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1000 results found for “pparg”
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Name :
PLGF3 Human, sf9Description:
Placental Growth Factor-3 Human Recombinant, sf9
Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.
Product # :
CYT-961Price :
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Description
PLGF3 Human Recombinant produced in Spodoptera frugiperda is a glycosylated homodimer containing 2 chains of 203 amino acids (Leu19-Arg221) and having a molecular mass of 58kDa.The PLGF-3 is purified by proprietary chromatographic techniques.
Source
Spodoptera frugiperda.
Formulation
PLGF-3 protein was lyophilized from a 0.2µm filtered solution in HCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its binding ability to rHuVEGF R1 in a functional ELISA, is less than 3ng/ml.More Info
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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
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Synonyms
Placental Growth Factor, Placental Growth Factor Vascular Endothelial Growth Factor-Related Protein, PGFL, PLGF, Placental Growth Factor-Like, Placenta Growth Factor, SHGC-10760, D12S1900, PlGF-2, PGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PLGF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF-3 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 PLGF3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
LGMN MouseDescription:
Legumain Mouse Recombinant
Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.
Product # :
ENZ-933Price :
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- sds-page
Description
LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (18-435a.a.) and having a molecular mass of 48.6kDa. LGMN is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LGMN protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Legumain, also known as LGMN is a lysosomal cysteine protease which is found in all mouse tissues, however it was mainly abundant in the kidney as well as placenta. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.
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Synonyms
Legumain, Asparaginyl endopeptidase, Protease, cysteine 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
VPVGVDDPED GGKHWVVIVA GSNGWYNYRH QADACHAYQI IHRNGIPDEQ IIVMMYDDIA NSEENPTPGV VINRPNGTDV YKGVLKDYTG EDVTPENFLA VLRGDAEAVK GKGSGKVLKS GPRDHVFIYF TDHGATGILV FPNDDLHVKD LNKTIRYMYE HKMYQKMVFY IEACESGSMM NHLPDDINVY ATTAANPKES SYACYYDEER GTYLGDWYSV NWMEDSDVED LTKETLHKQY HLVKSHTNTS HVMQYGNKSI STMKVMQFQG MKHRASSPIS LPPVTHLDLT PSPDVPLTIL KRKLLRTNDV KESQNLIGQI QQFLDARHVI EKSVHKIVSL LAGFGETAER HLSERTMLTA HDCYQEAVTH FRTHCFNWHS VTYEHALRYL YVLANLCEAP YPIDRIEMAM DKVCLSHYLE HHHHHH.
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 :
PDGF BB Human, YeastDescription:
Platelet Derived Growth Factor-BB Human Recombinant, Yeast
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
Product # :
CYT-242Price :
Quantity :
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Shipped at Room temp
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Description
Platelet-Derived Growth Factor BB Human Recombinant is a glycosylated homodimer produced in Saccharomyces cerevisiae, containing 2x109 amino acids and having a molecular mass of 32kDa. PDGF-BB is purified by proprietary chromatographic techniques.
Source
Saccharomyces cerevisiae.
Formulation
The PDGF-BB was lyophilized from 0.2 µm filtered solution in 20mM sodium phosphate in absence of any carrier protein.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to stimulate proliferation of mouse 3T3 fibroblasts is typically 1 ng/ml, corresponding to a Specific Activity of 1,000,000IU/mg.More Info
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Introduction
PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.
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Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Platelet-derived Growth Factor BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Platelet-derived Growth Factor-BB in sterile 18M-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 Ser-Leu-Gly-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 :
PGLYRP1 Human, HEKDescription:
Peptidoglycan Recognition Protein 1 Human Recombinant, HEK
PGLYRP, PGRP, PGRP-S, PGRPS, TAG7, TNFSF3L, Peptidoglycan recognition protein 1, peptidoglycan recognition protein short.
Product # :
PRO-2726Price :
Quantity :
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Shipped with Ice Packs
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Description
PGLYRP1 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 184 amino acids (22-196 a.a) and having a molecular mass of 20.5 kDa.PGLYRP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The PGLYRP1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Peptidoglycan. The ED50 range ≤ 30 ng/ml.
More Info
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Introduction
Peptidoglycan Recognition Protein 1 (PGLYRP1) is a member of the N-acetylmuramoyl-L-alanine amidase 2 family. PGLYRP1 binds to peptidoglycan of bacteria and affects the peptidoglycan biosynthesis. PGLYRP1 displays bactericidal activity towards Gram-positive bacteria and is bacteriostatic towards Gram-negative bacteria. PGLYRP1 has a role in innate immunity. PGLYRP1 is highly expressed in the bone marrow, and weakly expressed in the kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils.
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Synonyms
PGLYRP, PGRP, PGRP-S, PGRPS, TAG7, TNFSF3L, Peptidoglycan recognition protein 1, peptidoglycan recognition protein short.
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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
DGSQETEDPA CCSPIVPRNE WKALASECAQ HLSLPLRYVV VSHTAGSSCN TPASCQQQAR NVQHYHMKTL GWCDVGYNFL IGEDGLVYEG RGWNFTGAHS GHLWNPMSIG ISFMGNYMDR VPTPQAIRAA QGLLACGVAQ GALRSNYVLK GHRDVQRTLS PGNQLYHLIQ NWPHYRSPHH HHHH
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 :
T.pallidum p47 (Partial)Description:
Treponema pallidum p47 (Partial) Recombinant
Product # :
TRP-249Price :
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Description
The E.Coli derived recombinant protein is fused at the C- terminus with a 6xHis Tag and contains the T.Pallidum p47 immunodominant regions.
Source
Escherichia Coli.
Formulation
70mM Tris-HCl pH8.0, 50mM NaCl, 50% Glycerol and 1.5M urea.
Purity
Treponema Pallidum protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum subsp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
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Stability
Treponema Pallidum although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of T.Pallidum with minimal specificity problems.
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Specificity
Immunoreactive with sera of T.Pallidum infected individuals.
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Purification Method
Treponema Pallidum protein was purified by proprietary chromatographic technique.
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 :
PARK7 P1E12AT AntibodyDescription:
Parkinson Disease Protein 7 Clone P1E12AT, Mouse Anti Human
PARK7, Parkinson disease protein 7, Oncogene DJ-1, Parkinson disease (autosomal recessive, early onset) 7.
Product # :
ANT-515Price :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
The PARK7 is a ubiquitously expressed protein involved in various cellular processes including spermatogenesis and fertilization, cancer, RNA-binding, androgen-receptor signaling and oxidative stress. Mutations in the PARK7 are the cause of autosomal recessive early-onset Parkinson’s disease 7 (Park7).
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Synonyms
PARK7, Parkinson disease protein 7, Oncogene DJ-1, Parkinson disease (autosomal recessive, early onset) 7.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human PARK7 mAb, clone P1E12AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PARK7 protein 1-189 amino acids purified from E. coli
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Ig Subclass
Mouse IgG2b heavy chain and k light chain.
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Clone
P1E12AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
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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
PARK7 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 :
PTH (1-84) N15 HumanDescription:
Parathyroid Hormone (1-84) N15 Labeled Human Recombinant
Parathyrin, PTH, Parathormone.
Product # :
HOR-002Price :
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Shipped at Room temp
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Description
PTH (1-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 84 amino acids and having a molecular mass of 9550 Dalton labeled by the stable isotope N15.The PTH (1-84) N15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTH (1-84) N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 9,000 Units/mg.More Info
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Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calciumin the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptorin three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone.
In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb.
In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylationof 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
Recombinant Human full length PTH 1-84 has potential as an anti-osteoporotic agent, due to its properties as a bone formation stimulant, it increases bone turnover, stimulating osteoblasts and reducing both vertebral and non vertebral fractures. -
Synonyms
Parathyrin, PTH, Parathormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Parathyrin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH 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 Parathormone in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SVSEIQLMHN LGKHLNSMER VEWLRKKLQD VHNFVALGAP LAPRDAGSQR PRKKEDNVLV ESHEKSLGEA DKADVNVLTK AKSQ.
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 :
IFNG MouseDescription:
IFN-Gamma Mouse Recombinant
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-358Price :
Quantity :
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Shipped at Room temp
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Description
IFN-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15.6kDa.The IFN-gamma is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs. -
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 IFN-gamma in sterile distilled water or 20mM AcOH at concentrations ranging between 0.1mg-0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
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Background
What is the molecular weight/Mw of IFNG MOUSE Protein?
IFNG MOUSE Protein has a total Mw of 15.6kDa.
What is the source or expression system of IFNG MOUSE Protein?
Escherichia Coli.
What is the Purity of IFNG MOUSE Protein?
IFNG MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG MOUSE Protein?
The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg
What is the amino acid sequence of IFNG MOUSE Protein?
MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.
What applications can IFNG MOUSE Protein be used in?
IFNG MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG MOUSE Protein?
The endotoxin level is minimal, IFNG MOUSE 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.
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Name :
PGM1 HumanDescription:
Phosphoglucomutase 1 Human Recombinant
PGM1, Phosphoglucomutase 1, Glucose Phosphomutase 1, EC 5.4.2.2, PGM 1, CDG1T, GSD14, Phosphoglucomutase-1, EC 5.4.2.
Product # :
ENZ-916Price :
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Shipped with Ice Packs
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Description
PGM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 585 amino acids (1-562 a.a) and having a molecular mass of 63.8kDa.PGM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PGM1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Phosphoglucomutase-1 also known as PGM1 is a member of the phosphohexose mutase family. There are more than a few PGM isozymes, which catalyze the transfer of phosphate between the 1&6positions of glucose. In nearly all cell types, PGM1 isozymes predominate, representing around 90% of total PGM activity. It has been found that defects in PGM1 are the cause of glycogen storage disease type 14.
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Synonyms
PGM1, Phosphoglucomutase 1, Glucose Phosphomutase 1, EC 5.4.2.2, PGM 1, CDG1T, GSD14, Phosphoglucomutase-1, EC 5.4.2.
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Physical Appearance
Sterile Filtered clear 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 MGSMVKIVTV KTQAYQDQKP GTSGLRKRVK VFQSSANYAE NFIQSIISTV EPAQRQEATL VVGGDGRFYM KEAIQLIARI AAANGIGRLV IGQNGILSTP AVSCIIRKIK AIGGIILTAS HNPGGPNGDF GIKFNISNGG PAPEAITDKI FQISKTIEEY AVCPDLKVDL GVLGKQQFDL ENKFKPFTVE IVDSVEAYAT MLRSIFDFSA LKELLSGPNR LKIRIDAMHG VVGPYVKKIL CEELGAPANS AVNCVPLEDF GGHHPDPNLT YAADLVETMK SGEHDFGAAF DGDGDRNMIL GKHGFFVNPS DSVAVIAANI FSIPYFQQTG VRGFARSMPT SGALDRVASA TKIALYETPT GWKFFGNLMD ASKLSLCGEE SFGTGSDHIR EKDGLWAVLA WLSILATRKQ SVEDILKDHW QKYGRNFFTR YDYEEVEAEG ANKMMKDLEA LMFDRSFVGK QFSANDKVYT VEKADNFEYS DPVDGSISRN QGLRLIFTDG SRIVFRLSGT GSAGATIRLY IDSYEKDVAK INQDPQVMLA PLISIALKVS QLQERTGRTA PTVIT.
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 :
PLGF1 Human, Sf9Description:
Placental Growth Factor-1 Human Recombinant, Sf9
PIGF, PGF, PLGF-1.
Product # :
CYT-419Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Placenta Growth Factor-1 Human Recombinant produced in insect cells is a homodimer, glycosylated polypeptide chain containing 2 x 131 amino acids and having a total molecular mass of approximately 34 kDa. The PLGF-1 is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing 50mM acetic acid.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to bind to immobilized rh-sFlt-1 in a functional ELISA. PlGF-1 human Recombinant can bind to immobilized rh-sFlt-1 (100ng/well) with a linear range at 0.5-10ng/ml, corresponding to a Specific Activity of 1x105-2x106units/mg.More Info
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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
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Synonyms
PIGF, PGF, PLGF-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Placenta Growth Factor 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Placenta Growth Factor 1 in sterile 0.1M acetic acid 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 Met-Leu-Pro-Ala-Val.
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 :
T.pallidum p15 (Partial)Description:
Treponema pallidum p15 (Partial) Recombinant
Product # :
TRP-275Price :
Quantity :
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Shipped with Ice Packs
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Description
The E.Coli derived recombinant protein is fused at N-terminus with GST tag and contains the Trp. Pallidum p15 immunodominant regions.
Source
Escherichia Coli.
Formulation
70mM Tris-HCl pH-8, 84mM NaCl, 14mM Glutathione, 30% Glycerol & 0.2% Sarcosil.
Purity
Treponema Pallidum protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
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Stability
Treponema Pallidum protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of Trp. Pallidum with minimal specificity problems.
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Specificity
Immunoreactive with sera of Trp. Pallidum infected individuals.
-
Purification Method
Treponema Pallidum protein was purified by proprietary chromatographic technique.
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 :
Leptin qA Human, PEGDescription:
Leptin Quadruple Antagonist Pegylated Human Recombinant
Product # :
CYT-1251Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
- formulation
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Description
Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
PAPP-A NativeDescription:
Pregnancy-Associated Plasma Protein-1 Human
Pappalysin-1, Pregnancy-associated plasma protein A, PAPP-A, IGF-dependent IGFBP-4 protease, IGFBP-4ase, PAPPA, PAPA, DIPLA1, PAPPA1, ASBABP2.
Product # :
ENZ-1204Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PAPP-A Human native purified from human placenta having a total molecular mass of ~200 kDa. The PAPP-A is purified by proprietary chromatographic techniques.
Source
Human Placenta
Formulation
PAPP-A protein was lyophilized from 10mM Tris-HCl pH-7, 0.15M NaCl, 0.1% NGME & 0.09% NaN3.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PAPPA is a large zinc binding protein, which plays a role as a metalloprotease and specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. PAPP-A regulates IGF bioactivity in various biological systems, including the human ovary and cardiovascular systems. PAPP A levels were higher in patients with unstable angina or acute myocardial infarction. PAPPA is also involved in local proliferative processes such as wound healing and bone remodeling. Moreover, PAPP-A is produced in high concentrations during pregnancy and is released into the maternal circulation. In placenta, PAPP A is expressed in X cells in septa and anchoring villi, and in syncytiotrophoblasts in the chorionic villi.
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Synonyms
Pappalysin-1, Pregnancy-associated plasma protein A, PAPP-A, IGF-dependent IGFBP-4 protease, IGFBP-4ase, PAPPA, PAPA, DIPLA1, PAPPA1, ASBABP2.
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Physical Appearance
Brownish lyophilized (freeze-dried) powder.
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Stability
Lyophilized PAPP-A although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PAPP-A should be stored at 4C between 2-7 days and for future use below -18C. 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 add deionized water to a working concentration of 0.1mg/ml and let the lyophilized pellet dissolve completely.
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Human Virus Test
Starting material tested and found negative for HIV-I, HIV-II, HCV antibodies and HBsAg antigen.
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 :
PTH (7-84) N15 HumanDescription:
Parathyroid Hormone (7-84) N15 Labeled Human Recombinant
Parathyrin, PTH, Parathormone.
Product # :
HOR-013Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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Description
PTH (7-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8900 Dalton labeled by the stable isotope N15.The PTH (7-84) N15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTH (7-84) N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptor in three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone. In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb. In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
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Synonyms
Parathyrin, PTH, Parathormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PTH (7-84) N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH (7-84) N15 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 PTH (7-84) N15 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ
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 :
PCOLCE HumanDescription:
Procollagen C-Endopeptidase Enhancer Human Recombinant
Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase Enhancer 1, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1, PCPE-1, PCPE1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Procollagen C-Endopeptidase Enhancer 1, COOH-Terminal Proteinase Enhancer, Procollagen, Type 1, PCPE, Procollagen C-endopeptidase enhancer 1.
Product # :
ENZ-863Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PCOLCE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (26-449 a.a) and having a molecular mass of 47.9kDa. PCOLCE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PCOLCE protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Procollagen C-endopeptidase enhancer 1, also known as PCOLCE binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. In addition, C-terminal processed part of PCPE (CT-PCPE) has a metalloproteinase inhibitory activity. Among the diseases which are associated with PCOLCE: bone fracture & oculopharyngeal muscular dystrophy.
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Synonyms
Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase Enhancer 1, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1, PCPE-1, PCPE1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Procollagen C-Endopeptidase Enhancer 1, COOH-Terminal Proteinase Enhancer, Procollagen, Type 1, PCPE, Procollagen C-endopeptidase enhancer 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 MGSQTPNYTR PVFLCGGDVK GESGYVASEG FPNLYPPNKE CIWTITVPEG QTVSLSFRVF DLELHPACRY DALEVFAGSG TSGQRLGRFC GTFRPAPLVA PGNQVTLRMT TDEGTGGRGF LLWYSGRATS GTEHQFCGGR LEKAQGTLTT PNWPESDYPP GISCSWHIIA PPDQVIALTF EKFDLEPDTY CRYDSVSVFN GAVSDDSRRL GKFCGDAVPG SISSEGNELL VQFVSDLSVT ADGFSASYKT LPRGTAKEGQ GPGPKRGTEP KVKLPPKSQP PEKTEESPSA PDAPTCPKQC RRTGTLQSNF CASSLVVTAT VKSMVREPGE GLAVTVSLIG AYKTGGLDLP SPPTGASLKF YVPCKQCPPM KKGVSYLLMG QVEENRGPVL PPESFVVLHR PNQDQILTNL SKRKCPSQPV RAAASQD.
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 :
T.pallidum p17 (Partial)Description:
Treponema pallidum p17 (Partial) Recombinant
Product # :
TRP-248Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.Coli derived recombinant protein is fused at N-terminus with 6xHis tag and contains the Trp. Pallidum p17 immunodominant regions.
Source
Escherichia Coli.
Formulation
70mM Tris-HCl pH8.0, 50mM NaCl, 50% Glycerol, 1.5M Urea.
Purity
Treponema Pallidum protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
-
Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
-
Stability
Treponema Pallidum protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of Trp. Pallidum with minimal specificity problems.
-
Specificity
Immunoreactive with sera of Trp. Pallidum infected individuals.
-
Purification Method
Treponema Pallidum protein was purified by proprietary chromatographic technique.
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 :
Leptin tA Rat, PEGDescription:
Leptin Antagonist Triple Mutant Pegylated Rat Recombinant
Product # :
CYT-567Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
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Description
Leptin Antagonist Triple Mutant Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Rat Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Leptin Antagonist Triple Mutant Rat Recombinant half-life in circulation after SC injection was over 20 hours.
Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Rat Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Rat Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
Parvovirus VP2Description:
Parvovirus VP2 Canine Recombinant
Product # :
PRV-004Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
- formulation
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- More Info
Description
Recombinant canine Parvovirus VP2 produced in SF9 is a glycosylated, polypeptide chain containing 584 a.a and having a calculated molecular mass of 64,657 Dalton. Parvovirus VP2 is purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Parvovirus VP2 was lyophilized from 30mM NaCl, 20mM Na-phosphate, pH 7.4, 0.01% Tween 20 and 10% trehalose.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Parvovirus VP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Parvovirus VP2 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 Parvovirus VP2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Parvoviruses, small single-stranded DNA viruses, are known for their remarkable stability and diverse host range, causing infections in various animals, including humans. One of the key structural proteins in parvoviruses is VP2, a capsid protein responsible for viral entry and immune recognition. The study of Parvovirus VP2 Recombinant Protein has opened avenues for unraveling the intricacies of viral pathogenesis, host interactions, and has even spurred the development of innovative antiviral therapeutics. This research delves into the significance of Parvovirus VP2 Recombinant Protein, exploring its structural characteristics, functional roles, and its implications in both virology and therapeutic research.
Structural Insights into VP2 Protein:
VP2, forming the viral capsid, is pivotal for parvovirus infectivity. Its unique structural features, including distinct domains responsible for receptor binding and viral entry, provide valuable insights into the viral lifecycle. Understanding the three-dimensional structure of VP2, both in its native form and as a recombinant protein, sheds light on viral assembly, stability, and the mechanisms behind host specificity.
Functional Roles in Viral Pathogenesis:
VP2 plays a central role in determining tissue tropism and immune recognition. Its interactions with host cell receptors influence viral entry, replication, and spread. Additionally, VP2 is a target for neutralizing antibodies, making it a key player in the host immune response. By deciphering VP2's functions, researchers gain crucial knowledge about parvovirus pathogenesis, aiding in the development of antiviral strategies and vaccines.
VP2 Recombinant Protein as a Research Tool:
Recombinant VP2 proteins serve as invaluable tools in virological research. They enable scientists to study viral entry mechanisms, receptor interactions, and immune responses in a controlled laboratory setting. Utilizing VP2 recombinant proteins, researchers can investigate antiviral compounds, study the efficacy of potential vaccines, and explore the dynamics of parvovirus-host interactions, contributing significantly to our understanding of viral infections.
Therapeutic Implications and Vaccine Development:
Parvovirus VP2 has emerged as a promising target for antiviral drug development. By disrupting VP2 interactions with host receptors, researchers are exploring novel therapeutic interventions to inhibit viral entry and replication. Furthermore, insights into VP2 immunogenicity have paved the way for the development of vaccines that trigger robust immune responses against parvovirus infections, offering hope for the prevention and control of these diseases.
Parvovirus VP2 Recombinant Protein, with its pivotal roles in viral pathogenesis and host interactions, has become a cornerstone in parvovirus research. Its structural intricacies, functional significance, and potential therapeutic applications underscore its importance in both basic virology and drug discovery. As our understanding of VP2 continues to expand, it holds the promise of not only unraveling the mysteries of parvovirus infections but also guiding the development of innovative antiviral therapies, ultimately benefiting both human and animal health.
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 :
WIBG HumanDescription:
within BCGN Homolog Human Recombinant
PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.
Product # :
PRO-864Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
WIBG Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-204 a.a.) and having a molecular mass of 23.7 kDa. The WIBG is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
WIBG Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
WIBG is a cooperateing partner of Mago-Y14. The Mago-Y14 heterodimer is a key protein of the EJC(exon junction complex) that is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. WIBG is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. WIBG relates directly with Mago-Y14 by means of its N-terminal domain.
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Synonyms
PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.
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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
MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ QEKGEAEALS RTLDKVSLEE TAQLPSAPQG SRAAPTAASD QPDSAATTEK AKKIKNLKKK LRQVEELQQR IQAGEVSQPS KEQLEKLARR RALEEELEDL ELGLLEHHHH HH.
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 :
PYGL HumanDescription:
Phosphorylase, Glycogen, Liver Human Recombinant
GSD6, Glycogen phosphorylase, liver form.
Product # :
ENZ-675Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
PYGL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 879 amino acids (1-847 a.a) and having a molecular mass of 100.7kDa.PYGL is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PYGL protein solution (0.25mg/ml) in phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycogen phosphorylase (PYGL) converts from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of the PYGL enzyme is further regulated by numerous allosteric effectors and hormonal controls. The liver isozyme supplies the glycemic demands of the body in general whereas the brain and muscle isozymes supply just those tissues.
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Synonyms
GSD6, Glycogen phosphorylase, liver form.
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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 MGSEFELRRQ ASMAKPLTDQ EKRRQISIRG IVGVENVAEL KKSFNRHLHF TLVKDRNVAT TRDYYFALAH TVRDHLVGRW IRTQQHYYDK CPKRVYYLSL EFYMGRTLQN TMINLGLQNA CDEAIYQLGL DIEELEEIEE DAGLGNGGLG RLAACFLDSM ATLGLAAYGY GIRYEYGIFN QKIRDGWQVE EADDWLRYGN PWEKSRPEFM LPVHFYGKVE HTNTGTKWID TQVVLALPYD TPVPGYMNNT VNTMRLWSAR APNDFNLRDF NVGDYIQAVL DRNLAENISR VLYPNDNFFE GKELRLKQEY FVVAATLQDI IRRFKASKFG STRGAGTVFD AFPDQVAIQL NDTHPALAIP ELMRIFVDIE KLPWSKAWEL TQKTFAYTNH TVLPEALERW PVDLVEKLLP RHLEIIYEIN QKHLDRIVAL FPKDVDRLRR MSLIEEEGSK RINMAHLCIV GSHAVNGVAK IHSDIVKTKV FKDFSELEPD KFQNKTNGIT PRRWLLLCNP GLAELIAEKI GEDYVKDLSQ LTKLHSFLGD DVFLRELAKV KQENKLKFSQ FLETEYKVKI NPSSMFDVQV KRIHEYKRQL LNCLHVITMY NRIKKDPKKL FVPRTVIIGG KAAPGYHMAK MIIKLITSVA DVVNNDPMVG SKLKVIFLEN YRVSLAEKVI PATDLSEQIS TAGTEASGTG NMKFMLNGAL TIGTMDGANV EMAEEAGEEN LFIFGMRIDD VAALDKKGYE AKEYYEALPE LKLVIDQIDN GFFSPKQPDL FKDIINMLFY HDRFKVFADY EAYVKCQDKV SQLYMNPKAW NTMVLKNIAA SGKFSSDRTI KEYAQNIWNV EPSDLKISLS NESNKVNGN.
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 :
PLEKHF2 HumanDescription:
Pleckstrin Homology Domain Containing Family F Member 2 Human Recombinant
EAPF, PHAFIN2, ZFYVE18, Pleckstrin homology domain-containing family F member 2, PH domain-containing family F member 2, Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains, PH and FYVE domain-containing protein 2, Zinc finger FYVE domain-containing protein 18, PLEKHF2.
Product # :
PRO-1874Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PLEKHF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-249 a.a) and having a molecular mass of 30.2kDa. PLEKHF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PLEKHF2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
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Introduction
Pleckstrin Homology Domain Containing Family F Member 2, also known as PLEKHF2, contains 1 FYVE-type zinc finger and 1 PH domain. PLEKHF2 takes part in early endosome fusion upstream of RAB5, regulates receptor trafficking and fluid-phase transport. PLEKHF2 increases cellular sensitivity to TNF-induced apoptosis.
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Synonyms
EAPF, PHAFIN2, ZFYVE18, Pleckstrin homology domain-containing family F member 2, PH domain-containing family F member 2, Endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains, PH and FYVE domain-containing protein 2, Zinc finger FYVE domain-containing protein 18, PLEKHF2.
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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 MGSMVDRLAN SEANTRRISI VENCFGAAGQ PLTIPGRVLI GEGVLTKLCR KKPKARQFFL FNDILVYGNI VIQKKKYNKQ HIIPLENVTI DSIKDEGDLR NGWLIKTPTK SFAVYAATAT EKSEWMNHIN KCVTDLLSKS GKTPSNEHAA VWVPDSEATV CMRCQKAKFT PVNRRHHCRK CGFVVCGPCS EKRFLLPSQS SKPVRICDFC YDLLSAGDMA TCQPARSDSY SQSLKSPLND MSDDDDDDDS SD.
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 :
HBsAg adwDescription:
Hepatitis B Surface Antigen, adw Recombinant
Product # :
HBS-872Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.
Source
Pichia Pastoris.
Formulation
Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.
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Physical Appearance
Sterile Filtered pale solution.
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Stability
HBsAg Should be stored at 4°C.DO NOT FREEZE.
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 :
NDRG1 HumanDescription:
N-Myc Downstream Regulated 1 Human Recombinant
Protein NDRG1, N-myc downstream-regulated gene 1 protein, Differentiation-related gene 1 protein, Reducing agents and tunicamycin-responsive protein, Nickel-specific induction protein Cap43, DRG-1, RTP, Rit42, NDRG1, CAP43, DRG1, GC4, NDR1, NMSL, TDD5, CMT4D, HMSNL, TARG1, PROXY1.
Product # :
PRO-724Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NDRG1 Human Recombinant fused with 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 402 amino acids (1-394 a.a.) and having a molecular mass of 43.9 kDa.The NDRG1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDRG1 solution contains 20mM Tris-HCl buffer (pH8.0), 0.1mM PMSF and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using MCF7 cell. The ED50 for this effect is 0.5 - 1.5ng/ml, corresponding to a Specific Activity of 666,000 -2,000,000 IU/mg.More Info
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Introduction
NDRG1 is a cytoplasmic protein that is involved in stress responses, hormone responses, cell growth, and differentiation. NDRG1 is one of 4 members of the NDRG ?/?-hydrolase family. NDRG1 is classified in databases as a tumor suppressor and heavy metal-response protein. NDRG1’s functions include cell-cycle regulation, cellular differentiation, apoptosis, hypoxia response and metal-ion sensing. NDRG1 is also essential for p53-mediated caspase activation and apoptosis. The NDRG1 is a Rab4a effector that is involved in vesicular recycling of E-cadherin. NDRG1 is ubiquitous; it is expressed most notably in placental membranes and prostate, kidney, small intestine, and ovary tissues. NDRG1 has reduced expression in adenocarcinomas compared to normal tissues.
NDRG1 gene mutations are reported to be the cause for hereditary motor and sensory neuropathy-Lom (HMSNL), which is a severe autosomal recessive form of Charcot- Marie-Tooth (CMT) disease. In addition, decreased NDRG1 expression in glioma is linked to tumor progression. On the other hand, overexpression of NDRG1 is connected to malignant status of esophageal cancer. NDRG1 may also have a role in portal vein invasion and intrahepatic metastasis in human hepatocellular carcinoma. -
Synonyms
Protein NDRG1, N-myc downstream-regulated gene 1 protein, Differentiation-related gene 1 protein, Reducing agents and tunicamycin-responsive protein, Nickel-specific induction protein Cap43, DRG-1, RTP, Rit42, NDRG1, CAP43, DRG1, GC4, NDR1, NMSL, TDD5, CMT4D, HMSNL, TARG1, PROXY1.
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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
MSREMQDVDL AEVKPLVEKG ETITGLLQEF DVQEQDIETL HGSVHVTLCG TPKGNRPVIL TYHDIGMNHK TCYNPLFNYE DMQEITQHFA
VCHVDAPGQQ DGAASFPAGY MYPSMDQLAE MLPGVLQQFG LKSIIGMGTG AGAYILTRFA LNNPEMVEGL VLINVNPCAE GWMDWAASKI SGWTQALPDM VVSHLFGKEE MQSNVEVVHT YRQHIVNDMN PGNLHLFINA YNSRRDLEIE RPMPGTHTVT LQCPALLVVG DSSPAVDAVV ECNSKLDPTK TTLLKMADCG GLPQISQPAK LAEAFKYFVQ GMGYMPSASM TRLMRSRTAS GSSVTSLDGT RSRSHTSEGT RSRSHTSEGT RSRSHTSEGA HLDITPNSGA AGNSAGPKSM EVSCLEHHHH HH
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 :
Noggin HumanDescription:
Noggin Human Recombinant
SYM1, SYNS1, NOG.
Product # :
CYT-475Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.
More Info
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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC. -
Background
Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.
Abstract:
Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.
Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.
This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.
Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
- Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.
Molecular Characteristics of Noggin :
- This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.
Inhibition of BMP Signaling by Noggin:
- Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.
Physiological Functions of Noggin:
- Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.
Therapeutic Implications of Noggin:
- The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.
Clinical Studies and Translational Research:
- This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.
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.