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1000 results found for “Retinol Binding Protein”
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Name :
Eotaxin HumanDescription:
Eotaxin Human Recombinant (CCL11)
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
Product # :
CHM-256Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Eotaxin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8345.9 Dalton. The CCL11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.More Info
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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL11 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 Eotaxin Human Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD
SMKYLDQKSP TPKP.
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Background
What is the molecular weight/Mw of EOTAXIN HUMAN Protein?
EOTAXIN HUMAN Protein has a total Mw of 8.3459kDa.
What is the source or expression system of EOTAXIN HUMAN Protein?
Escherichia Coli.
What is the Purity of EOTAXIN HUMAN Protein?
EOTAXIN HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN HUMAN Protein?
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 0.1-10 ng/ml corresponding to a Specific Activity of 100,000-10,000,000IU/mg.
What is the amino acid sequence of EOTAXIN HUMAN Protein?
GPASVPTTCC FNLANRKIPL QRLESYRRIT SGKCPQKAVI FKTKLAKDICADPKKKWVQD
SMKYLDQKSP TPKP.
What applications can EOTAXIN HUMAN Protein be used in?
EOTAXIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN HUMAN Protein?
The endotoxin level is minimal, EOTAXIN HUMAN 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 :
NCL HumanDescription:
Nucleolin Human Recombinant
Nucleolin, Protein C23, NCL, C23.
Product # :
PRO-1508Price :
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Description
Nucleolin Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing the C-terminal section of the human nucleolin and missing the N-terminal histone-binding part of nucleolin, having a calculated molecular mass of 55,162 Dalton. NCL is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
NCL is supplied in 20mM HEPES pH-7.3, 600mM NaCl, 0.3mM Tris(2-carboxyethyl)phosphine (TCEP) and 25% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Nucleolin (NCL) which is a eukaryotic nucleolar phosphoprotein, involved in the synthesis and maturation of ribosomes. Nucleolin is the key nucleolar protein of growing eukaryotic cells. NCL is found linked with intranucleolar chromatin and pre-ribosomal particles. NCL induces chromatin decondensation by binding to histone H1. Nucleolin is assumed to have a role in pre-rRNA transcription and ribosome compilation. Nucleolin may also have a role in the process of transcriptional elongation. Nucleolin is located primarily in the dense fibrillar regions of the nucleolus. The Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb.
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Synonyms
Nucleolin, Protein C23, NCL, C23.
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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. Avoid multiple freeze-thaw cycles.
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 :
BMPR1A Human, IgG-HisDescription:
Bone Morphogenetic protein Receptor-1A Human Recombinant, IgG-His
BMPR1A, 10q23del, ACVRLK3, ALK3, CD292, SKR5, Bone Morphogenetic Protein Receptor Type 1A, Bone Morphogenetic Protein Receptor, Type IA, Serine/Threonine-Protein Kinase Receptor R5, Activin Receptor-Like Kinase 3, BMP Type-1A Receptor, EC 2.7.11.30, ALK-3, Bone Morphogenetic Protein Receptor Type-1A, Activin A Receptor, Type II-Like Kinase 3, CD292 Antigen, EC 2.7.1.
Product # :
CYT-1005Price :
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Description
BMPR1A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 371 amino acids (24-152a.a.) and having a molecular mass of 41.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BMPR1A is fused with a 242 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
BMPR1A protein solution (1mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas and activins transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.
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Synonyms
BMPR1A, 10q23del, ACVRLK3, ALK3, CD292, SKR5, Bone Morphogenetic Protein Receptor Type 1A, Bone Morphogenetic Protein Receptor, Type IA, Serine/Threonine-Protein Kinase Receptor R5, Activin Receptor-Like Kinase 3, BMP Type-1A Receptor, EC 2.7.11.30, ALK-3, Bone Morphogenetic Protein Receptor Type-1A, Activin A Receptor, Type II-Like Kinase 3, CD292 Antigen, EC 2.7.1.
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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
ADPQNLDSML HGTGMKSDSD QKKSENGVTL APEDTLPFLK CYCSGHCPDD AINNTCITNG HCFAIIEEDD QGETTLASGC MKYEGSDFQC KDSPKAQLRR TIECCRTNLC NQYLQPTLPP VVIGPFFDGS IRLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
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Background
Research Paper on Bone Morphogenetic Protein Receptor-1A Human Recombinant, IgG-His, Monomer, HEK
Abstract:
Welcome to the fascinating world of Bone Morphogenetic Protein Receptor-1A Human Recombinant, IgG-His, Monomer (BMPR-1A HR) in Human Embryonic Kidney Cells (HEK). This paper explores the vital role of BMPR-1A HR in cellular responses. As a critical receptor in the transforming growth factor-beta (TGF-β) superfamily, BMPR-1A HR guides cellular differentiation and tissue development. Join us as we uncover the molecular mechanisms behind BMPR-1A HR signaling in HEK cells and explore its synonyms, along with its interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Step into the captivating realm of BMPR-1A HR! This paper introduces the remarkable BMPR-1A HR and its crucial role in shaping cellular responses. As researchers, we are driven by curiosity to understand how BMPR-1A HR influences cellular behavior and contributes to tissue growth.
BMPR-1A HR Signaling in HEK Cells:
Unravel the intricate dance of BMPR-1A HR signaling within HEK cells! We explore the complex process of ligand-receptor binding, which initiates both the canonical SMAD-dependent and non-canonical SMAD-independent pathways, regulating gene transcription, cell proliferation, and differentiation.
Extensive Description of BMPR-1A HR:
As researchers, we provide a comprehensive overview of BMPR-1A HR's structural characteristics and unique attributes. With its Monomeric nature and the IgG-His tag, crucial for detection and purification, we delve into the intricacies of BMPR-1A HR.
Influential Role in Cellular Responses:
Marvel at BMPR-1A HR's influential role as a critical mediator of cellular responses within HEK cells! Witness how it skillfully modulates cellular differentiation, driving the expression of key differentiation markers like DIF, impacting diverse cellular pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMPR-1A HR and key cytokines like TNF-α and TNFSF2, fostering efficient cellular responses.
Therapeutic Implications and Tissue Development:
Explore the potential therapeutic implications of BMPR-1A HR in tissue development. We envision exciting possibilities of utilizing BMPR-1A HR in regenerative medicine, offering hope for enhanced tissue development and repair.
Conclusion:
As we conclude our exploration of BMPR-1A HR in HEK cells, we anticipate a promising future where BMPR-1A HR with an IgG-His tag becomes an invaluable tool in biomedical research, promoting human well-being.
What is the molecular weight/Mw of BMPR1A Protein?
BMPR1A Protein has a total Mw of 41.4kDa.
What is the source or expression system of BMPR1A Protein?
Sf9, Baculovirus cells.
What is the Purity of BMPR1A Protein?
BMPR1A Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMPR1A Protein?
The biological functionality of BMPR1A Protein will be determined in the future.
What is the amino acid sequence of BMPR1A Protein?
ADPQNLDSML HGTGMKSDSD QKKSENGVTL APEDTLPFLK CYCSGHCPDD AINNTCITNG HCFAIIEEDD QGETTLASGC MKYEGSDFQC KDSPKAQLRR TIECCRTNLC NQYLQPTLPP VVIGPFFDGS IRLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
What applications can BMPR1A Protein be used in?
BMPR1A Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMPR1A Protein?
The endotoxin level is minimal, BMPR1A 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 :
RLN2 Human, Sf9Description:
Relaxin-2 Human Recombinant, Sf9
Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.
Product # :
PRO-2406Price :
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Shipped with Ice Packs
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Description
RLN2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (25-185a.a.) and having a molecular mass of 19.3kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).RLN2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
RLN2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Prorelaxin H2 (RLN2) is a member of the insulin gene superfamily. This family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing oxytocin and vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.
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Synonyms
Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.
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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
ADPDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFCHHHHHH.
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 :
ATP5H HumanDescription:
ATP Synthase Mitochondrial Fo Complex Subunit D Human Recombinant
ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit D, ATP Synthase D Chain Mitochondrial, ATP Synthase H+ Transporting Mitochondrial F1F0 Subunit D, ATPase Subunit D, My032 Protein, ATPQ.
Product # :
PRO-1631Price :
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Shipped with Ice Packs
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Description
ATP5H Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (1-161) and having a molecular mass of 20.9kDa.ATP5H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ATP5H solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
ATP5H is a member of the ATPase d subunit family and encodes the d subunit of the F0 complex. Electron transport complexes of the respiratory chain create a proton gradient across the membrane which induces ATP5H to transform ADP to ATP. Two alternatively spliced isoforms of ATP5H, encoded by a gene that maps to human chromosome 17q25.1, are known. ATP5H is restricted to mitochondrial inner membrane.
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Synonyms
ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit D, ATP Synthase D Chain Mitochondrial, ATP Synthase H+ Transporting Mitochondrial F1F0 Subunit D, ATPase Subunit D, My032 Protein, ATPQ.
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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 MGSMAGRKLA LKTIDWVAFA EIIPQNQKAI ASSLKSWNET LTSRLAALPE NPPAIDWAYY KANVAKAGLV DDFEKKFNAL KVPVPEDKYT AQVDAEEKED VKSCAEWVSL SKARIVEYEK EMEKMKNLIP FDQMTIEDLN EAFPETKLDK KKYPYWPHQP IENL
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Leptin qA Ovine, PEGDescription:
Leptin Quadruple Antagonist Pegylated Ovine Recombinant
Product # :
CYT-1246Price :
Quantity :
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Shipped at Room temp
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Description
Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM 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 Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted 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 mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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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.
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Name :
LAYN HumanDescription:
Layilin Human Recombinant
Layilin
Product # :
PRO-1629Price :
Quantity :
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Shipped with Ice Packs
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Description
LAYN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (22-235) and having a molecular mass of 26.7kDa.LAYN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LAYN solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
LAYN, also known as Layilin, contains 1 c-type lectin domain. This protein is receptor for hyaluronate and Interacts with NF2, RDX and TLN1. The C-terminal domain interacts with the N-terminal domain of RDX.
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Synonyms
Layilin
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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 MGSATGRLLS ASDLDLRGGQ PVCRGGTQRP CYKVIYFHDT SRRLNFEEAK EACRRDGGQL VSIESEDEQK LIEKFIENLL PSDGDFWIGL RRREEKQSNS TACQDLYAWT DGSISQFRNW YVDEPSCGSE VCVVMYHQPS APAGIGGPYM FQWNDDRCNM KNNFICKYSD EKPAVPSREA EGEETELTTP VLPEETQEED AKKTFKESRE AALNLAY
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 :
UTP23 HumanDescription:
UTP23, Small Subunit Processome Component Human Recombinant
UTP23 Small Subunit (SSU) Processome Component, Homolog (Yeast), Chromosome 8 Open Reading Frame 53, RRNA-Processing Protein UTP23 Homolog, MGC14595, C8orf53.
Product # :
PRO-1235Price :
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Description
UTP23 Human Recombinant produced in E. coli is a single polypeptide chain containing 272 amino acids (1-249) and having a molecular mass of 30.8 kDa.UTP23 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The UTP23 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
rRNA-processing protein UTP23 homolog (UTP23) is a small subunit (SSU) processome component. The SSU processome is a complex involved in ribosome biogenesis and essential for pre-18S rRNA maturation. UTP23 is vital for the first 3 cleavage steps in 18S rRNA maturation. Furthermore, single-point mutations in the conserved putative active site of Utp24 but not Utp23 annul its function in ribosome biogenesis.
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Synonyms
UTP23 Small Subunit (SSU) Processome Component, Homolog (Yeast), Chromosome 8 Open Reading Frame 53, RRNA-Processing Protein UTP23 Homolog, MGC14595, C8orf53.
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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 MGSMKITRQK HAKKHLGFFR NNFGVREPYQ ILLDGTFCQA ALRGRIQLRE QLPRYLMGET QLCTTRCVLK ELETLGKDLY GAKLIAQKCQ VRNCPHFKNA VSGSECLLSM VEEGNPHHYF VATQDQNLSV KVKKKPGVPL MFIIQNTMVL DKPSPKTIAF VKAVESGQLV SVHEKESIKH LKEEQGLVKN TEQSRRKKRK KISGPNPLSC LKKKKKAPDT QSSASEKKRK RKRIRNRSNP KVLSEKQNAE GE
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 :
COPE HumanDescription:
Coatomer Protein Complex Subunit Epsilon Human Recombinant
Coatomer Protein Complex, Subunit Epsilon, Epsilon-Coat Protein, Epsilon-COP, Coatomer Epsilon Subunit, Coatomer Subunit Epsilon, Epsilon Coat Protein, Coatomer subunit epsilon.
Product # :
PRO-2120Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
COPE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 36.9kDa. COPE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
COPE protein solution (0.25 mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Coatomer Protein Complex SubunitEpsilon, also known as COPE is an epsilon subunit of coatomer protein complex. Coatomer is a cytosolic protein complex which binds to dilysine motifs and reversibly links with Golgi non-clathrin-coated vesicles. COPE is necessary forbudding from Golgi membranes, and is also essential for the retrograde Golgi-to-ER transport of dilysine-taggedproteins. Coatomer complex contain at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Alternatively spliced transcript variants encoding dissimilar isoforms have been identifiedfor COPE.
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Synonyms
Coatomer Protein Complex, Subunit Epsilon, Epsilon-Coat Protein, Epsilon-COP, Coatomer Epsilon Subunit, Coatomer Subunit Epsilon, Epsilon Coat Protein, Coatomer subunit epsilon.
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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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPPAPG PASGGSGEVD ELFDVKNAFY IGSYQQCINE AQRVKLSSPE RDVERDVFLY RAYLAQRKFG VVLDEIKPSS APELQAVRMF ADYLAHESRR DSIVAELDRE MSRSVDVTNT TFLLMAASIY LHDQNPDAAL RALHQGDSLE CTAMTVQILL KLDRLDLARK ELKRMQDLDE DATLTQLATA WVSLATGGEK LQDAYYIFQE MADKCSPTLL LLNGQAACHM AQGRWEAAEG LLQEALDKDS GYPETLVNLI VLSQHLGKPP EVTNRYLSQL KDAHRSHPFI KEYQAKENDF DRLVLQYAPS 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 :
CENPM HumanDescription:
Centromere Protein-M Human Recombinant
Centromere Protein M, Interphase Centromere Complex Protein 39, Chromosome 22 Open Reading Frame 18, Proliferation Associated Nuclear Element 1, bK250D10.2, CENP-M, ICEN39, C22orf18, PANE1.
Product # :
PRO-1626Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CENPM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (1-180) and having a molecular mass of 22.0kDa.CENPM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CENPM solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
The centromere is a specialized chromatin domain, present throughout the cell cycle, that acts as a platform on which the transient assembly of the kinetochore occurs during mitosis. All active centromeres are characterized by the presence of long arrays nucleosomes in which CENPA replaces histone H3. CENPM is an additional factor required for centromere assembly.
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Synonyms
Centromere Protein M, Interphase Centromere Complex Protein 39, Chromosome 22 Open Reading Frame 18, Proliferation Associated Nuclear Element 1, bK250D10.2, CENP-M, ICEN39, C22orf18, PANE1.
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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 MGSMSVLRPL DKLPGLNTAT ILLVGTEDAL LQQLADSMLK EDCASELKVH LAKSLPLPSS VNRPRIDLIV FVVNLHSKYS LQNTEESLRH VDASFFLGKV CFLATGAGRE SHCSIHRHTV VKLAHTYQSP LLYCDLEVEG FRATMAQRLV RVLQICAGHV PGVSALNLLS LLRSSEGPSL EDL
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 :
CEA ProteinDescription:
Carcinoembryonic Antigen Human
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
Product # :
PRO-2801Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CEA produced from patient source colon carcinoma liver metastatic tissue can be used as general marker in screening and monitoring malignant disease states.
Source
Liver tissue.
Formulation
CEA protein solution contains 0.1M PBS, pH 7.4, 0.09 % NaN3 and 2 % methyl-mannoside.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Synonyms
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
-
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.
-
Applications
Blood samples from tissue donors were tested and found to be negative for HBsAg, HIV-1 and HIV-2 antibodies and HCV.
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Background
Carcinoembryonic Antigen, commonly known as CEA, is a glycoprotein that was initially identified as a tumor marker. Over the years, research into CEA has unveiled its intricate involvement in various physiological processes, not only in cancer but also in the context of normal development and inflammatory conditions. This research aims to delve into the multifaceted roles of CEA, exploring its structural intricacies, regulatory mechanisms, and its implications in health, disease, and beyond.
Structural Complexity of CEA:
CEA, belonging to the immunoglobulin superfamily, is a complex glycoprotein featuring multiple structural domains. Its diverse forms and glycosylation patterns contribute to its functional versatility. CEA is primarily expressed in fetal tissues, but its presence is often detected in adults under pathological conditions, especially in various types of cancer.
CEA in Cancer Biology:
CEA was first recognized as a biomarker for colorectal cancer, but its overexpression is not limited to this context. Elevated CEA levels have been associated with several other malignancies, including breast, lung, and pancreatic cancers. CEA’s involvement in cancer biology ranges from promoting angiogenesis and metastasis to inhibiting immune responses, making it a critical player in tumor progression and evasion.
Beyond Cancer: CEA in Development and Inflammation:
While CEA’s role in cancer is prominent, recent studies have uncovered its participation in normal physiological processes. During embryonic development, CEA is involved in cell adhesion, contributing to tissue organization and morphogenesis. Additionally, CEA expression can be induced in inflammatory conditions, suggesting its involvement in immune responses and tissue repair mechanisms.
CEA as a Diagnostic and Therapeutic Target:
The diverse expression patterns of CEA in various diseases make it a valuable diagnostic tool. CEA assays are widely used for cancer screening, monitoring disease progression, and assessing treatment efficacy. Moreover, CEA’s presence on the surface of cancer cells has made it a target for immunotherapy, enabling the development of targeted therapies aimed at specifically eradicating CEA-positive tumor cells.
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 :
ARF3 HumanDescription:
ADP-Ribosylation Factor 3 Human Recombinant
ADP-ribosylation factor 3, ARF3.
Product # :
PRO-933Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARF3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.8kDa.ARF3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARF3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
ADP-ribosylation factor 3 (ARF3) belongs to the human ARF gene family. This family encodes small guanine nucleotide-binding proteins which stimulate the ADP-ribosyltransferase activity of cholera toxin and have a role in vesicular trafficking and as activators of phospholipase D. ARF3 functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARF3 is involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. The ARF3 gene is comprised of 5 exons and 4 introns.
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Synonyms
ADP-ribosylation factor 3, ARF3.
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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 MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK K.
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 :
ARL1 HumanDescription:
ADP-Ribosylation Factor-Like 1 Human Recombinant
ARFL1.
Product # :
PRO-508Price :
Quantity :
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Shipped with Ice Packs
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Description
ARL1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.5 kDa. The ARL1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARL1 solution (0.25mg/ml) containing 20mM Tris-HCl pH-8, 2mM DTT, 100mM NaCl and 40% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
ARL1 is part of the ARL (ADP-ribosylation factor-like) family of proteins, which are structurally associated to ADP-ribosylation factors (ARFs). ARFs, described as activators of cholera toxin (CT) ADP-ribosyltransferase activity, control intracellular vesicular membrane trafficking, and stimulate a phospholipase D (PLD) isoform.
ARL1 is a weak stimulator of PLD and CT in a phospholipid dependent manner.
ARL1 is a GTP-binding protein that has low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARL1 is involved in the Golgi apparatus. -
Synonyms
ARFL1.
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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 MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI LVVFANKQDM EQAMTSSEMA NSLGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR Q.
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 :
Adiponectin (108-244) HumanDescription:
Adiponectin (108-244 a.a.) Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-073Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
Acrp30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (108-244 a.a.) and having a molecular mass of 18.1kDa.Acrp30 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Acrp30 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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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 MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN.
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Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 18.1kDa.What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein? MGSSHHHHHH SSGLVPRGSH MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN..
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
MAPRE1 HumanDescription:
Microtubule-Associated Protein, RP/EB Family, Member 1 Human Recombinant
Microtubule-associated protein RP/EB family member 1, APC-binding protein EB1, End-binding protein 1, EB1, MAPRE1, MGC117374, MGC129946.
Product # :
PRO-058Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAPRE1 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 288 amino acids (1-268 a.a.) and having a molecular mass of 32.2kDa. The MAPRE1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPRE1 solution (0.5 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
MAPRE1 (EB1) is a member of the intermediate/early gene family. MAPRE1 was first identified by its binding to the APC protein, which is often mutated in familial and sporadic, forms of colorectal cancer. MAPRE1 localizes to microtubules, especially the growing ends, in interphase cells. During mitosis, MAPRE1 is associated with the centrosomes and spindle microtubules. MAPRE1 is involved in microtubule polymerization, and spindle function by stabilizing microtubules and anchoring them at centrosomes.
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Synonyms
Microtubule-associated protein RP/EB family member 1, APC-binding protein EB1, End-binding protein 1, EB1, MAPRE1, MGC117374, MGC129946.
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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 MAVNVYSTSV TSDNLSRHDM LAWINESLQL NLTKIEQLCS GAAYCQFMDM LFPGSIALKK VKFQAKLEHE YIQNFKILQA GFKRMGVDKI IPVDKLVKGK FQDNFEFVQW FKKFFDANYD GKDYDPVAAR QGQETAVAPS LVAPALNKPK KPLTSSSAAP QRPISTQRTA AAPKAGPGVV RKNPGVGNGD DEAAELMQQV NVLKLTVEDL EKERDFYFGK LRNIELICQE NEGENDPVLQ RIVDILYATD EGFVIPDEGG PQEEQEEY.
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 :
OLR1 HumanDescription:
Oxidized Low Density Lipoprotein Receptor 1 Human Recombinant
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1.
Product # :
PRO-923Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OLR1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (58-273) and having a molecular mass of 24.7 kDa.The OLR1 is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The OLR1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
OLR1 is a type II membrane protein which belongs to the C-type lectin family and performs as a cell-surface receptor for Ox-LDL. Ox-LDL has a part in early ather-osclerosis, which includes the transformation of monocyte-derived macro-phages to foam cells in atherosclerotic lesions. In addition, OLR1 protein triggers the activation of the NF?B signal transduction pathway.
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Synonyms
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 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
MQLSQVSDLL TQEQANLTHQ KKKLEGQISA RQQAEEASQE SENELKEMIE TLARKLNEKS KEQMELHHQN LNLQETLKRV ANCSAPCPQD WIWHGENCYL FSSGSFNWEK SQEKCLSLDA KLLKINSTAD LDFIQQAISY SSFPFWMGLS RRNPSYPWLW EDGSPLMPHL FRVRGAVSQT YPSGTCAYIQ RGAVYAENCI LAAFSICQKK ANLRAQ
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 :
RCN1 HumanDescription:
Reticulocalbin 1 Human Recombinant
PIG20, RCAL, RCN.
Product # :
PRO-544Price :
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Shipped with Ice Packs
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Description
RCN1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (30-331 a.a.) and having a molecular mass of 40.4kDa (real molecular weight on SDS-PAGE will be shift up). The RCN1 is fused to 39 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
RCN1 is a calcium-binding protein which binds calcium and controls calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment. RCN1 withholds six conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.
High conservation of amino acid residues outside of these motifs, in relation to mouse reticulocalbin, is consistent with a biochemical function further to that of calcium binding. In human endothelial and prostate cancer cell lines RCN1 protein is localized to the plasma membrane. -
Synonyms
PIG20, RCAL, RCN.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEK PTVRKERVVR PDSELGERPP EDNQSFQYDH EAFLGKEDSK TFDQLTPDES
KERLGKIVDR IDNDGDGFVT TEELKTWIKR VQKRYIFDNV AKVWKDYDRD KDDKISWEEY KQATYGYYLG NPAEFHDSSD HHTFKKMLPR
DERRFKAADL NGDLTATREE FTAFLHPEEF EHMKEIVVLE TLEDIDKNGD GFVDQDEYIA DMFSHEENGP EPDWVLSERE QFNEFRDLNK
DGKLDKDEIR HWILPQDYDH AQAEARHLVY ESDKNKDEKL TKEEILENWN MFVGSQATNY GEDLTKNHDE L.
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 :
PABPN1 HumanDescription:
Poly(A) Binding Protein, Nuclear 1 Human Recombinant
Poly(A) Binding Protein Nuclear 1, Poly(A) Binding Protein 2, Polyadenylate-Binding Nuclear Protein 1, PABP-2, OPMD, PAB2, Nuclear Poly(A)-Binding Protein 1, PABII.
Product # :
PRO-1827Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PABPN1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (119-306) and having a molecular mass of 23.8 kDa. PABPN1 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The PABPN1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PABPN1 is an highly expressed nuclear protein which has high affinity to nascent poly(A) tails. PABPN1 is essential for progressive and efficient polymerization of poly(A) tails at the 3' ends of eukaryotic transcripts and regulates the length of the poly(A) tail to about 250 nt. In its steady-state, PABPN1 is restricted to the nucleus however there are different poly(A) binding proteins which can be found in the cytoplasm. PABPN1 has a GCG trinucleotide repeat at the 5' end of the coding region. Expansion of this repeat from the normal 6 copies to 8-13 copies results in autosomal dominant oculopharyngeal muscular dystrophy (OPMD) disease. Associated pseudogenes were located on chromosomes 19 and X. Additionally, there is a read-through transcription between PABPN1 gene and the adjacent upstream BCL2L2 (BCL2-like 2) gene.
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Synonyms
Poly(A) Binding Protein Nuclear 1, Poly(A) Binding Protein 2, Polyadenylate-Binding Nuclear Protein 1, PABP-2, OPMD, PAB2, Nuclear Poly(A)-Binding Protein 1, PABII.
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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 MGSLEAIKAR VREMEEEAEK LKELQNEVEK QMNMSPPPGN AGPVIMSIEE KMEADARSIY VGNVDYGATA EELEAHFHGC GSVNRVTILC DKFSGHPKGF AYIEFSDKES VRTSLALDES LFRGRQIKVI PKRTNRPGIS TTDRGFPRAR YRARTTNYNS SRSRFYSGFN SRPRGRVYRG RARATSWYSP Y
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
Description:
Leptin Super Antagonist Human Recombinant
Product # :
CYT-1238Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Super Leptin Antagonist Human Recombinant is a single polypeptide chain containing 146 amino acids. Super Human Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super human leptin antagonist that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/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
ProSpec’s super human leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super human leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super human leptin antagonist can be stored at 4C 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 Super Leptin Antagonist in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Background
Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function. Leptin is a~16 kDa protein which is encoded by the obese gene. leptin is expressed predominantly by adipocytes, which fits with 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.
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 :
SNRPC Human, Sf9Description:
Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant, Sf9
U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.
Product # :
PRO-1510Price :
Quantity :
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Shipped with Ice Packs
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Description
SNRPC Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 25,000 Dalton. SNRPC is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
SNRPC is supplied in 20mM HEPES buffer pH-7.5, 0.01mM EDTA and 0.02% SDS.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SNRPC is a member of the U1 small nuclear ribonucleoprotein C family. The SNRPC protein component of the U1 small nuclear ribonucleoprotein (snRNP) particle required for the formation of the spliceosome. SNRPC participates in the processing of nuclear precursor messenger RNA splicing. snRNP particles are tackled by autoantibodies frequently produced by patients with connective tissue diseases.
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Synonyms
U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.
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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. Avoid multiple freeze-thaw cycles.
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 :
ExenatideDescription:
Exenatide
Exendin-4.
Product # :
HOR-246Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Exenatide is a single, non-glycosylated, peptide containing 39 amino acids and having a molecular mass of 4186.6 Dalton. Exenatide has the empirical formula C184H282N50O60S.
Formulation
The Exenatide peptide was lyophilized from a concentrated solution with no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Exenatide Derived from the saliva of the gila monster, is a 39 amino acid peptide that mimics the GLP-1 incretin, an insulin secretagogue with glucoregulatory effects. Typical responses to exenatide include improvements in the initial rapid release of endogenous insulin, suppression of glucagon release by the pancreas, regulation of gastric empyting, and reduced appetite - all of which function to lower blood glucose. Exenatide is self-regulating in that it lowers blood sugar when levels are elevated but does not continue to lower blood sugar when levels return to normal, unlike with sulfonylureas or insulins.
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Synonyms
Exendin-4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Exenatide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Exenatide 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 Exenatide 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
H-His-Gly-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Leu-Ser-Lys-Gln-Met-Glu-Glu-Glu-Ala-Val-Arg-Leu-Phe-Ile-Glu-Trp-Leu-Lys-Asn-Gly-Gly-Pro-Ser-Ser-Gly-Ala-Pro-Pro-Pro-Ser-NH2.
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 :
IpamorelinDescription:
Ipamorelin
Ipamorelin
Product # :
HOR-024Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ipamorelin Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 711.85 Dalton and a Molecular formula of C38H49N9O5.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Introduction
Ipamorelin is a peptide selective agonist of the ghrelin/growth hormone secretagogue receptor and a growth hormone secretagogue. Ipamorelin is a pentapeptide that was derived from GHRP1. Ipamorelin significantly increases plasma growth hormone levels in both animals and humans. Like pralmorelin and GHRP-6, ipamorelin does not affect prolactin, FSH, LH or TSH levels. However, unlike GHRP2 and GHRP6, but as growth hormone-releasing hormone (GHRH), ipamorelin does not stimulate the secretion of adrenocorticotropic hormone (ACTH) or cortisol, and is highly selective for inducing the secretion only of GH.
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Synonyms
Ipamorelin
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Ipamorelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Ipamorelin 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 Ipamorelin 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
Aib-His-D-2-Nal-D-Phe-Lys-NH2.
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 :
PDLIM1 HumanDescription:
PDZ And LIM Domain 1 Human Recombinant
PDZ And LIM Domain Protein 1, Carboxyl Terminal LIM Domain Protein 1, Epididymis Secretory Protein Li 112m, C-Terminal LIM Domain Protein 1, LIM Domain Protein CLP-36, hCLIM1, HEL-S-112, CLP-36, Elfin.
Product # :
PRO-1848Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PDLIM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 354 amino acids (1-329) and having a molecular mass of 38.7 kDa. PDLIM1 is fused to a 25 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The PDLIM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl, 1mM DTT, 2mM EDTA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
PDLIM1, a cytoplasmic protein linked to the cytoskeleton, belongs to the enigma protein family. PDLIM1 holds two protein interacting domains - PDZ domain at the amino terminal end and one to three LIM domains at the carboxyl terminal. PDLIM1 enables bringing other LIM interacting proteins to the cytoskeleton. Pseudogenes related to PDLIM1 are situated on chromosomes 3, 14 and 17.
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Synonyms
PDZ And LIM Domain Protein 1, Carboxyl Terminal LIM Domain Protein 1, Epididymis Secretory Protein Li 112m, C-Terminal LIM Domain Protein 1, LIM Domain Protein CLP-36, hCLIM1, HEL-S-112, CLP-36, Elfin.
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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 MGSEFMTTQQ IDLQGPGPWG FRLVGGKDFE QPLAISRVTP GSKAALANLC IGDVITAIDG ENTSNMTHLE AQNRIKGCTD NLTLTVARSE HKVWSPLVTE EGKRHPYKMN LASEPQEVLH IGSAHNRSAM PFTASPASST TARVITNQYN NPAGLYSSEN ISNFNNALES KTAASGVEAN SRPLDHAQPP SSLVIDKESE VYKMLQEKQE LNEPPKQSTS FLVLQEILES EEKGDPNKPS GFRSVKAPVT KVAASIGNAQ KLPMCDKCGT GIVGVFVKLR DRHRHPECYV CTDCGTNLKQ KGHFFVEDQI YCEKHARERV TPPEGYEVVT VFPK
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 :
CFB Human, NativeDescription:
Complement Factor B Human
CFB, C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, BF, BFD, AHUS4, ARMD14, CFAB, CFBD, FB, FBI12, GBG, H2-Bf.
Product # :
PRO-2698Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Human Complement Factor B produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 93kDa.
Source
Human Plasma.
Formulation
CFB protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.
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Synonyms
CFB, C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, BF, BFD, AHUS4, ARMD14, CFAB, CFBD, FB, FBI12, GBG, H2-Bf.
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Physical Appearance
Sterile filtered solution.
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Stability
CFB Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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.