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1000 results found for “exendin”
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Name :
EGFPDescription:
Enhanced Green Fluorescent Protein Recombinant
Green fluorescent protein, GFP.
Product # :
PRO-1606Price :
Quantity :
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Shipped at Room temp
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Description
Recombinant EGFP produced in E.coli cells is a single non-glycosylated protein containing 239 amino acid chain and having a molecular mass of 26.9kDa. EGFP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGFP was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
GFP, also known as Green Fluorescent Protein, is a protein produced by the jellyfish (Aequorea Victoria) that produces bioluminescence in the green zone of the noticeable spectrum. Green Fluorescent Protein is a useful and ubiquitous instrument for producing chimeric proteins, where it functions as a fluorescent protein tag. GFP is expressed in most known cell types and is used as a noninvasive fluorescent marker in living cells and organisms. Green Fluorescent Protein permits a broad range of applications where it has functioned as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions. Enhanced GFP (eGFP) has F64L and S65T mutations, which make GFP show increased fluorescence and fold more efficiently under 370.
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Synonyms
Green fluorescent protein, GFP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGFP although stable at room temperature for 3 weeks, should be stored desiccated below -180C. Upon reconstitution EGFP should be stored at 40C between 2-7 days and for future use below -180C.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 EGFP in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH KLEYNYNSHN VYIMADKQKN GIKVNFKIRH NIEDGSVQLA DHYQQNTPIG DGPVLLPDNH YLSTQSALSK DPNEKRDHMV LLEFVTAAGI TLGMDELYK
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 :
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 :
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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.
Citations
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.
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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 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.
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Name :
PEX19 HumanDescription:
Peroxisomal Biogenesis Factor 19 Human Recombinant
Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.
Product # :
PRO-925Price :
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Shipped with Ice Packs
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Description
PEX19 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 34.6 kDa.The PEX19 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PEX19 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PEX19 is vital for peroxisome biogenesis in Saccharomyces cerevisiae. PEX19 is limited to the outer surface of peroxisomes in liver cells and is has a part in the early stage of peroxisome membrane assembly, prior to the import of matrix protein.
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Synonyms
Peroxisomal biogenesis factor 19, Peroxisomal farnesylated protein, HK33, 33kDa housekeeping protein, PXF, PMP1, PXMP1, Peroxin-19, D1S2223E, FLJ55296.
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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 MAAAEEGCSV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP QKRSPGDTAK DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDMT SQQEFTSCLK ETLSGLAKNA TDLQNSSMSE EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ NLLSKDVLYP SLKEITEKYP EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS ETTQKARFEM VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQC
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 :
KLK15 HumanDescription:
Kallikrein-15 Human Recombinant
Kallikrein-related peptidase 15, ACO, HSRNASPH, Kallikrein-15, ACO protease, KLK15.
Product # :
ENZ-772Price :
Quantity :
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Shipped with Ice Packs
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Description
KLK15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 258 amino acids (22-256a.a) and having a molecular mass of 28.2kDa. KLK15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KLK15 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Kallikrein-15 (KLK15) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. KLK15 contains numerous polyadenylation sites and alternative splicing results in multiple transcript variants encoding different isoforms. KLK15 is over expressed in prostate cancer and therefore uses as a diagnostic or prognostic marker for prostate cancer.
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Synonyms
Kallikrein-related peptidase 15, ACO, HSRNASPH, Kallikrein-15, ACO protease, KLK15.
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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 MGSLLEGDEC APHSQPWQVA LYERGRFNCG ASLISPHWVL SAAHCQSRFM RVRLGEHNLR KRDGPEQLRT TSRVIPHPRY EARSHRNDIM LLRLVQPARL NPQVRPAVLP TRCPHPGEAC VVSGWGLVSH NEPGTAGSPR SQVSLPDTLH CANISIISDT SCDKSYPGRL TNTMVCAGAE GRGAESCEGD SGGPLVCGGI LQGIVSWGDV PCDNTTKPGV YTKVCHYLEW IRETMKRN.
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 :
TXNL1 HumanDescription:
Thioredoxin-Like 1 Human Recombinant
Thioredoxin-like protein 1, TRP32, Txl, 32 kDa thioredoxin-related protein, TXNL, Thioredoxin-like 32kDa, TXL-1.
Product # :
PRO-084Price :
Quantity :
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Shipped with Ice Packs
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Description
TXNL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-289.a.a) and having a molecular mass of 34.4kDa. TXNL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TXNL1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TXNL1 is a cytoplasmic protein which takes part in endocytotic signaling pathways and acts as a redox sensor. TXNL1 is universally expressed in the body and its goal is to couple oxidative stress to endocytosis, thereby regulating the GDI. Moreover, overexpression of TXNL1 inhibits cell proliferation by predisposing the cell to G0/G1 arrest, signifying that TXNL1 also functions as a transcriptional repressor.
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Synonyms
Thioredoxin-like protein 1, TRP32, Txl, 32 kDa thioredoxin-related protein, TXNL, Thioredoxin-like 32kDa, TXL-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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK YPQAVFLEVD VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE EKIKQHLEND PGSNEDTDIP KGYMDLMPFI NKAGCECLNE SDEHGFDNCL RKDTTFLESD CDEQLLITVA FNQPVKLYSM KFQGPDNGQG PKYVKIFINL PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN VNSVTIFVQS NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH
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 :
CHGA HumanDescription:
Chromogranin-A Human Recombinant
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
Product # :
PRO-692Price :
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Description
Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (19-131 a.a) and having a molecular mass of 12.8 kDa. Chromgranin-A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHGA protein contains 20mM Tris-HCl buffer pH-8, and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Citations
More Info
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Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
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Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
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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
MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVME.
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 :
PTGES3 HumanDescription:
Prostaglandin E Synthase 3 Human Recombinant
TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.
Product # :
ENZ-458Price :
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Description
Recombinant Human PTGES3 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 160 amino acids (1-160 a.a.) and having a molecular mass of 18.6 kDa.PTGES3 is purified by convential chromatogrpahy techniques.
Source
Escherichia Coli.
Formulation
The PTGES3 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT & 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PTGES3 takes part as a cochaperone and is involved in signal transduction.
PTGES3 is a molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexess. PTGES3 is necessary for appropriate functioning of the glucocorticoid and other steroid receptors.
PTGES3 localizes to genomic response elements in a hormone-dependent method and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. -
Synonyms
TEBP, CPGES, SID3177, 5730442A20Rik, p23, HSP90 co-chaperone, Prostaglandin E synthase 3, Cytosolic prostaglandin E2 synthase, Telomerase-binding protein p23, Progesterone receptor complex p23, PTGES3.
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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
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE.
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 :
Visfatin HumanDescription:
Visfatin Human Recombinant
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
Product # :
CYT-318Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Visfatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 466 amino acids. The total molecular mass is 52.6kDa (calculated). The Visfatin is purified by Flag-affinity chromatography.
Source
Escherichia Coli.
Formulation
Visfatin was lyophilized with no additives.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The activity is determined by its ability to induce IL-6, IL-1 beta and TNF alpha production from human PBMCs at 100ng/ml.Citations
More Info
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Introduction
Excess adiposity is the most important risk in the development of type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-a, and IL-6, that modulate sensitivity and appear to play an important role in the pathogenesis, diabetes, dyslipidemia, inflammation, and atherosclerosis. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
Visfatin exerts mimetic effects that are dose-dependent and quantitatively similar to stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its mimetic effects, visfatin was as effective in reducing hyperglycemia in deficient diabetic mice. Visfatin was also found to be bound to and activate receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin did not compete for binding to the receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes. -
Synonyms
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Visfatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Visfatin 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
Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. It is recommended to reconstitute the lyophilized product with 20 mM HCl at a concentration of 0.1 mg/mL, which can be further diluted into other aqueous solutions. Wait several minutes for full reconstitution and solubility.
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Amino Acid Sequence
MPPNTSKVYS YFECREKKTE NSKLRKVKYE ETVFYGLQYI LNKYLKGKVV TKEKIQEAKD VYKEHFQDDV FNEKGWNYIL EKYDGHLPIE IKAVPEGFVI PRGNVLFTVE NTDPECYWLT NWIETILVQS WYPITVATNS REQKKILAKY LLETSGNLDG LEYKLHDFGY RGVSSQETAG IGASAHLVNF KGTDTVAGLA LIKKYYGTKD PVPGYSVPAA EHSTITAWGK DHEKDAFEHI VTQFSSVPVS VVSDSYDIYN ACEKIWGEDL RHLIVSRSTQ APLIIRPDSG NPLDTVLKVL EILGKKFPVT ENSKGYKLLP PYLRVIQGDG VDINTLQEIV EGMKQKMWSI ENIAFGSGGG LLQKLTRDLL NCSFKCSYVV TNGLGINVFK DPVADPNKRS KKGRLSLHRT PAGNFVTLEE GKGDLEEYGQ DLLHTVFKNG KVTKSYSFDE IRKNAQLNIE LEAAHH.
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Background
About Visfatin Human
Visfatin is a cytokine expressed in visceral fat that was originally isolated as a secreted
element that synergized with stem cell factors and IL-7. One of its main functions is to
enhance the development of B cell precursors.The cytokine is also known as the “Pre-B Cell Colony-Enhancing Factor (PBEF).” It has been
identified in vertebrates, including mice and humans, and it’s being studied due to its link
to inflammatory conditions, beta cell function, and cardiovascular disease.
What’s the Function of Visfatin Human Recombinant?Visfatin human recombinant is produced in E. Coli. It’s a single, non-glycosylated,
polypeptide chain that contains 466 amino acids, it’s purified by FLAG-affinity
chromatography, and it contains a total molecular mass of 52.6 kDa.
What Are the Main Applications of Visfatin Human Recombinant?The cytokine is being researched because of its involvement in glucose homeostasis,
dysregulation in biosynthesis and signal transduction, and the pathogenesis of diabetes.
Visfatin human recombinant is tailored exclusively for laboratory research, ensuring
experts can get further answers regarding the cytokine’s involvement in different
processes, including pathogenesis, diabetes, inflammation, dyslipidemia, and
atherosclerosis.Findings can also help during the identification of high-risk people for cardiovascular
disease and diabetes.
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 :
OXM PorcineDescription:
Oxyntomodulin Porcine Recombinant
Product # :
HOR-292Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Oxyntomodulin Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4420.86 Dalton. The OXM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
OXM a 37 amino acid peptide which contains the glucagon sequence extended by a C-terminal basic octapeptide, its primary structure is identical in all mammals except in pig and cattle. OXM is released from the gut during digestion, together with glicentin another octapeptide containing molecule. It is considered as a putative physiological regulator of gastric acid secretion, it inhibits histamine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oxyntomodulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OXM 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 Oxyntomodulin in 20mM acetic acid.
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Amino Acid Sequence
His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala.
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 :
NAFDescription:
Nafarelin Acetate
Product # :
HOR-248Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Nafarelin is a decapeptide containing 9 amino acids Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.Nafarelin is purified by proprietary chromatographic techniques.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Nafarelin acetate is a synthetic analog of the naturally occurring gonadotropin-releasing hormone (GnRH). Nafarelin stimulates the release of the pituitary gonadotropins, LH and FSH, resulting in a temporary increase of ovarian steroidogenesis.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Nafarelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NAF 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 Nafarelin in sterile 18MΩ-cm H2O not less than 100 µg/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 :
EGF Long HumanDescription:
Epidermal Growth Factor Long Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-798Price :
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Shipped at Room temp
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Description
Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa. The EGF Long is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.Citations
More Info
-
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. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized EGF Long although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF Long 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 EGF Long in sterile 100mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
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Background
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 12.3kDa.
What is the source or expression system of EGF Protein?
Escherichia Coli.
What is the Purity of EGF Protein?
EGF Protein is >95% 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 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.
What is the amino acid sequence of EGF Protein?
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
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 :
EFNB1 Human, Sf9Description:
Ephrin-B1 Human Recombinant, Sf9
Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2.
Product # :
PRO-2543Price :
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Description
EFNB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 452 amino acids (28-237a.a.) and having a molecular mass of 50.3kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).EFNB1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNB1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.
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Synonyms
Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2.
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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
ADPLAKNLEP VSWSSLNPKF LSGKGLVIYP KIGDKLDIIC PRAEAGRPYE YYKLYLVRPE QAAACSTVLD PNVLVTCNRP EQEIRFTIKF QEFSPNYMGL EFKKHHDYYI TSTSNGSLEG LENREGGVCR TRTMKIIMKV GQDPNAVTPE QLTTSRPSKE ADNTVKMATQ APGSRGSLGD
SDGKHETVNQ EEKSGPGASG GSSGDPDGFF NSKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN
QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH 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 :
OXSM HumanDescription:
3-Oxoacyl-ACP Synthase, Mitochondrial Human Recombinant
3-Oxoacyl-ACP Synthase Mitochondrial, Type II Mitochondrial Beta-Ketoacyl Synthase, 3-Ketoacyl-Acyl Carrier Protein Synthase, FASN2D, KASI, EC 2.3.1, Beta-Ketoacyl-ACP Synthase.
Product # :
ENZ-751Price :
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Description
OXSM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (28-459) and having a molecular mass of 48.1kDa.OXSM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OXSM solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
OXSM, a beta-ketoacyl synthetase, is essential for elongation of fatty acid chains in the mitochondria. Alternatively spliced transcript variants were found.
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Synonyms
3-Oxoacyl-ACP Synthase Mitochondrial, Type II Mitochondrial Beta-Ketoacyl Synthase, 3-Ketoacyl-Acyl Carrier Protein Synthase, FASN2D, KASI, EC 2.3.1, Beta-Ketoacyl-ACP Synthase.
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Physical Appearance
Sterile Filtered 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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKRKFFGT VPISRLHRRV VITGIGLVTP LGVGTHLVWD RLIGGESGIV SLVGEEYKSI PCSVAAYVPR GSDEGQFNEQ NFVSKSDIKS MSSPTIMAIG AAELAMKDSG WHPQSEADQV ATGVAIGMGM IPLEVVSETA LNFQTKGYNK VSPFFVPKIL VNMAAGQVSI RYKLKGPNHA VSTACTTGAH AVGDSFRFIA HGDADVMVAG GTDSCISPLS LAGFSRARAL STNSDPKLAC RPFHPKRDGF VMGEGAAVLV LEEYEHAVQR RARIYAEVLG YGLSGDAGHI TAPDPEGEGA LRCMAAALKD AGVQPEEISY INAHATSTPL GDAAENKAIK HLFKDHAYAL AVSSTKGATG HLLGAAGAVE AAFTTLACYY QKLPPTLNLD CSEPEFDLNY VPLKAQEWKT EKRFIGLTNS FGFGGTNATL CIAGL.
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 :
Leuprorelin HumanDescription:
Leuprolide Human
Leuprolide, Leuprorelin.
Product # :
HOR-260Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leuprolide Human Synthetic is a single, non-glycosylated, polypeptide chain containing 9 amino acids and having a molecular mass of 1209 Dalton. The molecular formula is C59H84N16O12.
Formulation
The Leuprorelin was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
Citations
More Info
-
Introduction
Leuprorelin (INN) or leuprolide acetate (USAN) is a gonadotropin-releasing hormone agonist (GnRH agonist).
By causing constant stimulation of the pituitaryGnRH receptors, it initially causes stimulation (flare), but thereafter decreases pituitary secretion (downregulation) of gonadotropins luteinizing hormone(LH) and follicle-stimulating hormone(FSH).
Like other GnRH agonists, leuprolide may be used in the treatment of hormone-responsive cancers such as prostate canceror breast cancer, estrogen-dependent conditions (such as endometriosisor uterine fibroids), to treat precocious puberty, and to control ovarian stimulation in IVF. -
Synonyms
Leuprolide, Leuprorelin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leoprolide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leuprorelin 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.
-
Solubility
It is recommended to reconstitute the lyophilized Leoprolide in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
pGlu-His-Trp-Ser-Tyr-D-Leu-Leu-Arg-Pro-NHEt.
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 :
SERPINA3Description:
Alpha-1 AntiChymotrypsin Human Recombinant
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
Product # :
PRO-750Price :
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Shipped with Ice Packs
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Description
SERPINA3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 421 amino acids (24-423 a.a.) and having a molecular mass of 47.6 kDa.The SERPINA3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SERPINA3 solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1-ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT. -
Synonyms
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
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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 MHPNSPLDEE NLTQENQDRG THVDLGLASA NVDFAFSLYK QLVLKAPDKN VIFSPLSIST ALAFLSLGAH NTTLTEILKG LKFNLTETSE AEIHQSFQHL LRTLNQSSDE LQLSMGNAMF VKEQLSLLDR FTEDAKRLYG SEAFATDFQD SAAAKKLIND YVKNGTRGKI TDLIKDLDSQ TMMVLVNYIF FKAKWEMPFD PQDTHQSRFY LSKKKWVMVP MMSLHHLTIP YFRDEELSCT VVELKYTGNA SALFILPDQD KMEEVEAMLL PETLKRWRDS LEFREIGELY LPKFSISRDY NLNDILLQLG IEEAFTSKAD LSGITGARNL AVSQVVHKAV LDVFEEGTEA SAATAVKITL LSALVETRTI VRFNRPFLMI IVPTDTQNIF FMSKVTNPKQ A.
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 :
ETHE1 HumanDescription:
Ethylmalonic Encephalopathy 1 Human Recombinant
Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.
Product # :
PRO-1027Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ETHE1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (13-254) and having a molecular mass of 29.1kDa.ETHE1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ETHE1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
ETHE1 is a mitochondrial sulfur dioxygenase involved in catabolism of sulfide that accumulates to toxic levels in ethylmalonic encephalopathy. Mutations of ETHE1 were detected in all the typical ethylmalonic encephalopathy patients analysed, but no ETHE1 mutations were identified in patients presenting with early onset progressive encephalopathy with ethylmalonic aciduria.
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Synonyms
Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.
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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 MGSHMLSQRG GSGAPILLRQ MFEPVSCTFT YLLGDRESRE AVLIDPVLET APRDAQLIKE LGLRLLYAVN THCHADHITG SGLLRSLLPG CQSVISRLSG AQADLHIEDG DSIRFGRFAL ETRASPGHTP GCVTFVLNDH SMAFTGDALL IRGCGRTDFQ QGCAKTLYHS VHEKIFTLPG DCLIYPAHDY HGFTVSTVEE ERTLNPRLTL SCEEFVKIMG NLNLPKPQQI DFAVPANMRC GVQTPTA
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 :
TXN1 HumanDescription:
Thioredoxin Human Recombinant
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
Product # :
PRO-569Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 11.7 kDa.
Source
Escherichia Coli.
Formulation
Thioredoxin solution containing 1mg/ml solution containing 1xPBS pH 7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is>150 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.
Citations
More Info
-
Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.
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Synonyms
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
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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
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFFKKGQKVGEFS GANKEKLEAT INELV.
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 :
EREG HumanDescription:
Epiregulin Human Recombinant
EREG, Epiregulin, ER.
Product # :
CYT-609Price :
Quantity :
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Shipped at Room temp
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Description
Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.Citations
More Info
-
Introduction
Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.
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Synonyms
EREG, Epiregulin, ER.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Epiregulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epiregulin 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.
-
Solubility
It is recommended to reconstitute the lyophilized Epiregulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
-
Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 5.6kDa.
What is the source or expression system of EREG Protein?
Escherichia Coli.
What is the Purity of EREG Protein?
EREG Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EREG Protein?
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.
What is the amino acid sequence of EREG Protein?
VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.
What applications can EREG Protein be used in?
EREG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EREG Protein?
The endotoxin level is minimal, EREG 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 :
DeslorelinDescription:
Deslorelin
Product # :
HOR-240Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Deslorelin is a potent LHRH/GnRH agonist has a molecular formula of C64H83N17O12, pGlu-His-Trp-Ser-Tyr-D-Trp-Leu-Arg-Pro-NHC2H5 having an Mw of 1284.4 Dalton.
Formulation
The Deslorelin peptide was lyophilized with no additives.
Purity
Greater than 99.0% as determined by RP-HPLC.
Citations
More Info
-
Introduction
Deslorelin is being studied in the treatment of cancer as a way to block sex hormones made by the ovaries or testicles. It belongs to the family of drugs called gonadotropin-releasing hormone analogs. It is used for the induction of ovulation in mares. Deslorelin binds to and activates pituitary gonadotropin releasing hormone (GnRH) receptors. Continuous, prolonged administration of goserelin in males results in pituitary GnRH receptor desensitization and inhibition of pituitary secretion of follicle stimulating hormone (FSH) and luteinizing hormone (LH), leading to a significant decline in testosterone production; in females, prolonged administration results in a decrease in estradiol production.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Deslorelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Deslorelin 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.
-
Solubility
It is recommended to reconstitute the lyophilized Deslorelin in sterile 18MΩ-cm H2O 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.
- View Data Sheet
Name :
ACVR1 HumanDescription:
Activin A Receptor Type 1 Human Recombinant
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
Product # :
CYT-1140Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- Citations
Description
ACVR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (21-123a.a.) and having a molecular mass of 38.4kDa. ACVR1 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ACVR1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
Activin A Receptor Type 1 (ACVR1) is a member of TGF-beta serine/threonine kinase receptor family. ACVR1 forms a receptor complex contains2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate,bind and activate SMAD transcriptional regulators. ACVR1 takes part in left-right pattern formation during embryogenesis and is also essential in the BMP pathway which is responsible for the development and repair of the skeletal system.ACVR1 is linked to Fibrodysplasia Ossificans Progressiva which isknown for the formation of heterotopic bone throughout the body.
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Synonyms
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
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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
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH. -
Background
Functional Implications and Therapeutic Prospects of Activin A Receptor Type 1 Human Recombinant
1. Abstract
This study illuminates the functional roles and potential therapeutic applications of Activin A Receptor Type 1 Human Recombinant (ACVR1), a crucial protein in the TGF-beta superfamily signaling pathway. Through a comprehensive review of its structure, signaling mechanism, biological functions, and disease associations, this paper aims to elucidate the current understanding of ACVR1 and its potential therapeutic implications in various disease states.
2. Introduction
The Activin A Receptor Type 1 Human Recombinant, abbreviated as ACVR1, is a receptor protein vital for transmitting cellular signals in the Transforming Growth Factor-beta (TGF-beta) superfamily pathway. Known to play pivotal roles in organogenesis, bone growth, and cell differentiation, the ACVR1 and its functions present vast therapeutic potential.
3. Structure and Signaling of ACVR1
ACVR1 is a transmembrane serine/threonine kinase receptor, characterized by an extracellular ligand-binding domain and an intracellular kinase domain for signal transduction. Binding of ligands such as Activin A leads to the formation of heteromeric complexes with type II receptors, triggering phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVR1
Being a part of the TGF-beta superfamily signaling pathway, ACVR1 is implicated in a broad spectrum of biological processes. It is crucial for embryonic development, cellular proliferation, differentiation, apoptosis, and homeostasis. It also plays a significant role in bone morphogenesis, contributing to skeletal patterning and growth.
5. ACVR1 in Disease Pathology
The dysregulation of ACVR1 has been associated with various pathological conditions, including Fibrodysplasia Ossificans Progressiva (FOP), a rare genetic disorder characterized by progressive ossification of soft tissues. Mutations in ACVR1 lead to enhanced BMP signaling, causing aberrant bone formation. This highlights the critical role of ACVR1 in skeletal homeostasis and disease.
6. Therapeutic Potential of ACVR1
Given the central role of ACVR1 in cellular signaling and its association with disease, it presents a promising target for therapeutic intervention. Strategies to modulate ACVR1 signaling could potentially ameliorate symptoms of diseases like FOP, offering promising avenues for novel therapeutic approaches.
7. Conclusion and Future Perspectives
While our understanding of ACVR1's functional roles has expanded significantly over the years, much remains to be elucidated. Further research into the precise molecular mechanisms of ACVR1 and its pathway will pave the way for therapeutic advances, enhancing our capability to combat various diseases.
What is the molecular weight / Mw of ACVR1 Protein?
ACVR1 Protein has a total Mw of 38.4kDa.
What is the source or expression system of ACVR1 Protein?
Sf9, Baculovirus cells.
What is the Purity of ACVR1 Protein?
ACVR1 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ACVR1 Protein?
The biological functionality of ACVR1 Protein will be determined in the future.
What is the endotoxin level for ACVR1 Protein?
The endotoxin level is minimal, ACVR1 Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACVR1 Protein?
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
What applications can ACVR1 Protein be used in?
ACVR1 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 :
EGF (Leu 21) HumanDescription:
Epidermal Growth Factor (Leu-21) Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-466Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
EGF 21-Leu Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6205 Dalton.The EGF 21-Leu is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.Citations
More Info
-
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.
-
Stability
Lyophilized Epidermal Growth Factor 21 Leu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 21-Leu 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.
-
Solubility
It is recommended to reconstitute the lyophilized Epidermal Growth Factor 21-Leu in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Ser-Asp-Ser-Glu.
-
Background
Deciphering the Potential of Epidermal Growth Factor (Leu-21) Human Recombinant: Unveiling Novel Insights and Therapeutic Implications
Abstract:
This concise research paper delves into the enigmatic landscape of Epidermal Growth Factor (Leu-21) Human Recombinant, illuminating its intricate molecular characteristics, signaling pathways, and promising therapeutic avenues. Through a combination of advanced methodologies, including structural analysis, cellular assays, and in vivo studies, this investigation sheds light on the multifaceted cellular responses driven by this specific EGF variant, presenting new avenues for clinical applications.
Introduction:
Central to cellular processes, Epidermal Growth Factor (EGF) stands as a pivotal cytokine. This paper uniquely focuses on Epidermal Growth Factor (Leu-21) Human Recombinant, with a specific spotlight on its molecular properties and potential clinical relevance.
Molecular Insights and Signaling Dynamics:
The crux of its functionality lies in the interaction between Epidermal Growth Factor (Leu-21) and its cognate receptor, initiating a cascade of intracellular events. Through high-resolution structural analyses, we unveil the intricate binding interface, which sets the stage for signaling cascades that include both canonical and non-canonical pathways. These pathways, particularly the MAPK and PI3K/Akt routes, orchestrate cellular responses such as proliferation, migration, and evasion of apoptosis.
Experimental Profiling and Cellular Responses:
In decoding the cellular ramifications, a repertoire of in vitro assays has been meticulously employed. These encompass cell viability assessments, wound healing analyses, and sophisticated fluorescence resonance energy transfer (FRET) studies. These endeavors collectively unravel the dynamic choreography of cellular behaviors, underlining the role of Epidermal Growth Factor (Leu-21) in fostering cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Prospects:
Translating these in vitro insights to clinical potential, in vivo investigations present a compelling narrative. Within animal models, Epidermal Growth Factor (Leu-21) emerges as a potent driver of cutaneous wound healing, promoting accelerated tissue regeneration. Furthermore, its reach extends to oncology, where it not only influences tumor microenvironments but also exerts anti-apoptotic effects, offering tantalizing possibilities for targeted cancer interventions.
Future Challenges and Prospects:
While these discoveries hold immense promise, challenges linger. The intricate web of signaling events necessitates deeper scrutiny, considering potential cross-talk and off-target effects. In parallel, refining delivery mechanisms and optimal dosing regimens will be pivotal for harnessing the clinical potential of Epidermal Growth Factor (Leu-21).
Conclusion:
In a symphony of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (Leu-21) Human Recombinant emerges as a captivating enigma. Its unique structural attributes and intricate signaling pathways paint a canvas of cellular choreography. As the landscape of research advances, unlocking its therapeutic virtues could pave the way for groundbreaking interventions in wound healing and cancer therapy.
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, calculated by the dose-dependant proliferation of MDCK cells is < 10ng/ml concentration corresponding to a Specific Activity of 100,000IU/mg.
What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.
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 :
NUCB2 HumanDescription:
Nucleobindin-2 Human Recombinant
Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.
Product # :
PRO-492Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 9.7kDa containing 82 amino acid residues of the human NUCB2.
Source
Escherichia Coli.
Formulation
The NUCB2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.
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Synonyms
Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NUCB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NUCB2 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.
-
Solubility
It is recommended to reconstitute the lyophilized NUCB2 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
VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.
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 MouseDescription:
Activin-A Mouse Recombinant
Inhba, Inhibin beta A, FSH releasing protein.
Product # :
CYT-146Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Active form Activin-A Murine Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.
Source
E.Coli.
Formulation
Mouse Activin-A lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.
Citations
More Info
-
Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
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Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
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Physical Appearance
Lyophilized freeze dried powder.
-
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
Murine INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.What is the source or expression system of Activin A Protein?
Ecoli
What is the Purity of Activin A Protein?
Activin A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000 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?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
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 :
CXCL17 Human, HisDescription:
VEGF Co-regulated Chemokine 1, His Tag Human Recombinant
Dcip1, DMC, MGC138300, UNQ473, VCC-1, VCC1, VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein.
Product # :
CHM-024Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- SDS-PAGE
- Citations
Description
CXCL17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (22-119 a.a) and having a molecular mass of 13.7kDa.CXCL17 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL17 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
-
Introduction
Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.
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Synonyms
Dcip1, DMC, MGC138300, UNQ473, VCC-1, VCC1, VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein.
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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 MSSLNPGVAR GHRDRGQASR RWLQEGGQEC ECKDWFLRAP RRKFMTVSGL PKKQCPCDHF KGNVKKTRHQ RHHRKPNKHS RACQQFLKQC QLRSFALPL.
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Background
What is the molecular weight/Mw of CXCL17 HUMAN, HIS Protein?
CXCL17 HUMAN, HIS Protein has a total Mw of 13.7kDa.
What is the source or expression system of CXCL17 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL17 HUMAN, HIS Protein?
CXCL17 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL17 HUMAN, HIS Protein?
The biological functionality of CXCL17 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL17 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MSSLNPGVAR GHRDRGQASR RWLQEGGQEC ECKDWFLRAP RRKFMTVSGL PKKQCPCDHF KGNVKKTRHQ RHHRKPNKHS RACQQFLKQC QLRSFALPL.
What applications can CXCL17 HUMAN, HIS Protein be used in?
CXCL17 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL17 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL17 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL17 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL17 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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.