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1000 results found for “Noggin”
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Name :
IL37 HumanDescription:
Interleukin-37 Human Recombinant
Interleukin-37, FIL1 zeta, IL-1X, Interleukin-1 family member 7, IL-1F7, Interleukin-1 homolog 4, IL-1H, IL-1H4, Interleukin-1 zeta, IL-1 zeta, Interleukin-1-related protein, IL-1RP1, Interleukin-23, IL-37, IL37, FIL1Z, IL1F7, IL1H4, IL1RP1, FIL1, FIL1(ZETA).
Product # :
CYT-011Price :
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Shipped at Room temp
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Description
Interleukin-37 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 167 amino acids (Lys27-Asp192) and having a molecular mass of 18.6kDa.The IL37 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL37 was lyophilized from a 0.2μM filtered solution of 20mM PB, 150mM NaCl and 2mM DTT pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
As measured by its binding ability in a functional ELISA, immobilized IL1F7 at 1 µg/ml (100 µl/well) can bind rhIL-18 R/Fc Chimera with a linear range of 0.015-1µg/ml.More Info
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Introduction
Human interleukin family 1, member 7 (IL1F7) belongs to the interleukin 1 cytokine family. There are 5 alternatively spliced transcript variants encoding distinct isoforms with distinct expression profiles. The longest IL-1F7 transcript, named IL1F7b or IL1F7 isoform 1, encodes a 218 aa residues proprotein and containing a 45 aa propeptide which is cleaved to produce a mature protein. IL1F7b binds to IL18 Rb with low affinity however it doesn’t exert any IL18 agonistic or antagonistic effects. IL1F7b also binds IL18BP (interleukin 18 binding protein), which is an inhibitory binding protein of interleukin 18 (IL18), and afterward forms a complex with IL18 receptor beta subunit, and through which it inhibits the activity of IL18.
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Synonyms
Interleukin-37, FIL1 zeta, IL-1X, Interleukin-1 family member 7, IL-1F7, Interleukin-1 homolog 4, IL-1H, IL-1H4, Interleukin-1 zeta, IL-1 zeta, Interleukin-1-related protein, IL-1RP1, Interleukin-23, IL-37, IL37, FIL1Z, IL1F7, IL1H4, IL1RP1, FIL1, FIL1(ZETA).
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL37 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-37 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 quick spin followed by reconstitution of IL37 in PBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MKNLNPKKFSIHDQDHKVLVLDSGNLIAVPDKNYIRPEIFFALASSLSSASAEKGSPILLGVSKGEFCLYCDKDKGQSHPSLQLKKEKLMKLAAQKESARRPFIFYRAQVGSWNMLESAAHPGWFICTSCNCNEPVGVTDKFENRKHIEFSFQPVCKAEMSPSEVSD.
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 :
Resistin Human, AntagonistDescription:
Resistin Antagonist Human Recombinant
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-1255Price :
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Description
Resistin Human antagonist is a monomeric C7A mutant that does not form covalent dimers. Resistin Human antagonist is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
Resistin was lyophilized from a concentrated (1mg/ml) solution with 0.03% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.
(c) Analysis by RP-HPLC.
Biological Activity
The biological activity was evidenced by resistin antagonist activity to inhibit resistin-induced Akt phosphorylation in two cell lines. It also reduced the weight (mainly the visceral fat) and normalized GTT and ITT inHFD-fed mice.
More Info
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Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin Mouse 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 Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first seven N-terminal amino acids was determined and was found to be Ala-Ser-Ser-Lys-Thr-Leu-Ala.
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Background
Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis. Resistin blocks insulin stimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of low-density lipoprotein (LDL), increasing the risk of heart disease.
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 :
ANXA5 HumanDescription:
Annexin A5 Human Recombinant
PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.
Product # :
PRO-732Price :
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Shipped with Ice Packs
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Description
ANXA5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-320 a.a.) and having a molecular mass of 35.9 kDa.ANXA5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ANXA5 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ANXA5 is a member of the annexin family of calcium-dependent phospholipid binding proteins which are involved in membrane-related activity along exocytotic and endocytotic pathways. ANXA5 is a phospholipase A2 and protein kinase C inhibitory protein with calcium channel properties and takes part in cellular signal transduction, inflammation, growth and differentiation. ANXA5 is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. ANXA5 regulates coagulability in the blood stream by binding to phosphatidylserine and sulfatide. ANXA5 protects sinsuoidal endothelial cells from ischemia reperfusion damage. ANXA5 is necessary for normal CFTR chloride channel activity.
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Synonyms
PP4, ANX5, ENX2, ANXA5, Annexin A5, Annexin-5, Annexin V, Lipocortin V, Endonexin II, Calphobindin I, CBP-I, Placental anticoagulant protein I, PAP-I, Placental anticoagulant protein 4, Thromboplastin inhibitor, Vascular anticoagulant-alpha, VAC-alpha, Anchorin CII.
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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
MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI KGDTSGDYKK ALLLLCGEDD.
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 :
MAGOH HumanDescription:
Mago-Nashi Homolog Human Recombinant
MAGOH1, MAGOHA, Protein mago nashi homolog, MAGOH, proliferation-associated (Drosophila).
Product # :
PRO-810Price :
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Shipped with Ice Packs
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Description
MAGOH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids (1-146 a.a.) and having a molecular mass of 18.2 kDa. MAGOH protein is fused to a 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
MAGOH Human solution containing 20mM Tris-HCl pH-8, 2mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Drosophila that have mutations in their MAGOH gene produce progeny with defects in germplasm assembly and germline development. MAGOH, the human homolog of Drosophila mago nashi, is necessary for embryo development. In mammals, mRNA expression is not limited to the germ plasm, but is expressed ubiquitously in adult tissues and is induced by serum stimulation of quiescent fibroblast.
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Synonyms
MAGOH1, MAGOHA, Protein mago nashi homolog, MAGOH, proliferation-associated (Drosophila).
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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
MESDFYLRYY VGHKGKFGHE FLEFEFRPDG KLRYANNSNY KNDVMIRKEA YVHKSVMEEL KRIIDDSEIT KEDDALWPPP DRVGRQELEI VIGDEHISFT TSKIGSLIDV NQSKDPEGLR VFYYLVQDLK CLVFSLIGLH FKIKPILEHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL9 MouseDescription:
MIG Mouse Recombinant (CXCL9)
Small inducible cytokine B9, CXCL9, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, M119.
Product # :
CHM-337Price :
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Shipped at Room temp
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Description
MIG (CXCK9) Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 12208 Dalton. The MIG is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH7.4 and 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability to chemoattract Human lymphocytes using a concentration of 0.1-1 ng/ml.More Info
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Introduction
Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belonging to the CXC chemokine family that is also known as Monokine induced by MIG. CXCL9 is a T-cell chemoattractant. It is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.
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Synonyms
Small inducible cytokine B9, CXCL9, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, M119.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL9 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 MIG 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
TLVIRNARCS CISTSRGTIH YKSLKDLKQF APSPNCNKTE IIATLKNGDQ TCLDPDSANV KKLMKEWEKK INQKKKQKRG KKHQKNMKNR KPKTPQSRRR SRKTT.
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Background
What is the molecular weight/Mw of CXCL9 MOUSE Protein?
CXCL9 MOUSE Protein has a total Mw of 12.2kDa.
What is the source or expression system of CXCL9 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL9 MOUSE Protein?
CXCL9 MOUSE Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL9 MOUSE Protein?
The Activity is calculated by the ability to chemoattract Human lymphocytes using a concentration of 0.1-1 ng/ml.
What is the amino acid sequence of CXCL9 MOUSE Protein?
TLVIRNARCS CISTSRGTIH YKSLKDLKQF APSPNCNKTE IIATLKNGDQ TCLDPDSANV KKLMKEWEKK INQKKKQKRG KKHQKNMKNR KPKTPQSRRR SRKTT.
What applications can CXCL9 MOUSE Protein be used in?
CXCL9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL9 MOUSE Protein?
The endotoxin level is minimal, CXCL9 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NAP 2 95 a.a. HumanDescription:
Neutrophil Activating Protein-2 (CXCL7) Human Recombinant, 95 a.a.
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Product # :
CHM-277Price :
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Shipped with Ice Packs
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Description
NAP 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (35-128) and having a molecular mass of 10.3 kDa.The NAP 2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAP 2 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-7.5, 1mM DTT and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
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Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
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Physical Appearance
NAP 2 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
MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD
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 :
NAP 2 RatDescription:
Neutrophil Activating Protein-2 Rat Recombinant (CXCL7)
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Product # :
CHM-269Price :
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Shipped at Room temp
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Description
NAP-2 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 62 amino acids and having a molecular mass of 6.8kDa.The NAP 2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAP-2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to chemoattract BaF3 mouse pro-B cells transfected with human CXCR2. The ED50 for this effect is less than 10ng/ml, corresponding to a specific activity of 100,000units/mg.More Info
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Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
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Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NAP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL7 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 NAP-2 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
IELRCRCTNT LSGIPLNSIS RVNVFRPGAH CDNVEVIATL KNGKEVCLDP TAPMIKKIVK KI.
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 :
VEGI Human, HisDescription:
Vascular Endothelial Growth InhibitorHuman Recombinant, His Tag
Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.
Product # :
CYT-589Price :
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Shipped with Ice Packs
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Description
VEGI Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids(72-251a.a.) and having a molecular mass of 22.7kDa. The VEGI is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The VEGI solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50% glycerol, 1mM DTT and 0.2M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
TNFSF15 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of TNFSF15 is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. TNFSF15 is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. An additional isoform encoded by an alternatively spliced transcript variant has been reported but the sequence of this transcript has not been determined.
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Synonyms
Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.
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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 MLKGQEFAPS HQQVYAPLRA DGDKPRAHLT VVRQTPTQHF KNQFPALHWE HELGLAFTKN RMNYTNKFLL IPESGDYFIY SQVTFRGMTS ECSEIRQAGR PNKPDSITVV ITKVTDSYPE PTQLLMGTKS VCEVGSNWFQ PIYLGAMFSL QEGDKLMVNV SDISLVDYTK EDKTFFGAFL L
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ARTN HumanDescription:
Artemin Human Recombinant
ART, ARTN , EVN, NBN.
Product # :
CYT-306Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.More Info
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Introduction
The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.
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Synonyms
ART, ARTN , EVN, NBN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Artemin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Artemin 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
It is recommended to reconstitute the lyophilized Artemin 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
AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.
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Background
Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications
Abstract:
Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.
Introduction:
Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.
Artemin Signaling and Mechanisms:
Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.
Artemin in Neurological Disorders:
Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.
Therapeutic Potential of Artemin Human Recombinant:
Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.
Challenges and Future Directions:
While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.
Conclusion:
Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.
What is the molecular weight/Mw of ARTN Protein?
ARTN Protein has a total Mw of 24.2kDa.
What is the source or expression system of ARTN Protein?
Escherichia Coli.
What is the Purity of ARTN Protein?
ARTN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of ARTN Protein?
The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.
What is the amino acid sequence of ARTN Protein?
AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.
What applications can ARTN Protein be used in?
ARTN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ARTN Protein?
The endotoxin level is minimal, ARTN 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 :
Lymphotactin HumanDescription:
Lymphotactin Human Recombinant (XCL1)
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Product # :
CHM-314Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Lymphotactin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 92 amino acids and having a molecular mass of 10007 Dalton. The Lymphotactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The XCL1 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
-
Introduction
Chemokine (C motif) ligand (XCL1) is a small cytokine belonging to the XC chemokine family that is also known as lymphotactin. It is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to another chemokine called XCL2, whose geneis found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
-
Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Lymphotactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution XCL1 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.
-
Solubility
It is recommended to reconstitute the lyophilized Lymphotactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Ser-Glu-Val-Ser.
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 :
NCF1 HumanDescription:
Neutrophil Cytosolic Factor 1 Human Recombinant
NCF1A, NOXO2, p47phox, SH3PXD1A .
Product # :
PRO-488Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
NCF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-390 a.a.) and having a molecular mass of 45.7 kDa. The NCF1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.5mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
NCF1 is a cytosolic subunit protein of neutrophil NADPH oxidase which a
Multi-component enzyme that is activates production of superoxide anion. NCF1, along with NCF2 and a membrane bound cytochrome b558, is necessary for activation of the latent NADPH oxidase necessary for superoxide production. Mutations in this NCF1 have been related with chronic granulomatous disease. -
Synonyms
NCF1A, NOXO2, p47phox, SH3PXD1A .
-
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
MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG EAVEVIHKLL DGWWVIRKDDVTGYFPSMYL QKSGQDVSQA QRQIKRGAPP RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV VEHHHHHH.
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 :
ARPC5 HumanDescription:
Actin Related Protein 2/3 Complex, Subunit 5 Human Recombinant
Actin-related protein 2/3 complex subunit 5, Arp2/3 complex 16 kDa subunit, p16-ARC, ARPC5, ARC16, MGC88523, dJ127C7.3.
Product # :
PRO-145Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARPC5 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 171 amino acids (1-151 a.a.) and having a molecular mass of 18.4kDa. The ARPC5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARPC5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
ARPC5 is a 151 amino acid subunit of the Arp2/3 complex. ARPC5 is believed to have a role in maintaining the integrity of Arp2/3. ARPC5 is a substrate for MAPKAPK-2 which, via phosphorylation of ARPC5, may participate in Arp2/3 regulatory functions and remodeling of the Actin cytoskeleton.
-
Synonyms
Actin-related protein 2/3 complex subunit 5, Arp2/3 complex 16 kDa subunit, p16-ARC, ARPC5, ARC16, MGC88523, dJ127C7.3.
-
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
MGSSHHHHHH SSGLVPRGSH MSKNTVSSAR FRKVDVDEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN SSAMLLQWHE KALAAGGVGS IVRVLTARKT V.
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 :
NTS HumanDescription:
Neurotensin Human Recombinant
NTS, Neurotensin, NT/N, NMN-125, NTS1, NN, Neurotensin/Neuromedin N, NT.
Product # :
PRO-1311Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
NTS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (24-170 a.a.) and having a molecular mass of 19.9kDa.NTS is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NTS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
-
Synonyms
NTS, Neurotensin, NT/N, NMN-125, NTS1, NN, Neurotensin/Neuromedin N, NT.
-
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
MGSSHHHHHH SSGLVPRGSH MGSHMSDSEE EMKALEADFL TNMHTSKISK AHVPSWKMTL LNVCSLVNNL NSPAEETGEV HEEELVARRK LPTALDGFSL EAMLTIYQLH KICHSRAFQH WELIQEDILD TGNDKNGKEE VIKRKIPYIL KRQLYENKPR RPYILKRDSY YY.
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 :
Follistatin MouseDescription:
Follistatin Mouse Recombinant
Follistatin, FST, FS, Activin-binding protein, AL033346.
Product # :
CYT-124Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
- More Info
Description
Follistatin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 289 amino acids and having a total molecular mass of 31.6kDa.The FST is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Mouse Follistatin is lyophilized from 10mM Na2PO4 and 50mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50, determined by the dose-dependent neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, is 0.13-0.19µg/ml.More Info
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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
-
Synonyms
Follistatin, FST, FS, Activin-binding protein, AL033346.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Follistatin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.
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Background
What is the molecular weight/Mw of FOLLISTATIN MOUSE Protein?
FOLLISTATIN MOUSE Protein has a total Mw of 31.6kDa.
What is the source or expression system of FOLLISTATIN MOUSE Protein?
Escherichia Coli.
What is the Purity of FOLLISTATIN MOUSE Protein?
FOLLISTATIN MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of FOLLISTATIN MOUSE Protein?
The ED50, determined by the dose-dependent neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, is 0.13-0.19µg/ml.
What is the amino acid sequence of FOLLISTATIN MOUSE Protein?
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.
What applications can FOLLISTATIN MOUSE Protein be used in?
FOLLISTATIN MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN MOUSE Protein?
The endotoxin level is minimal, FOLLISTATIN MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
KIT HumanDescription:
KIT Proto-Oncogene Receptor Tyrosine Human Recombinant
Mast/stem cell growth factor receptor Kit, SCFR, Piebald trait protein, PBT, Proto-oncogene c-Kit, Tyrosine-protein kinase Kit, p145 c-kit, v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog, CD117.
Product # :
PKA-102Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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- purity
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Description
KIT produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 507 amino acids (26-524 a.a.) and having a molecular mass of 57.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).KIT is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus.
Formulation
KIT protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
KIT, also known as KIT Proto-Oncogene Receptor Tyrosine, is a cytokine receptor which is expressed not only in hematopoietic stem cells but likewise in other cell types. KIT binds to receptor tyrosine kinase type III, which is a stem cell factor, also named a "rigid factor" or "c-kit ligand". Once this receptor binds to stem cell factor (SCF), it forms a dimer which activates intrinsic tyrosine kinase activity, which sequentially phosphorylates & activates signaling molecules which breed signals in cells. This receptor protects vascular smooth muscle cells from apoptosis in addition to restoring cardiac function after myocardial infarction.
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Synonyms
Mast/stem cell growth factor receptor Kit, SCFR, Piebald trait protein, PBT, Proto-oncogene c-Kit, Tyrosine-protein kinase Kit, p145 c-kit, v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog, CD117.
-
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
QPSVSPGEPS PPSIHPGKSD LIVRVGDEIR LLCTDPGFVK WTFEILDETN ENKQNEWITE KAEATNTGKY TCTNKHGLSN SIYVFVRDPA KLFLVDRSLY GKEDNDTLVR CPLTDPEVTN YSLKGCQGKP LPKDLRFIPD PKAGIMIKSV KRAYHRLCLH CSVDQEGKSV LSEKFILKVR PAFKAVPVVS VSKASYLLRE GEEFTVTCTI KDVSSSVYST WKRENSQTKL QEKYNSWHHG DFNYERQATL TISSARVNDS GVFMCYANNT FGSANVTTTL EVVDKGFINI FPMINTTVFV NDGENVDLIV EYEAFPKPEH QQWIYMNRTF TDKWEDYPKS ENESNIRYVS ELHLTRLKGT
EGGTYTFLVS NSDVNAAIAF NVYVNTKPEI LTYDRLVNGM LQCVAAGFPE PTIDWYFCPG TEQRCSASVL PVDVQTLNSS GPPFGKLVVQ SSIDSSAFKH NGTVECKAYN DVGKTSAYFN FAFKGNNKEQ IHPHTLFTPL EHHHHHH.
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 :
CHGB HumanDescription:
Chromogranin B Human Recombinant
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
Product # :
PRO-824Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
-
Introduction
CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.
-
Synonyms
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
-
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
MGSSHHHHHH SSGLVPRGSH MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
WIBG HumanDescription:
within BCGN Homolog Human Recombinant
PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.
Product # :
PRO-864Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
WIBG Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-204 a.a.) and having a molecular mass of 23.7 kDa. The WIBG is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
WIBG Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
WIBG is a cooperateing partner of Mago-Y14. The Mago-Y14 heterodimer is a key protein of the EJC(exon junction complex) that is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. WIBG is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. WIBG relates directly with Mago-Y14 by means of its N-terminal domain.
-
Synonyms
PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ QEKGEAEALS RTLDKVSLEE TAQLPSAPQG SRAAPTAASD QPDSAATTEK AKKIKNLKKK LRQVEELQQR IQAGEVSQPS KEQLEKLARR RALEEELEDL ELGLLEHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BDNF Human, CHODescription:
Brain-Derived Neurotrophic Factor Human Recombinant, CHO
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-1262Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
Description
Brain-derived Neurotrophic Factor Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 119 amino acids and having a total molecular mass of 27kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
CHO Cells
Formulation
The protein was lyophilized with 5% trehalose and 1x PBS
Purity
Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.sds-page
More Info
-
Introduction
BDNF is crucial for the signal survival eukaryotes. BDNF is responsible for the development, repair, adaptation and proper functionality of the nervous system.
BDNF major roles include Neuron survival and development, synaptic flexibility, stress adaptation, Repair and recovery post injury/disease and Pain signaling.
-
Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
CHO Cells
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.
What is the amino acid sequence of BDNF Protein?
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
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References
Title:Generation of Neurons with Improved Cell Survival and Phenotype Maintenance Using a Degradation-Resistant Nurr1 Mutant†‡
Publication:Article first published online: 11 JUN 2009 DOI: 10.1002/stem.146 Copyright © 2009 AlphaMed Press.
Link:BDNF prospec publication
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 :
Desmin HumanDescription:
Desmin Human Recombinant
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
Product # :
PRO-520Price :
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Shipped at Room temp
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Description
Desmin Human Recombinant having a calculated molecular mass of 53,539 Dalton, showing a 55kDa band on SDS-page, pI-5.16.
Source
Escherichia Coli.
Formulation
Desmin was lyophilized from a 1mg/ml solution containing 30mM Tris-HCl pH 8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Desmin is a muscle-specific class III intermediate filament. Homopolymers of this protein form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. Mutations in this gene are associated with desmin-related myopathy, a familial cardiac and skeletal myopathy (CSM), and with distal myopathies.
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Synonyms
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Desmin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
After Desmin is dissolved in 9.5M urea buffer (see formulation), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Tris-HCl, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).
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 :
NTS Human, sf9Description:
Neurotensin Human Recombinant, sf9
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
Product # :
PRO-2374Price :
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Description
NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NTS protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
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Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
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Synonyms
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
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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
ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NUP62 HumanDescription:
Nucleopurin 62kDa Human Recombinant
Nuclear pore glycoprotein p62, 62 kDa nucleoporin, Nucleoporin Nup62, NUP62, p62, IBSN, SNDI.
Product # :
PRO-999Price :
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Description
NUP62 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 66 kDa. NUP62 is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
NUP62 is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Nucleopurin 62kDa (NUP62) belongs to the FG-repeat containing nucleoporins and is localized to the nuclear pore central plug. Nucleoporins are the principal components of the nuclear pore complex in eukaryotic cells. This complex is a colossal structure which extends across the nuclear envelope, forming an entryway that regulates the stream of macromolecules between the nucleus and the cytoplasm. NUP62 associates with the importin alpha/beta complex that is involved in the import of proteins containing nuclear localization signals. Defects in the NUP62 are the cause of SNDI (infantile striatonigral degeneration), aka infantile bilateral striatal necrosis (IBSN) or familial striatal degeneration.
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Synonyms
Nuclear pore glycoprotein p62, 62 kDa nucleoporin, Nucleoporin Nup62, NUP62, p62, IBSN, SNDI.
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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 IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera), immunodot analysis with positive/negative samples.
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coating concentration
0.5-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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Applications
Western blot with Polyclonal anti-Nup62 antibodies.
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 :
C17ORF103 HumanDescription:
Chromosome 17 Open Reading Frame 103 Human Recombinant
Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.
Product # :
PRO-1619Price :
Quantity :
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Description
C17ORF103 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113) and having a molecular mass of 15.4kDa.C17ORF103 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The C17ORF103 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
C17orf103 is a member of the GTLF3B family and is encoded by a gene which is located in human chromosome 17p11.2. BRCA1 and p53 are 2 main tumor suppressor genes which are linked to chromosome 17. Tumor suppressor p53 is necessary for maintenance of cellular genetic integrity by moderating cell fate through DNA repair versus cell death. C17orf103 is also related to neurofibromatosis, a disorder characterized by neural and epidermal lesions, and dysregulated Schwann cell growth.
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Synonyms
Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.
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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 MGSMAHSAAA VPLGALEQGC PIRVEHDRRR RQFTVRLNGC HDRAVLLYEY VGKRIVDLQH TEVPDAYRGR GIAKHLAKAA LDFVVEEDLK AHLTCWYIQK YVKENPLPQY LERLQP
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 :
VEGF (121 a.a.) HumanDescription:
Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-343Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.
More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 Vascular Endothelial Growth Factor -121 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
APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENCDKPR R
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 :
FGFR1OP Human (1-80)Description:
FGFR1 Oncogene Partner (1-80 a.a.) Human Recombinant
FGFR1 oncogene partner, FGFR1OP, FOP.
Product # :
PKA-138Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The FGFR1O PHuman is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FGFR1OP His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 80 amino acid residues of the FGFR1OP Human, 1-80 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
FGFR1 oncogene partner, FGFR1OP, FOP.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized FGFR1OP at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
L MAATAAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE SLRKFLNTKD GRLVASLVA
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Background
FGFR1 oncogene partner also known as FGFR1OP is a leucine-rich member of the FGFR1OP family. The ensuing chimeric protein contains the N-terminal leucine-rich region of the FGFR1OP protein fused to the catalytic domain of FGFR1. The FGFR1OP plays a main role in normal proliferation and differentiation of the erythroid lineage.
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.