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1000 results found for “Serglycin”
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Name :
TNC RabbitDescription:
Skeletal Muscle Troponin-C Rabbit
Troponin C skeletal muscle, TNNC2, TNC.
Product # :
PRO-323Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Rabbit Skeletal Muscle Troponin-C is a single, glycosylated, polypeptide chain having a molecular mass of 18kDa. Troponin-C is one of three subunits that form the Troponin complex of striated muscle thin filaments. Skeletal muscle Troponin-C is purified using a combination of ion-exchange and affinity chromatography steps.
Source
Rabbit Skeletal Muscle.
Formulation
The Troponin C Rabbit protein solution contains 150mM sodium chloride, 10mM sodium phosphate and 0.05% sodium azide, pH-7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Troponin C skeletal muscle, TNNC2, TNC.
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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. 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 :
Shiga Like Toxin 1B AntibodyDescription:
Mouse Anti Shiga Like Toxin 1B
Product # :
ANT-660Price :
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Description
Shiga like toxin 1B monoclonal antibody IgG1 derived from mouse, immunized with recombinant Shiga-like toxin 1 subunit B ( E. coli O157:H7). The subunit B has nontoxic action and is a functional region which binds to the receptor. Shiga-like toxin 1 subunit B contains amino acid from 2 to 90 of Shiga-like toxin 1subunit B, it forms pentamer binding to the host cell receptor.
Formulation
1x PBS and 0.05% sodium nitrate.
Purity
Greater than 95% as determined by 12% PAGE (coomassie staining).
More Info
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Introduction
Shiga-like toxin (verotoxin) is a toxin produced by some strains of Escherichia coli. Shiga-like toxin is named for its similarity to the AB5-type Shiga toxin produced by the bacteria Shigella dysenteriae. There are two known types-SLT1 and SLT2. The Shiga-like toxin is linked with hemolytic-uremic syndrome. Shiga-like toxin requires highly specific receptors on the cells'' surface in order to attach and enter the cell. Species such as cattle, swine, and deer which do not carry these receptors may harbor toxigenic bacteria without any ill effect, dropping them in their feces, from where they may be distributed to humans. Shiga Like Toxin-1 Subunit B has nontoxic action, it is the functional region which binds to the receptor. The Shiga Like Toxin-1 Subunit B can be useful in vaccine study, antibody test and other functional research.
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Physical Appearance
Sterile Filtered clear colorless solution.
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Stability
Shiga like toxin 1B monoclonal antibody although stable at 4°C for 1 week, should be stored 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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Type
Mouse antibody Monoclonal.
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 :
CXCL4 Variant 1 HumanDescription:
Platelet Factor-4 Variant 1 Human Recombinant
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Product # :
CHM-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL4 Variant-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa. The CXCL4 Variant-1 is fused to 6xHis tag at N-Terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized without additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets . Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily. Human PF4 is used for the proof of induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.
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Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
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Physical Appearance
Sterile Filtered white lyophilized powder.
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Stability
Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CXCL4 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
MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.
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 :
SCGB1A1 MouseDescription:
Uteroglobin Mouse Recombinant
Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.
Product # :
CYT-746Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Uteroglobin Mouse Recombinant produced in E.coli is a non-glycosylated disulfide-linked homodimeric protein containing 2x75 amino acids chains and having a molecular mass of 16.7kDa.The SCGB1A1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Uteroglobin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the ability of the immobilized protein to support the adhesion of the A549 human lung carcinoma cells is less than 5.0µg/ml, corresponding to a specific activity of > 200 IU/mg.More Info
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Introduction
Uteroglobin (SCGB1A1) which belongs to the Secretoglobin (SCGBs) superfamily, is a multifunctional protein that exerts anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules such as phospholipids and prostaglandins. Uteroglobin is involved in numerous functions including anti-inflammation, inhibition of phospholipase A2 and the sequestering of hydrophobic ligands. SCGB1A1 is expressed by Clara cells, the non-ciliated, non-mucous secretory cells predominant in lung bronchioles, and by other epithelia which communicate with the external environment. On top of sequestering pro-inflammatory mediators and carcinogens, Uteroglobin is implicated in the inhibition of cell migration and invasion, platelet aggregation, and T cell differentiation. SCGB1A1 gene defects are associated with a susceptibility to asthma.
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Synonyms
Uteroglobin, Clara cell 17 kDa protein, Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Scgb1a1, Ugb, Utg, UG, CC16, CCSP, PCB-BP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Uteroglobin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCGB1A1 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 SCGB1A1 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
DICPGFLQVL EALLMESESG YVASLKPFNP GSDLQNAGTQ LKRLVDTLPQ ETRINIMKLT EKILTSPLCK QDLRF.
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 :
SEPSECS MouseDescription:
Selenocysteinyl-tRNA(Sec) synthase Mouse Recombinant
AA986712, D5Ertd135e, SecS, SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein, SepSecS.
Product # :
ENZ-1081Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SEPSECS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 527 amino acids (1-504 a.a.) and having a molecular mass of 57.7kDa.SEPSECS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SEPSECS protein solution (0.25 mg/ml) is formulated in 20mM Tris-HCl buffer (pH7.5) 1mM DTT, 0.2M NaCl and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SEPSECS catalyzes the last step of sec synthesis by converting O-phosphoseryl-tRNA(sec) to selenocysteinyl-tRNA(sec) using selenophosphate as the selenium donor. Furthermore, SEPSECS protein is considered a specific marker of autoimmune hepatitis.
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Synonyms
AA986712, D5Ertd135e, SecS, SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein, SepSecS.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNPESFA AGERRVSPAY VRQGCEARRA HEHLIRLLLE QGKCPEDGWD ESTLELFLHE LAVMDSNNFL GNCGVGEREG RVASALVARR HYRFIHGIGR SGDISAVQPK AAGSSLLNKI TNSLVLNVIK LAGVHSVASC FVVPMATGMS LTLCFLTLRH
KRPKAKYIIW PRIDQKSCFK SMVTAGFEPV VIENVLEGDE LRTDLKAVEA KIQELGPEHI LCLHSTTACF APRVPDRLEE LAVICANYDI PHVVNNAYGL QSSKCMHLIQ QGARVGRIDA FVQSLDKNFM VPVGGAIIAG FNEPFIQDIS KMYPGRASAS PSLDVLITLL SLGCSGYRKL
LKERKEMFVY LSTQLKKLAE AHNERLLQTP HNPISLAMTL KTIDGHHDKA VTQLGSMLFT RQVSGARAVP LGNVQTVSGH TFRGFMSHAD NYPCAYLNAA AAIGMKMQDV DLFIKRLDKC LNIVRKEQTR ASVVSGADRN KAEDADIEEM ALKLDDVLGD VGQGPAL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Leptin Human, PEGDescription:
Leptin Human Recombinant, PEG
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1108Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pegylated Leptin Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Leptin Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
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
Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It’s in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo it has profound weight reducing effect, resulting mainly from reduced food intake.
More Info
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Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
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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 Pegylated leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K 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 Pegylated leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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 :
HexarelinDescription:
Hexarelin
Product # :
HOR-288Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Hexarelin has 7 amino acids H-His-D-2-Methyl-Trp-Ala-Trp-D-Phe-Lys-NH2 and having a molecular weight of 887 Dalton. The Molecular Formula is C47H58N12O6.
Formulation
The Hexarelin peptide was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Hexarelin stimulates GH secretion. Hexarelin is more resistant to proteolytic degradation than GHRP-6.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
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Stability
Lyophilized Hexarelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hexarelin 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 Hexarelin 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Fra e 1.0101Description:
Allergen Fra e 1.0101 Recombinant
Allergen Fra e 1.0101, Fra e 1.0101, Fra e 1.
Product # :
PRO-2286Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Allergen Fra e 1.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 17,794 Dalton. Fra e 1.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Fra e 1.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Allergen Fra e 1.0101 (Fra e 1.0101) causes an allergic reaction in humans.
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Synonyms
Allergen Fra e 1.0101, Fra e 1.0101, Fra e 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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Molar extinction coefficient
14815; A280(1mg/ml)=0.833
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 :
Betacellulin BovineDescription:
Betacellulin Bovine Recombinant
Product # :
CYT-406Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Betacellulin Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9003 Dalton. Betacellulin Bovine Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Betacellulin Bovine Recombinant was lyophilized after extensive dialysis against 50mM acetic acid.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.
More Info
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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Betacellulin Bovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC Bovine 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 BTC Bovine 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 Asp-Gly-Asn-Ser-Thr.
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Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 9kDa.
What is the source or expression system of BETACELLULIN Protein?
Escherichia Coli.
What is the Purity of BETACELLULIN Protein?
BETACELLULIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BETACELLULIN Protein?
The ED50, calculated by the dose-dependent proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 10.0 ng/ml, corresponding to a Specific Activity 100,000 units/mg.
What is the amino acid sequence of BETACELLULIN Protein?
BETACELLULIN Protein is composed from 80 amino acids.
What applications can BETACELLULIN Protein be used in?
BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN Protein was purified using conventional chromatography techniques.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.59 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 a calibrated solution of BTC 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.
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Name :
SHH RatDescription:
Sonic HedgeHog Rat Recombinant
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Product # :
CYT-1099Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Sonic HedgeHog Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.9kDa. SHH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SHH is lyophilized from a sterile (0.2 µm) filtered solution containing 10 mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog helps in guiding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is necessary for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
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Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SHH 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
MIIGPGRGFG KRQHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKARI HCSVKAENSV AAKSDG.
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 :
Transferrin HumanDescription:
Transferrin Human Recombinant
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Product # :
PRO-747Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Transferrin produced in Plant is a non-glycosylated, polypeptide chain containing 679 amino acids and having a molecular mass of 76 kDa. The Recombinant Human Transferrin is purified by proprietary chromatographic techniques.
Source
Oryza sativa (rice).
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Purity as determined by SDS-PAGE is 97%.
Biological Activity
One mg of Recombinant Human Transferrin will bind to approximately 2 micrograms of Fe.
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
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Stability
Lyophilized Transferrin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transferrin Human Recombinant 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
Stock solutions can be prepared by dissolving gently into PBS for several minutes. Recommended stock concentrations are 5mg/ml to 20 mg/ml in PBS, though others can be used as well. Please try to avoid the formation of bubbles when dissolving the protein. Sterile filter through 0.2µm filter.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin qA Rat, PEGDescription:
Leptin Quadruple Antagonist, Pegylated Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1241Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Rat Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro.
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Rat Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of rat pegylated leptin antagonist and filter sterilization rat pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Rat Leptin Pegylated Quadruple Antagonist 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 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 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.
- View Data Sheet
Name :
Ag85ADescription:
Mycobacterium Tuberculosis major secretory protein Antigen 85A Recombinant
Ronectin-binding protein A, Mycolyl transferase 85A.
Product # :
PRO-1076Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Mycobacterium tuberculosis Ag85A (43-338 a.a) produced in Hi-5 cells is a single, glycosylated polypeptide chain having a molecular mass of 32.8kDa (305 a.a in total).Antigen 85A is fused to a 6 amino acid His tag at C-terminus and purified by conventional chromatographic techniques.
Source
Baculovirus
Formulation
The Ag85A solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Antigen 85A is a member of the antigen 85 complex (Antigen 85A, B, C). The enzymes of the antigen 85 complex have mycolyltransferase activity and catalyze the synthesis of the very rich glycolipid of the mycobacterial cell wall, the cord factor (trehalose 6,6'-dimycolate, TDM). The cord factor is vital for the integrity of the mycobacterial cell wall and pathogenesis of the bacillus. TDM is synthesized from two molecules of trehalose-6'-monomycolate (TMM) by Antigen 85A.
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Synonyms
Ronectin-binding protein A, Mycolyl transferase 85A.
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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
ADPAFSRPGL PVEYLQVPSP SMGRDIKVQF QSGGANSPAL YLLDGLRAQD DFSGWDINTP AFEWYDQSGL SVVMPVGGQS SFYSDWYQPA CGKAGCQTYK WETFLTSELP GWLQANRHVK PTGSAVVGLS MAASSALTLA IYHPQQFVYA GAMSGLLDPS QAMGPTLIGL AMGDAGGYKA SDMWGPKEDP AWQRNDPLLN VGKLIANNTR VWVYCGNGKP SDLGGNNLPA KFLEGFVRTS NIKFQDAYNA GGGHNGVFDF PDSGTHSWEY WGAQLNAMKP DLQRALGATP NTGPAPQGAH HHHHH.
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 :
DCN MouseDescription:
Decorin Mouse Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
Product # :
PRO-2234Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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Description
DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
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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.
-
Amino Acid Sequence
GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
C1GALT1 HumanDescription:
Core 1 Beta3-Gal-T1 Human Recombinant
Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Core 1 Beta3-Gal-T1, Core 1 O-Glycan T-Synthase, Core 1 UDP-Galactose:N-Acetylgalactosamine-Alpha-R Beta 1,3 Galactosyltransferase 1, B3Gal-T8, EC 2.4.1.122, Core 1 Beta3-Gal-T, C1GALT, T-synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Beta-1,3-galactosyltransferase, C1GalT1, Core 1 Beta1,3-Galactosyltransferase 1.
Product # :
ENZ-721Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
C1GALT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (30-363 a.a) and having a molecular mass of 41.4kDa.C1GALT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
C1GALT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
Core 1 Beta3-Gal-T1 also known as,C1GALT1 creates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for lots of extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice have shown that this gene takes a main role in angiogenesis, thrombopoiesis and kidney homeostasis.
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Synonyms
Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Core 1 Beta3-Gal-T1, Core 1 O-Glycan T-Synthase, Core 1 UDP-Galactose:N-Acetylgalactosamine-Alpha-R Beta 1,3 Galactosyltransferase 1, B3Gal-T8, EC 2.4.1.122, Core 1 Beta3-Gal-T, C1GALT, T-synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Beta-1,3-galactosyltransferase, C1GalT1, Core 1 Beta1,3-Galactosyltransferase 1.
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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 MGSLLGEKVD TQPNVLHNDP HARHSDDNGQ NHLEGQMNFN ADSSQHKDEN TDIAENLYQK VRILCWVMTG PQNLEKKAKH VKATWAQRCN KVLFMSSEEN KDFPAVGLKT KEGRDQLYWK TIKAFQYVHE HYLEDADWFL KADDDTYVIL DNLRWLLSKY DPEEPIYFGR RFKPYVKQGY MSGGAGYVLS KEALKRFVDA FKTDKCTHSS SIEDLALGRC MEIMNVEAGD SRDTIGKETF HPFVPEHHLI KGYLPRTFWY WNYNYYPPVE GPGCCSDLAV SFHYVDSTTM YELEYLVYHL RPYGYLYRYQ PTLPERILKE ISQANKNEDT KVKLGNP.
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 :
PODXL MouseDescription:
Podocalyxin-Like Mouse Recombinant
Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.
Product # :
PRO-2310Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PODXL Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 391 amino acids (22-404a.a.) and having a molecular mass of 41.0kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). PODXL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PODXL protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Podocalyxin (PODXL) is a greatly glycosylated transmembrane sialoprotein in the CD34 and endoglycan family. The PODXL protein is involved in the regulation of both adhesion and cell morphology and cancer progression. PODXL functions as an anti-adhesive molecule, which retains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Moreover, PODXL serves as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner.
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Synonyms
Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
HNGNETSTSA IKSSTVQSHQ SATTSTEVTT GHPVASTLAS TQPSNPTPFT TSTQSPSMPT STPNPTSNQS GGNLTSSVSE VDKTKTSSPS STAFTSSSGQ TASSGGKSGD SFTTAPTTTL GLINVSSQPT DLNTTSKLLS TPTTDNTTSP QQPVDSSPST ASHPVGQHTP AAVPSSSGST PSTDNSTLTW KPTTHKPLGT SEATQPLTSQ TPGITTLPVS TLQQSMASTV GTTTEEFTHL ISNGTPVAPP GPSTPSPIWA FGNYQLNCEP PIRPDEELLI LNLTRASLCE RSPLDEKEKL VELLCHSVKA SFKPAEDLCT LHVAPILDNQ AVAVKRIIIE TKLSPKAVYE LLKDRWDDLT EAGVSDMKLG KEGPPEVNED RFSLEHHHHH H.
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 :
S100A8 HumanDescription:
S100 Calcium Binding Protein A8 Human Recombinant
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
Product # :
PRO-800Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids (1-93 a.a.) and having a molecular mass of 10.8 kDa. The S100A8 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The S100A8 solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.
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Synonyms
Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.
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Physical Appearance
Sterile Filtered clear 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
MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.
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 :
SEC22B HumanDescription:
SEC22 Homolog B Human Recombinant
SEC22 Vesicle Trafficking Protein Homolog B (S. Cerevisiae) Gene/Pseudogene, SEC22 Vesicle Trafficking Protein-Like 1 (S. Cerevisiae), ER-Golgi SNARE Of 24 KDa, SEC22L1, ERS-24.
Product # :
PRO-1212Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SEC22B Human Recombinant produced in E. coli is a single polypeptide chain containing 205 amino acids (14-194) and having a molecular mass of 23.3 kDa.SEC22B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SEC22B solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 0.15M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Vesicle-trafficking protein SEC22b precursor (SEC22B) is a member of the synaptobrevin family. SEC22B forms a complex with SNARE and it is believed to have a role in the ER-Golgi protein trafficking. SEC22B has a strong similarity to the mouse and Chinese hamster proteins.
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Synonyms
SEC22 Vesicle Trafficking Protein Homolog B (S. Cerevisiae) Gene/Pseudogene, SEC22 Vesicle Trafficking Protein-Like 1 (S. Cerevisiae), ER-Golgi SNARE Of 24 KDa, SEC22L1, ERS-24.
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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 MGSM LPLAAS MQEDEQSGRD LQQYQSQAKQ LFRKLNEQSP TRCTLEAGAM TFHYIIEQGV CYLVLCEAAF PKKLAFAYLE DLHSEFDEQH GKKVPTVSRP YSFIEFDTFI QKTKKLYIDS RARRNLGSIN TELQDVQRIM VANIEEVLQR GEALSALDSK ANNLSSLSKK YRQDAKYLNM RSTYA
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 :
Noggin HumanDescription:
Noggin Human Recombinant
SYM1, SYNS1, NOG.
Product # :
CYT-475Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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- biological activity
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Description
Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.
More Info
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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC. -
Background
Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.
Abstract:
Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.
Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.
This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.
Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
- Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.
Molecular Characteristics of Noggin :
- This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.
Inhibition of BMP Signaling by Noggin:
- Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.
Physiological Functions of Noggin:
- Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.
Therapeutic Implications of Noggin:
- The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.
Clinical Studies and Translational Research:
- This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Noggin MouseDescription:
Noggin Mouse Recombinant
Noggin, SYM1, SYNS1, NOG.
Product # :
CYT-600Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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- biological activity
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Description
Noggin Mouse Recombinant produced in E.Coli is a non-glycosylated, disulfide-linked protein consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.4 kDa (each chain 23.2 kDa).
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered solution in 30% acetonitrile, 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by inhibiting BMP-4-induced alkaline phosphatase production of murine ATDC5 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg in the presence of 5ng/ml BMP-4.More Info
-
Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
Noggin, SYM1, SYNS1, NOG.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Mouse Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse Noggin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
-
Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYD
PGFMATSPPEDRPGGGGGPAGGAEDLAELDQLLRQRPSGAMPSEIKG
LEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRF
WPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGQR
CGWIPIQYPIISECKCSC.
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 :
CD164L2 HumanDescription:
CD164 Sialomucin-Like 2 Human Recombinant
CD164 Sialomucin-Like 2, EAPG6122, UNQ6122, CD164 Sialomucin-Like 2 Protein.
Product # :
PRO-1892Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD164L2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (30-141 a.a) and having a molecular mass of 14.4kDa.CD164L2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CD164L2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CD164 Sialomucin-Like 2, also known as CD164L2 is amember of the CD164 family.
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Synonyms
CD164 Sialomucin-Like 2, EAPG6122, UNQ6122, CD164 Sialomucin-Like 2 Protein.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGKGARGF GRGALIRLNI WPAVQGACKQ LEVCEHCVEG DRARNLSSCM WEQCRPEEPG HCVAQSEVVK EGCSIYNRSE ACPAAHHHPT YEPKTVTTGS PPVPEAHSPG FDGAS
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 :
Latexin HumanDescription:
Latexin Human Recombinant
LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.
Product # :
ENZ-407Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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- More Info
Description
Recombinant Human Latexin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids and having a molecular mass of 25.7kDa. Latexin is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The Latexin protein solution contains 20mM Tris-HCl, pH-7.5, 50mM NaCl and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.
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Synonyms
LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.
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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
MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYRLKFAVEE IIQKQVKVNC TAEVLYPSTG QETAPEVNFTFEGETGKNPD EEDNTFYQRL KSMKEPLEAQ NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDYTILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE.
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 :
GHRL HumanDescription:
Ghrelin Human Recombinant
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
Product # :
HOR-294Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Ghrelin Human Recombinant contains 115 amino acids (24-117 a.a.) and a total molecular mass of 12.8 kDa. The GHRL is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ghrelin protein solution contains 20mM Tris-HCl, pH-8 & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.
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Synonyms
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
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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 MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
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Background
What is the molecular weight/Mw of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein has a total Mw of 12.8kDa.
What is the source or expression system of GHRELIN HUMAN Protein?
Escherichia Coli.
What is the Purity of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GHRELIN HUMAN Protein?
The biological functionality of GHRELIN HUMAN Protein will be determined in the future.
What is the amino acid sequence of GHRELIN HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
What applications can GHRELIN HUMAN Protein be used in?
GHRELIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GHRELIN HUMAN Protein?
The endotoxin level is minimal, GHRELIN 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.
- View Data Sheet
Name :
Clusterin Human, HisDescription:
Apolipoprotein-J Human Recombinant, His Tag
CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU.
Product # :
CYT-814Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- formulation
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- sds-page
Description
Clusterin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 463 amino acids (23-449 a.a.) and having a molecular mass of 54.1kDa. Clusterin is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Clusterin protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others. -
Synonyms
CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE.
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Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 54.1kDa.
What is the source or expression system of CLUSTERIN Protein?
Escherichia Coli.
What is the Purity of CLUSTERIN Protein?
CLUSTERIN Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CLUSTERIN Protein?
The biological functionality of CLUSTERIN Protein will be determined in the future.
What is the amino acid sequence of CLUSTERIN Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE.
What applications can CLUSTERIN Protein be used in?
CLUSTERIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN 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.