENLQLLVDR PDGTYCFRLH NDRVYYVSEK IMKLAANISG DKLVSLGTCFGKFTKTHKFR LHVTALDYLA PYAKYKVWIK PGAEQSFLYG NHVLKSGLGR ITENTSQYQG VVVYSMADIPLGFGVAAKST QDCRKVDPMA IVVFHQADIG EYVRHEETLT LEHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GFER HumanDescription:
Growth Factor, Augmenter of Liver Regeneration Human Recombinant
FAD-linked sulfhydryl oxidase ALR, Augmenter of liver regeneration, Hepatopoietin, GFER, ALR, HERV1, HPO, ALR, HSS, ERV1, HPO1, HPO2.
Product # :
PRO-1326Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GFER Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-205 a.a) and having a molecular mass of 26kDa.GFER is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GFER protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
FAD-linked sulfhydryl oxidase ALR (GFER) is a member of the Erv1/ALR family of proteins, which is found in higher and lower eukaryotes. GFER is a hepatotrophic growth factor and flavin-linked sulfhydryl oxidase expressed in a variety of tissues. Moreover, GFER induces the expression of S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases (ODC), which each have a central role in the synthesis of polyamines. The hepatotrophic factor designated augmenter of liver regeneration (ALR) is assumed to be one of the factors responsible for the exceptional regenerative capacity of mammalian liver. The GFER gene is located on chromosome 16 in the interval containing the locus for polycystic kidney disease (PKD1).
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Synonyms
FAD-linked sulfhydryl oxidase ALR, Augmenter of liver regeneration, Hepatopoietin, GFER, ALR, HERV1, HPO, ALR, HSS, ERV1, HPO1, HPO2.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAAPGE RGRFHGGNLF FLPGGARSEM MDDLATDARG RGAGRRDAAA SASTPAQAPT SDSPVAEDAS RRRPCRACVD FKTWMRTQQK RDTKFREDCP PDREELGRHS WAVLHTLAAY YPDLPTPEQQ QDMAQFIHLF SKFYPCEECA EDLRKRLCRN HPDTRTRACF TQWLCHLHNE VNRKLGKPDF DCSKVDERWR DGWKDGSCD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ARF5 HumanDescription:
ADP-Ribosylation Factor 5 Human Recombinant
ADP-ribosylation factor 5, ARF5.
Product # :
PRO-245Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARF5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (1-180 a.a) and having a molecular mass of 22.6kDa.ARF5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARF5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ADP-ribosylation factor 5 (ARF5) is a small guanine nucleotide-binding protein which enhances the enzymatic activities of cholera toxin. ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the connection of actin to the golgi via rho family-dependent G-protein localization and WASP/Arp2/3 complexes. ARF5 is involved in vesicular transport and functioning via phospholipase D activation.
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Synonyms
ADP-ribosylation factor 5, ARF5.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGLTVSALFS RIFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV QESADELQKM LQEDELRDAV LLVFANKQDM PNAMPVSELT DKLGLQHLRS RTWYVQATCA
TQGTGLYDGL DWLSHELSKR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
FGFBP HumanDescription:
Fibroblast Growth Factor Binding Protein 1 Human Recombinant
Fibroblast Growth Factor Binding Protein 1, FGFBP, HBP17, 17 KDa Heparin-Binding Growth Factor-Binding Protein, 17 KDa HBGF-Binding Protein, FGF-Binding Protein 1, FGF-BP1, FGFBP-1, FGF-BP, Heparin-Binding Growth Factor Binding Protein, Fibroblast Growth Factor-Binding Protein 1, Fibroblast growth factor-binding protein 1.
Product # :
CYT-860Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
FGFBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (24-234 a.a) and having a molecular mass of 26.2kDa. FGFBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FGFBP protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Fibroblast Growth Factor Binding Protein 1, also known as FGFBP1 is a secreted fibroblast growth factor carrier protein. FGFBP1 plays a vital part in cell proliferation, differentiation and migration by binding to fibroblast growth factors and potentiating their biological effects on target cells. In addition, FGFBP1 also takes part in tumor growth as an angiogenic switch molecule, furthermore an expression of FGFBP1 has been associated with more than a few types of cancer as well as pancreatic and colorectal adenocarcinoma.
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Synonyms
Fibroblast Growth Factor Binding Protein 1, FGFBP, HBP17, 17 KDa Heparin-Binding Growth Factor-Binding Protein, 17 KDa HBGF-Binding Protein, FGF-Binding Protein 1, FGF-BP1, FGFBP-1, FGF-BP, Heparin-Binding Growth Factor Binding Protein, Fibroblast Growth Factor-Binding Protein 1, Fibroblast growth factor-binding protein 1.
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Physical Appearance
Sterile Filtered colorless clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC.
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Background
What is the molecular weight/Mw of CYT-860 Protein?
CYT-860 Protein has a total Mw of 26.2kDa.
What is the source or expression system of CYT-860 Protein?
Escherichia Coli.
What is the Purity of CYT-860 Protein?
CYT-860 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CYT-860 Protein?
The biological functionality of CYT-860 Protein will be determined in the future.
What is the amino acid sequence of CYT-860 Protein?
MGSSHHHHHH SSGLVPRGSH MGSKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC.
What applications can CYT-860 Protein be used in?
CYT-860 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CYT-860 Protein?
The endotoxin level is minimal, CYT-860 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EIF4E MouseDescription:
Eukaryotic Translation Initiation Factor 4E Recombinant Mouse
eIF-4E, eIF4E, mRNA cap-binding protein, eIF-4F 25 kDa subunit, Eif4e.
Product # :
PRO-2411Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
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Description
EIF4E Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 241 amino acids (1-217 a.a) and having a molecular mass of 27.6kDa. EIF4E is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EIF4E protein solution (1mg/ml) 20mM Tris-HCl Buffer (pH8.0), 10% glycerol, 1mM DTT, 0.1M NaCl and 0.1mM PMSF.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
EIF4E is part of the eukaryotic initiation factor 4 families, controls translation of maternal mRNAs in early embryos before the onset of zygotic transcription. EIF4E identifies and binds to the 7 methyl GTP cap structure of eukaryotic mRNAs, thus modulates the initiation of translation. EIF4E enables ribosome binding by inducing the unwinding of the mRNAs secondary structures.
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Synonyms
eIF-4E, eIF4E, mRNA cap-binding protein, eIF-4F 25 kDa subunit, Eif4e.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMATVEP ETTPTTNPPP AEEEKTESNQ EVANPEHYIK HPLQNRWALW FFKNDKSKTW QANLRLISKF DTVEDFWALY NHIQLSSNLM PGCDYSLFKD GIEPMWEDEK NKRGGRWLIT LNKQQRRSDL DRFWLETLLC LIGESFDDYS DDVCGAVVNV RAKGDKIAIW TTECENRDAV THIGRVYKER LGLPPKIVIG YQSHADTATK SGSTTKNRFV V
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SEPSECS MouseDescription:
Selenocysteinyl-tRNA(Sec) synthase Mouse Recombinant
AA986712, D5Ertd135e, SecS, SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein, SepSecS.
Product # :
ENZ-1081Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
SEPSECS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 527 amino acids (1-504 a.a.) and having a molecular mass of 57.7kDa.SEPSECS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SEPSECS protein solution (0.25 mg/ml) is formulated in 20mM Tris-HCl buffer (pH7.5) 1mM DTT, 0.2M NaCl and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SEPSECS catalyzes the last step of sec synthesis by converting O-phosphoseryl-tRNA(sec) to selenocysteinyl-tRNA(sec) using selenophosphate as the selenium donor. Furthermore, SEPSECS protein is considered a specific marker of autoimmune hepatitis.
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Synonyms
AA986712, D5Ertd135e, SecS, SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein, SepSecS.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNPESFA AGERRVSPAY VRQGCEARRA HEHLIRLLLE QGKCPEDGWD ESTLELFLHE LAVMDSNNFL GNCGVGEREG RVASALVARR HYRFIHGIGR SGDISAVQPK AAGSSLLNKI TNSLVLNVIK LAGVHSVASC FVVPMATGMS LTLCFLTLRH
KRPKAKYIIW PRIDQKSCFK SMVTAGFEPV VIENVLEGDE LRTDLKAVEA KIQELGPEHI LCLHSTTACF APRVPDRLEE LAVICANYDI PHVVNNAYGL QSSKCMHLIQ QGARVGRIDA FVQSLDKNFM VPVGGAIIAG FNEPFIQDIS KMYPGRASAS PSLDVLITLL SLGCSGYRKL
LKERKEMFVY LSTQLKKLAE AHNERLLQTP HNPISLAMTL KTIDGHHDKA VTQLGSMLFT RQVSGARAVP LGNVQTVSGH TFRGFMSHAD NYPCAYLNAA AAIGMKMQDV DLFIKRLDKC LNIVRKEQTR ASVVSGADRN KAEDADIEEM ALKLDDVLGD VGQGPAL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
OSM Human, HisDescription:
Oncostatin-M Human Recombinant, His Tag
OSM, MGC20461.
Product # :
CYT-060Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OSM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (26-234) and having a molecular mass of 25.9 kDa.The OSM is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSM protein (0.5mg/ml) is supplied in 20mM Tris-HCl, pH-8, 1mM DTT and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
POU2AF1 is a lymphocyte specific transcription coactivator protein. POU2AF1 cooperates only with the Oct1/2 proteins using sub domains in the POU domain of the Oct1/2 proteins, increasing their transcriptional efficiency. Even though POU2AF1 have no basic ability to bind DNA, it links firmly with the octomer motif in the presence of Oct1 and Oct2. POU2AF1 is expressed at maximum levels in spleen and peripheral blood leukocytes.
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Synonyms
OSM, MGC20461.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAIGSCSKE YRVLLGQLQK QTDLMQDTSR LLDPYIRIQG LDVPKLREHC RERPGAFPSE ETLRGLGRRG FLQTLNATLG CVLHRLADLE QRLPKAQDLE RSGLNIEDLE KLQMARPNIL GLRNNIYCMA QLLDNSDTAE PTKAGRGASQ PPTPTPASDA FQRKLEGCRF LHGYHRFMHS VGRVFSKWGE SPNRSRRHSP HQALRKGVRR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EGF HumanDescription:
Epidermal Growth Factor Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-217Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Epidermal Growth Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6.2kDa. The EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EGF was lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.
More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
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Background
About EGF:
In the sphere of biomedical studies, epidermal boom factor (EGF) is a cornerstone that gives precious insights into the mechanisms underlying tissue healing, differentiation, and mobile proliferation. In this article we will explore the characteristics and uses of epidermal growth factor (EGF).
Description:
Epidermal growth factor (EGF) is a 6-kDa protein consisting of 53 amino acid residues and 3 intramolecular disulfide linkages. Human tissues, such as platelets, the parotid gland, and the submandibular gland, are rich in EGF. EGF, which was first discovered in human urine and the submaxillary glands of mice, functions as a major modulator of cell proliferation by attaching to its receptor, EGFR, which is found on the cell membrane. EGF triggers autophosphorylation of transmembrane protein tyrosine kinase EGFR upon binding, hence initiating downstream signaling cascades through pathways such as phosphatidylinositol and ras. Beyond the cell membrane, EGF has a variety of roles as it also initiates cytoplasmic processes such actin depolymerization and membrane ruffle formation. Studies indicate that EGF and its receptor might possibly be important components of the nucleus, highlighting the complexity of EGF-mediated cellular responses.
Function:
By attaching to the epidermal growth factor receptor (EGFR), EGF promotes the survival, differentiation, and multiplication of cells. This connection is essential for boosting many physiological processes and stimulating cell proliferation. The preservation of oro-esophageal and stomach tissue integrity is greatly supported by salivary EGF, which is regulated by dietary inorganic iodine. Its actions include the healing of gastric and oral ulcers, the inhibition of gastric acid secretion, the stimulation of DNA synthesis, and the protection of mucosal surfaces against harmful substances such as bile acids, gastric acid, and bacteria. Salivary EGF's role extends to repairing gastric tissue and addressing oro-esophagal issues, showcasing its healing ability in resolving oral and gastrointestinal ailments, including ulcers.
Mechanism:
EGF functions by forming a strong bond with the cell surface's epidermal growth factor receptor (EGFR), which triggers ligand- induced dimerization. This incident sets off the intrinsic protein-tyrosine kinase activity of EGFR, which in turn initiates a signal transduction cascade inside the cell. Numerous biochemical changes are brought about by this cascade, such as increased intracellular calcium levels, increased glycolysis and protein synthesis, and increased expression of particular genes, most notably the EGFR gene. These carefully planned alterations eventually promote DNA synthesis and cell division, illuminating the complex process by which EGF directs basic biological functions and modulates cellular responses.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.2kDa.
What is the source or expression system of EGF Protein?
Escherichia Coli.
What is the Purity of EGF Protein?
EGF Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of >1.0x107 IU/mg.
What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Omentin HumanDescription:
Omentin Human Recombinant
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-301Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 313 amino acids and having a molecular mass of 35 kDa. Intelectin is purified by proprietary chromatographic techniques.
Source
E.Coli.
Formulation
Each mg of lyophilized powder contains 10mM NaP, pH-7.5 and 5:1 mannitol to protein.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase INSstimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of INS presence. Its role in glucose metabolism and obesity remains to be described; an INS-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
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Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Intelectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Omentin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MNQLSFLLFL IATTRGWSTD EANTYFKEWTCSSSPSLPRS CKEIKDECPS AFDGLYFLRT ENGVIYQTFC DMTSGGGGWT LVASVHENDM RGKCTVGDRW SSQQGSKADY PEGDGNWANY NTFGSAEAAT SDDYKNPGYY DIQAKDLGIW HVPNKSPMQH WRNSSLLRYR TDTGFLQTLG HNLFGIYQKY PVKYGEGKCW TDNGPVIPVV YDFGDAQKTA SYYSPYGQRE FNNERAANAL CAGMRVTGCN TEHHCIGGGG YFPEASPQQC GDFSGFDWSG YGTHVGYSSS REITEAAVLLFYR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ARL2BP HumanDescription:
ADP-Ribosylation Factor-Like 2 Binding Protein Human Recombinant
ADP-ribosylation factor-like protein 2-binding protein, ARF-like 2-binding protein, Binder of ARF2 protein 1, ARL2BP, BART, BART1.
Product # :
PRO-274Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
ARL2BP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-163) and having a molecular mass of 20.9 kDa. The ARL2BP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARL2BP solution (1 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5) and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ARL2BP is an effector of ADP-ribosylation factor-like 2(ARL2) which is vital for nuclear retention of STAT3. The ARL2BP protein binds to ARL2.GTP with high affinity but does not interact with ARL2.GDP, activated ARF, or RHO proteins. Though primarily cytosolic, ARL2BP can enter the mitochondria and bind the adenine nucleotide transporter while bound to ARL2. Accordingly, it may also be involved in mitochondria transport and apoptosis.
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Synonyms
ADP-ribosylation factor-like protein 2-binding protein, ARF-like 2-binding protein, Binder of ARF2 protein 1, ARL2BP, BART, BART1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDALEGESFA LSFSSASDAE FDAVVGYLED IIMDDEFQLL QRNFMDKYYL EFEDTEENKL IYTPIFNEYI SLVEKYIEEQ LLQRIPEFNM AAFTTTLQHH KDEVAGDIFD MLLTFTDFLA FKEMFLDYRA EKEGRGLDLS SGLVVTSLCK SSSLPASQNN LRH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.