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1000 results found for “peptide hormones”
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Name :
Leptin Ovine, MTSDescription:
Leptin Ovine Recombinant, MTS tag
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-531Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Ovine MTS tagged Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.5 kDa.The Leptin is purified by proprietary chromatographic techniques. The membrane translocating sequence Tag is composed of 10 amino acids Val-Leu-Leu-Pro-Val-Leu-Leu-Ala-Ala-Pro located at the N-terminus.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.Citations
More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Ovine MTS tagged although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 0.02% NaHCO3 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-Leu-Leu-Pro.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 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 :
PREP HumanDescription:
Prolyl Endopeptidase Human Recombinant
Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.
Product # :
ENZ-828Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PREP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 733 amino acids (1-710 a.a) and having a molecular mass of 83.1kDa. PREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PREP protein solution (0.25mg/ml) containing PBS buffer (pH 7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Prolyl Endopeptidase , also known as PREP is a cytosolic prolyl endopeptidase which cleaves peptide bonds on the C-terminal side of prolyl residues within peptides which are up to about 30 a.a long. In addition, Prolyl endopeptidases have been shown to be implicated in the maturation and degradation of peptide hormones and neuropeptides.
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Synonyms
Prolyl Endopeptidase, Post-Proline Cleaving Enzyme, EC 3.4.21.26, PEP, PE, DJ355L5.1 (Prolyl Endopeptidase), Prolyl Oligopeptidase, Prolyl endopeptidase.
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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 MGSMLSLQYP DVYRDETAVQ DYHGHKICDP YAWLEDPDSE QTKAFVEAQN KITVPFLEQC PIRGLYKERM TELYDYPKYS CHFKKGKRYF YFYNTGLQNQ RVLYVQDSLE GEARVFLDPN ILSDDGTVAL RGYAFSEDGE YFAYGLSASG SDWVTIKFMK VDGAKELPDV LERVKFSCMA WTHDGKGMFY NSYPQQDGKS DGTETSTNLH QKLYYHVLGT DQSEDILCAE FPDEPKWMGG AELSDDGRYV LLSIREGCDP VNRLWYCDLQ QESSGIAGIL KWVKLIDNFE GEYDYVTNEG TVFTFKTNRQ SPNYRVINID FRDPEESKWK VLVPEHEKDV LEWIACVRSN FLVLCYLHDV KNILQLHDLT TGALLKTFPL DVGSIVGYSG QKKDTEIFYQ FTSFLSPGII YHCDLTKEEL EPRVFREVTV KGIDASDYQT VQIFYPSKDG TKIPMFIVHK KGIKLDGSHP AFLYGYGGFN ISITPNYSVS RLIFVRHMGG ILAVANIRGG GEYGETWHKG GILANKQNCF DDFQCAAEYL IKEGYTSPKR LTINGGSNGG LLVAACANQR PDLFGCVIAQ VGVMDMLKFH KYTIGHAWTT DYGCSDSKQH FEWLVKYSPL HNVKLPEADD IQYPSMLLLT ADHDDRVVPL HSLKFIATLQ YIVGRSRKQS NPLLIHVDTK AGHGAGKPTA KVIEEVSDMF AFIARCLNVD WIP.
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 :
AKR1C4 Human, HisDescription:
Aldo-Keto Reductase Family 1 Member C4 Human Recombinant, His Tag
Aldo-keto reductase family 1 member C4 (chlordecone reductase 3-alpha hydroxysteroid dehydrogenase type I dihydrodiol dehydrogenase 4), 3-alpha-hydroxysteroid dehydrogenase type I, MGC22581, HAKRA, 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase 4, CDR, DD4, CHDR, 3-alpha-HSD1, C11.
Product # :
ENZ-145Price :
Quantity :
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Shipped with Ice Packs
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Description
AKR1C4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-323) and having a molecular mass of 39.2 kDa.The AKR1C4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AKR1C4 protein 1mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 700 pmol/min/ug, and is defined as the amount of enzyme that catalyze the oxidation of 1.0 pmole 1-Acenaphthenol in the presence of NADP per minute at pH 8.8 at 25°C.Citations
More Info
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Introduction
AKR1C4 is a member of the aldo/keto reductase superfamily that has over 40 known enzymes and proteins. AKR1C4 enables the conversion of aldehydes and ketones to their corresponding alcohols by using NADH and/or NADPH as cofactors. AKR1C4 takes part in the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in liver.
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Synonyms
Aldo-keto reductase family 1 member C4 (chlordecone reductase 3-alpha hydroxysteroid dehydrogenase type I dihydrodiol dehydrogenase 4), 3-alpha-hydroxysteroid dehydrogenase type I, MGC22581, HAKRA, 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase 4, CDR, DD4, CHDR, 3-alpha-HSD1, C11.
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Physical Appearance
AKR1C4 is supplied as a sterile filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDPKYQRVEL NDGHFMPVLG FGTYAPPEVP RNRAVEVTKL AIEAGFRHID SAYLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCTFF QPQMVQPALE SSLKKLQLDY VDLYLLHFPM ALKPGETPLP KDENGKVIFD TVDLSATWEV MEKCKDAGLA
KSIGVSNFNC RQLEMILNKP GLKYKPVCNQ VECHPYLNQS KLLDFCKSKD IVLVAHSALG TQRHKLWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIREN IQVFEFQLTS EDMKVLDGLN RNYRYVVMDF LMDHPDYPFS DEY.
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 :
STC 2 HumanDescription:
Stanniocalcin-2 Human Recombinant
Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.
Product # :
HOR-296Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stanniocalcin-2 Human Recombinant produced in HEK 293 cell line is a single, glycosylated, polypeptide chain containing 289 amino acids and having a total molecular mass of 31.9kDa (calculated). The Stanniocalcin contains four extra residues which were used as a spacer and 8 residues form the C-Terminal Flag- tag.Stanniocalcin is purified by proprietary chromatographic techniques.The amino acid sequence of the recombinant human Stanniocalcin-2 is 100% homologous to the amino acid sequence AA 25-302 of the human mature Human Stanniocalcin-2.
Source
HEK 293 cell line (Human embryonic kidney).
Formulation
Filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris buffer, 20mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
STC2 is a homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The encoded protein has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. Its C-terminus contains a cluster of histidine residues which may interact with metal ions. The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Constitutive over expression of human stanniocalcin 2 in mice resulted in pre- and postnatal growth restriction, reduced bone and skeletal muscle growth, and organomegaly. Expression of this gene is induced by estrogen and altered in some breast cancers.
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Synonyms
Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized STC-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Stanniocalcin 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
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
TDATNPPEGP QDRSSQQKGR LSLQNTAEIQ HCLVNAGDVG CGVFECFENN SCEIRGLHGI CMTFLHNAGKFDAQGKSFIK DALKCKAHAL RHRFGCISRK CPAIREMVSQ LQRECYLKHD LCAAAQENTR VIVEMIHFKDLLLHEPYVDL VNLLLTCGEE VKEAITHSVQ VQCEQNWGSL CSILSFCTSA IQKPPTAPPE RQPQVDRTKLSRAHHGEAGH HLPEPSSRET GRGAKGERGS KSHPNAHARG RVGGLGAQGP SGSSEWEDEQ SEYSDIRRAAADYKDDDDK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin HorseDescription:
Leptin Horse Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-504Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Horse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.Citations
More Info
-
Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.1 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Horse as a Reference Standard.
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 :
Super Leptin qA OvineDescription:
Super Leptin Antagonist Ovine Recombinant
Product # :
CYT-1245Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Super Leptin Antagonist Ovine Recombinant is a single polypeptide chain containing 146 amino acids, an additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa. Super Ovine Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A 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 Ovine leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Ovine leptin antagonist also inhibits various leptin effects in several in vitro bioassays.
Citations
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 Ovine leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super Ovine 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 water or sterile 0.4% NaHCO3 adjusted to pH 10, 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-Arg.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviours which save energy. When leptin levels are high, the brain interprets 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 quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin Human, MutantDescription:
Leptin Mutant D23L Human Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Leptin Mutant D23L is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. Leptin Mutant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
Leptin Mutant was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Human Leptin Mutant D23L is fully biologically active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.
Citations
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Leptin Mutant D23L although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 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 Mutant 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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Amino Acid Sequence
The sequence of the first five N-terminal amino acids of recombinant human leptin was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Background
Leptin’s main part is to regulate long-term energy balance. Leptin is a hormone which mainly produced by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings 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.
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 :
HN1 HumanDescription:
Hematological And Neurological Expressed 1 Human Recombinant
ARM2, HN1A, Hematological and neurological expressed 1 protein, Androgen-regulated protein 2, HN1.
Product # :
PRO-1434Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-154) and having a molecular mass of 18.1kDa. HN1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The HN1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hematological and neurological expressed 1 protein (HN1) is a small protein which is extremely preserved among species. HN1 expression is upregulated in regenerating neural tissues, including the axotomized adult rodent facial motor nerve and dedifferentiating retinal pigment epithelial cells of the Japanese newt. HN1 is also expressed in several tissues during embryonic development as well as in regions of the adult brain which display high plasticity.
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Synonyms
ARM2, HN1A, Hematological and neurological expressed 1 protein, Androgen-regulated protein 2, HN1.
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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 MTTTTTFKGV DPNSRNSSRV LRPPGGGSNF SLGFDEPTEQ PVRKNKMASN IFGTPEENQA SWAKSAGAKS SGGREDLESS GLQRRNSSEA SSGDFLDLKG EGDIHENVDT DLPGSLGQSE EKPVPAAPVP SPVAPAPVPS RRNPPGGKSS LVLG.
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 :
GRPEL1 HumanDescription:
GrpE-Like 1 Human Recombinant
HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.
Product # :
PRO-263Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GRPEL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (28-217a.a.) and having a molecular mass of 23.6kDa.GRPEL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GRPEL1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GRPEL1 is a vital component of the PAM complex, a complex necessary for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. GRPEL1 protein controls the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.
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Synonyms
HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MCTATKQKNS GQNLEEDMGQ SEQKADPPAT EKTLLEEKVK LEEQLKETVE KYKRALADTE NLRQRSQKLV EEAKLYGIQA FCKDLLEVAD VLEKATQCVP KEEIKDDNPH LKNLYEGLVM TEVQIQKVFT KHGLLKLNPV GAKFDPYEHE ALFHTPVEGK EPGTVALVSK VGYKLHGRTL RPALVGVVKE 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.
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Name :
CXCL8 Porcine (1-72)Description:
Interleukin-8 (1-72 a.a) Porcine Recombinant (CXCL8)
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP, Alveolar macrophage chemotactic factor I.
Product # :
CHM-340Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-8 Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 9.1kDa. The IL8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
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.Biological Activity
The biological activity was determined by a chemotaxis bioassay using human peripheral blood neutrophils is in a concentration range of 20-200 ng/ml.Citations
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP, Alveolar macrophage chemotactic factor I.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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 Interleukin 8 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
ARVSAELRCQ CINTHSTPFH PKFIKELRVI ESGPHCENSE IIVKLVNGKE VCLDPKEKWV QKVVQIFLKR TEKQQQQQ.
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Background
What is the molecular weight/Mw of CXCL8 PORCINE (1-72) Protein?
CXCL8 PORCINE (1-72) Protein has a total Mw of 9.1kDa.
What is the source or expression system of CXCL8 PORCINE (1-72) Protein?
Escherichia Coli.
What is the Purity of CXCL8 PORCINE (1-72) Protein?
CXCL8 PORCINE (1-72) Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 PORCINE (1-72) Protein?
The biological activity was determined by a chemotaxis bioassay using human peripheral blood neutrophils is in a concentration range of 20-200 ng/ml.
What is the amino acid sequence of CXCL8 PORCINE (1-72) Protein?
ARVSAELRCQ CINTHSTPFH PKFIKELRVI ESGPHCENSE IIVKLVNGKE VCLDPKEKWV QKVVQIFLKR TEKQQQQQ.
What applications can CXCL8 PORCINE (1-72) Protein be used in?
CXCL8 PORCINE (1-72) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 PORCINE (1-72) Protein?
The endotoxin level is minimal, CXCL8 PORCINE (1-72) Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL8 PORCINE (1-72) 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 CXCL8 PORCINE (1-72)?
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.
- View Data Sheet
Name :
NCALD HumanDescription:
Neurocalcin Delta Recombinant Human
Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.
Product # :
PRO-093Price :
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Shipped with Ice Packs
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Description
NCALD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-193.a.a) and having a molecular mass of 24.4kDa. NCALD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NCALD protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NCALD belongs to the neuronal calcium sensor (NCS) family. NCALD is cytosolic at inactive calcium levels; but, high intracellular calcium levels induce a conformational transformation which exposes the myristoyl group, causing protein association with membranes and partial co-localization with the perinuclear trans-golgi network. NCALD protein is a regulator of signal transduction by G protein-coupled receptor.
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Synonyms
Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGKQNSKLRP EVMQDLLEST DFTEHEIQEW YKGFLRDCPS GHLSMEEFKK IYGNFFPYGD ASKFAEHVFR TFDANGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISKAE MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNR DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA GQF.
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 :
EBV p18, GSTDescription:
Epstein - Barr virus (HHV-4) p18 Recombinant, GST Tag
Product # :
EBV-277Price :
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Description
The E.Coli derived recombinant protein contains the HHV-4 p18 regions, having a molecular mass of 35.4kDa which includes GST tag at N-terminus.
Source
Escherichia Coli.
Formulation
3.8mg/ml in 50mM Tris-HCl, pH 8.0.
Purity
Protein is >90% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
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Introduction
The Epstein-Barr virus (EBV), also called Human herpes virus 4 (HHV-4), is a virus of the herpes family (which includes Herpes simplex virus and Cytomegalovirus. On infecting the B-lymphocyte, the linear virus genome circularizes and the virus subsequently persists within the cell as an episome. The virus can execute several distinct programs of gene expression which can be broadly categorized as being lytic cycle or latent cycle. The lytic cycle or productive infection results in staged expression of a host of viral proteins with the ultimate objective of producing infectious virions. Formally, this phase of infection does not inevitably lead to lysis of the host cell as EBV virions are produced by budding from the infected cell. The latent cycle (lysogenic) programs are those that do not result in production of virions. A very limited, distinct set of viral proteins are produced during latent cycle infection. These include Epstein-Barr nuclear antigen (EBNA)-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA-leader protein (EBNA-LP) and latent membrane proteins (LMP)-1, LMP-2A and LMP-2B and the Epstein-Barr encoded RNAs (EBERs).
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Stability
EBV p18, GST although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
ASAGTGALAS SAPSTAVAQS ATPSVSSSIS SLRAATSGAT AAASAAAAVD TGSGGGGQPH DTAPRGARKK Q.
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Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Description:
Leptin Super Antagonist Human Recombinant
Product # :
CYT-1238Price :
Quantity :
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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.
Citations
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 :
PEPD HumanDescription:
Peptidase D Human Recombinant
Xaa-Pro dipeptidase, X-Pro dipeptidase, Imidodipeptidase, Peptidase D, Proline dipeptidase, Prolidase, PRD, PEPD, Xaa-Pro dipeptidase isoform 1, PROLIDASE.
Product # :
ENZ-856Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PEPD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-493a.a.) and having a molecular mass of 56.9kDa.PEPD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
PEPD protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Peptidase D, also known as PEPD, Is a part of the peptidase family. PEPD is involved in collagen metabolism due to the high level of iminoacids in collagen. PEPD recycles proline, and sets the pace for the production of collagen. PEPD is also parts dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position.
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Synonyms
Xaa-Pro dipeptidase, X-Pro dipeptidase, Imidodipeptidase, Peptidase D, Proline dipeptidase, Prolidase, PRD, PEPD, Xaa-Pro dipeptidase isoform 1, PROLIDASE.
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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 MGSMAAATGP SFWLGNETLK VPLALFALNR QRLCERLRKN PAVQAGSIVV LQGGEETQRY CTDTGVLFRQ ESFFHWAFGV TEPGCYGVID VDTGKSTLFV PRLPASHATW MGKIHSKEHF KEKYAVDDVQ YVDEIASVLT SQKPSVLLTL RGVNTDSGSVCREASFDGIS KFEVNNTILH PEIVECRVFK TDMELEVLRY TNKISSEAHR EVMKAVKVGM KEYELESLFE HYCYSRGGMR HSSYTCICGS GENSAVLHYG HAGAPNDRTI QNGDMCLFDM GGEYYCFASD ITCSFPANGK FTADQKAVYE AVLRSSRAVM GAMKPGVWWP DMHRLADRIH LEELAHMGIL SGSVDAMVQA HLGAVFMPHG LGHFLGIDVH DVGGYPEGVE RIDEPGLRSL RTARHLQPGM VLTVEPGIYF IDHLLDEALA DPARASFLNR EVLQRFRGFG GVRIEEDVVV TDSGIELLTC VPRTVEEIEA CMAGCDKAFT PFSGPK.
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 :
MME HumanDescription:
Membrane Metalloendopeptidase Human Recombinant
Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.
Product # :
ENZ-1053Price :
Quantity :
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Shipped with Ice Packs
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Description
MME Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 708 amino acids (52-750 a.a.) and having a molecular mass of 80.9kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).MME is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
MME protein solution (1mg/ml) 20 mM Tris-HCl buffer (pH 8.0) containing 100mM NaCl, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Membrane Metalloendopeptidase, also known as MME is a zinc metallopeptidase which is expressed at the cell surface of various cells. MME degrades the amyloid beta peptide whose abnormal misfolding as well as aggregation in neural tissue has been implicated as the cause for Alzheimer's disease. MME is expressed in an extended range of tissues and is especially plentiful in the kidney. MME is also a common acute lymphocytic leukemia antigen which is a significant cell surface marker in the diagnosis of human acute lymphocytic leukemia (ALL). MME is used in hematological diagnosis because it is expressed by early B, pro-B and pre-B lymphocytes, and also by lymph node germinal centers.
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Synonyms
Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.
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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
ADPYDDGICK SSDCIKSAAR LIQNMDATTE PCTDFFKYAC GGWLKRNVIP ETSSRYGNFD ILRDELEVVL KDVLQEPKTE DIVAVQKAKA LYRSCINESA IDSRGGEPLL KLLPDIYGWP VATENWEQKY GASWTAEKAI AQLNSKYGKK VLINLFVGTD DKNSVNHVIH IDQPRLGLPS RDYYECTGIY KEACTAYVDF MISVARLIRQ EERLPIDENQ LALEMNKVME LEKEIANATA KPEDRNDPML LYNKMTLAQI QNNFSLEING KPFSWLNFTN EIMSTVNISI TNEEDVVVYA PEYLTKLKPI LTKYSARDLQ NLMSWRFIMD LVSSLSRTYK ESRNAFRKAL YGTTSETATW
RRCANYVNGN MENAVGRLYV EAAFAGESKH VVEDLIAQIR EVFIQTLDDL TWMDAETKKR AEEKALAIKE RIGYPDDIVS NDNKLNNEYL ELNYKEDEYF ENIIQNLKFS QSKQLKKLRE KVDKDEWISG AAVVNAFYSS GRNQIVFPAG ILQPPFFSAQ QSNSLNYGGI GMVIGHEITH GFDDNGRNFN KDGDLVDWWT QQSASNFKEQ SQCMVYQYGN FSWDLAGGQH LNGINTLGEN IADNGGLGQA YRAYQNYIKK NGEEKLLPGL DLNHKQLFFL NFAQVWCGTY RPEYAVNSIK TDVHSPGNFR IIGTLQNSAE FSEAFHCRKN SYMNPEKKCR VWHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin HumanDescription:
Human Leptin
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
Product # :
CYT-683Price :
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Shipping Method :
Shipped at Room temp
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Description
Leptin Human produced syntheticaly contains 35 amino acids (22-56 a.a.) having a molecular mass of 3950.6 Dalton.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 95.0% as determined by RP-HPLC.
Citations
More Info
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Introduction
A 16kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature, should be stored desiccated below -20°C. Reconstituted Leptin is best stored refrigerated at 4°C.
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Solubility
The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.
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Amino Acid Sequence
Val-Pro-Ile-Gln-Lys-Val-Gln-Asp-Asp-Thr-Lys-Thr-Leu-Ile-Lys-Thr-Ile-Val-Thr-Arg-Ile-Asn-Asp-Ile-Ser-His-Thr-Gln-Ser-Val-Ser-Ser-Lys-Gln-Lys.
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 :
Thyroglobulin HumanDescription:
Thyroglobulin Human Recombinant
Thyroglobulin, TGN, AITD3, TG.
Product # :
PRO-2803Price :
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Shipping Method :
Shipped at Room temp
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Description
Thyroglobulin Human produced in a mammalian cell line is a single, non-glycosylated polypeptide chain (1-2768 a.a.) and having a molecular mass of 304640 Dalton. Thyroglobulin Human is fused with GlyAlaProGly4SerHis10-tag at C-terminal and purified by proprietary chromatographic techniques.
Source
Mammalian cell line.
Formulation
Thyroglobulin was lyophilized from PBS, pH 7.4 and 5.4 % sucrose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
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Synonyms
Thyroglobulin, TGN, AITD3, TG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thyroglobulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thyroglobulin 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 Thyroglobulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Thyroglobulin, a glycoprotein primarily produced in the thyroid gland, stands at the center of thyroid hormone synthesis. Comprising a series of tyrosine residues, thyroglobulin serves as the scaffold upon which thyroid hormones are assembled. Beyond its pivotal role in thyroid physiology, thyroglobulin has garnered significant attention in the realm of thyroid disease diagnostics, offering valuable insights into thyroid function and disorders. This research delves into the intricacies of thyroglobulin human recombinant protein, exploring its biochemical properties, physiological significance, and its crucial applications in both clinical and research settings.
Structural Complexity of Thyroglobulin:
Thyroglobulin is a large, dimeric protein boasting an intricate structure composed of multiple domains. Within its structure lie tyrosine residues crucial for iodine incorporation, a process fundamental for thyroid hormone synthesis. Its size and complexity reflect the sophistication of thyroid hormone production, as thyroglobulin acts as a reservoir for thyroid hormones within the thyroid follicles.
Physiological Significance in Thyroid Function:
Thyroglobulin plays a central role in the synthesis of triiodothyronine (T3) and thyroxine (T4), the thyroid hormones essential for regulating metabolism and overall body homeostasis. During thyroid hormone synthesis, thyroglobulin is secreted into the follicular lumen, where it undergoes iodination and subsequent proteolysis, releasing T3 and T4. This process highlights the indispensable nature of thyroglobulin in thyroid hormone production, making it a key biomolecule in thyroid physiology.
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 :
PDI HumanDescription:
Protein Disulfide Isomerase Human Recombinant
Protein Disulfide Isomerase, PDI, EC 5.3.4.1, Prolyl 4-hydroxylase subunit beta, Cellular thyroid hormone-binding protein, p55, P4HB, ERBA2L, PDIA1, PO4DB, DSI, GIT, PHDB, PO4HB, PROHB, P4Hbeta.
Product # :
ENZ-262Price :
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Shipping Method :
Shipped at Room temp
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Description
PDI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing a total of 502 amino acids and having a molecular mass of 56.6kDa. The PDI is fused to a 12 amino acid His tag at N-terminal and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PDI protein (1mg/ml)solution was lyophilized from PBS pH-7.
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
Protein disulfide isomerases (PDIs) constitute a family of structurally related enzymes which catalyze disulfide bonds formation, reduction, or isomerization of newly synthesized proteins in the lumen of the endoplasmic reticulum (ER). They act also as chaperones, and are, therefore, part of a quality-control system for the correct folding of the proteins in the same subcellular compartment. PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro.
Recombinant Human Protein Disulfide Isomerase is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. Recombinant PDI has been found to have moderate effects (25-fold) on the rate of oxidative folding of proteins in vitro. -
Synonyms
Protein Disulfide Isomerase, PDI, EC 5.3.4.1, Prolyl 4-hydroxylase subunit beta, Cellular thyroid hormone-binding protein, p55, P4HB, ERBA2L, PDIA1, PO4DB, DSI, GIT, PHDB, PO4HB, PROHB, P4Hbeta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Protein Disulfide Isomerase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human PDI 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 avoid freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized PDI 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
MRGSGSHHHHHHAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKA
AGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVN
WLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNS
DVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIK
THILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITL
EEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEK
KNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFP
ASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
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Reductase Activity
0.001 650nm/ min-2. By measuring the turbidity increase at 650 nm due to insulin reduction (Holmgren, A. (1979) J. Biol. Chem. 254, 9627–9632). The activity is expressed as the ratio of the slope of a linear part of the turbidity curve to the lag time (Mart
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Isomerase Activity
0.5 µmol active RNase A min-1 µmol PDI-1. According to the re-activation of reduced and denatured RNase A (Lyles, M. M. and Gilbert, H. F. (1991) Biochemistry 30, 613-619).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Omentin 298 a.a. HumanDescription:
Omentin 298 a.a. Human Recombinant
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Product # :
CYT-061Price :
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Description
Omentin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (17-313) and having a molecular mass of 33.2 kDa.The Omentin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Omentin protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.4M Urea and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
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Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
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Physical Appearance
Sterile Filtered 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
MWSTDEANTY FKEWTCSSSP SLPRSCKEIK DECPSAFDGL YFLRTENGVI YQTFCDMTSG GGGWTLVASV HENDMRGKCT VGDRWSSQQG SKAVYPEGDG NWANYNTFGS AEAATSDDYK NPGYYDIQAK DLGIWHVPNK SPMQHWRNSS LLRYRTDTGF LQTLGHNLFG IYQKYPVKYG EGKCWTDNGP VIPVVYDFGD AQKTASYYSP YGQREFTAGF VQFRVFNNER AANALCAGMR VTGCNTEHHC IGGGGYFPEA SPQQCGDFSG FDWSGYGTHV GYSSSREITE AAVLLFYR
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 :
GH Zebrafish MutantDescription:
Growth Hormone Mutant Zebrafish Recombinant
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
Product # :
CYT-709Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Somatotropin Zebrafish Mutant G113R Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.18 kDa. The Zebrafish Mutant G113R Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.5% NaHCO3 pH-8.
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
GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Growth-Hormone although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 Zebrafish Mutant G113R in 0.4% NaHCO3 or water adjusted to pH-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.
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Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Gln-Arg-Leu-Phe-Asn.
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 HumanDescription:
Leptin Antagonist Quadruple Mutant Human Recombinant
Product # :
CYT-353Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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Description
Leptin Quadruple Mutant Human Recombinant is a single polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a Mw of 16 kDa, Human Leptin was mutated, resulting in L39A/D40A/F41A/I42A.Leptin Antagonist Quadruple Mutant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin Quadruple Antagonist Mutant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Quadruple Mutant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant 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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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.89 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 :
Leptin tA OvineDescription:
Leptin Antagonist Triple Mutant Ovine Recombinant
Product # :
CYT-356Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin-Antagonist Triple Mutant Ovine Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of mouse leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Lep-tA mutant mg/ml and up to 2 mM and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, 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-Arg.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 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 :
MME Human, ActiveDescription:
Membrane Metalloendopeptidase Human Recombinant, Active
Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.
Product # :
ENZ-1116Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
MME Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 708 amino acids (52-750 aa) and having a molecular mass of 80.9kDa.MME is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The MME solution (1mg/ml) contains 10% Glycerol, 20 mM Tris-HCl buffer (pH 8.0), 0.1mM PMSF and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity > 5,000 pmol/min/ug. One unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute, at pH 8.8 at 25C˚.
Citations
More Info
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Introduction
Neutral endopeptidase (NEP) is an enzyme located in the cell membrane (bound to it) that is able to dissolve biologically active proteins and is expressed on the surface of lymphoid progenitors, human podocytes, syncytiotrophoblastic cells, and many other epithelial cells including polymorphonuclear leukocytes.
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Synonyms
Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.
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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
ADPYDDGICK SSDCIKSAAR LIQNMDATTE PCTDFFKYAC GGWLKRNVIP ETSSRYGNFD ILRDELEVVL KDVLQEPKTE DIVAVQKAKA LYRSCINESA IDSRGGEPLL KLLPDIYGWP VATENWEQKY GASWTAEKAI AQLNSKYGKK VLINLFVGTD DKNSVNHVIH IDQPRLGLPS RDYYECTGIY KEACTAYVDF MISVARLIRQ EERLPIDENQ LALEMNKVME LEKEIANATA KPEDRNDPML LYNKMTLAQI QNNFSLEING KPFSWLNFTN EIMSTVNISIT NEEDVVVYAP EYLTKLKPI LTKYSARDLQ NLMSWRFIMD LVSSLSRTYK ESRNAFRKAL YGTTSETATW RRCANYVNGN MENAVGRLYV EAAFAGESKH VVEDLIAQIR EVFIQTLDDL TWMDAETKKR AEEKALAIKE RIGYPDDIVS NDNKLNNEYL ELNYKEDEYF ENIIQNLKFS QSKQLKKLRE KVDKDEWISG AAVVNAFYSS GRNQIVFPAG ILQPPFFSAQ QSNSLNYGGI GMVIGHEITH GFDDNGRNFN KDGDLVDWWT QQSASNFKEQ SQCMVYQYGN FSWDLAGGQH LNGINTLGEN IADNGGLGQA YRAYQNYIKK NGEEKLLPGL DLNHKQLFFL NFAQVWCGTY RPEYAVNSIK TDVHSPGNFR IIGTLQNSAE FSEAFHCRKN SYMNPEKKCR VWHHHHHH
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 :
AKR1D1 Human, HisDescription:
Aldo-Keto Reductase Family 1 Member D1 Human Recombinant, His Tag
3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-keto reductase family 1 member D1, Delta(4)-3-ketosteroid 5-beta-reductase, Delta(4)-3-oxosteroid 5-beta-reductase, KR1D1, SRD5B1, CBAS2, 3o5bred.
Product # :
ENZ-098Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AKR1D1 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 346 amino acids (1-326 a.a.) and having a molecular mass of 39.5kDa. The AKR1D1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1D1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Aldo-keto reductase family 1 member D1 (AKR1D1) belongs to the AKR superfamily. The AKR family proteins are soluble NADPH oxidoreductases, which have vital roles in the metabolism of drugs, carcinogens and reactive aldehydes. AKR1D1 is also responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones that carry a delta (4)-3-1 structure. AKR1D1 is highly expressed in the liver, colon and testis. Deficiency of the AKR1D1 enzyme may contribute to hepatic dysfunction.
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Synonyms
3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-keto reductase family 1 member D1, Delta(4)-3-ketosteroid 5-beta-reductase, Delta(4)-3-oxosteroid 5-beta-reductase, KR1D1, SRD5B1, CBAS2, 3o5bred.
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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 MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR HIDGAYIYQN EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP TLERTLRVLQ LDYVDLYIIE VPMAFKPGDE IYPRDENGKW LYHKSNLCAT WEAMEACKDA GLVKSLGVSN FNRRQLELIL NKPGLKHKPV SNQVECHPYF TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK DALLNSLGKR YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE ALNKNVRFVE LLMWRDHPEY PFHDEY.
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.