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1000 results found for “mortality factor”
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Name :
MSRB2 HumanDescription:
Methionine Sulfoxide Reductase B2 Human Recombinant
CBS-1, PILB, Pilin-like Transcription Factor, MSRB, CGI-131, Mmethionine Sulfoxide Reductase B2, Methionine-R-Sulfoxide Reductase B2 Mitochondrial, MGC26104, MsrB2. EC 1.8.4.
Product # :
ENZ-036Price :
Quantity :
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Shipped with Ice Packs
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Description
MSRB2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (21-182a.a.) and having a molecular mass of 19.5kDa.MSRB2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MSRB2 protein solution (1mg/1ml) is formulated in In 20 mM Tris-HCl Buffer (pH 7.5), 1 mM DTT, 0.1 mM PMSF and 10% Glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MSRB2 is a member of the methionine sulfoxide reductases(MSRs) family which are antioxidant repair enzymes. MSRB2 protein catalyzes the decrease of free and protein-bound methionine sulfoxide to methionine. MSRB2 has a part in protecting against oxidative stress in numerous organs.
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Synonyms
CBS-1, PILB, Pilin-like Transcription Factor, MSRB, CGI-131, Mmethionine Sulfoxide Reductase B2, Methionine-R-Sulfoxide Reductase B2 Mitochondrial, MGC26104, MsrB2. EC 1.8.4.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVRGQAGGGG PGTGPGLGEA GSLATCELPL AKSEWQKKLT PEQFYVTREK GTEPPFSGIY LNNKEAGMYH CVCCDSPLFS SEKKYCSGTG WPSFSEAHGT SGSDESHTGI LRRLDTSLGS ARTEVVCKQC EAHLGHVFPD GPGPNGQRFC INSVALKFKP RKH
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 :
BDNF Human, HisDescription:
Brain-Derived Neurotrophic Factor Human Recombinant, His Tag
Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.
Product # :
CYT-881Price :
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Shipped with Ice Packs
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- sds-page
Description
BDNF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (129-247 a.a) and having a molecular mass of 15.8kDa. BDNF is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BDNF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
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Synonyms
Brain-Derived Neurotrophic Factor, Neurotrophin, Abrineurin, ANON2, BULN2, Brain-derived neurotrophic factor.
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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 MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 15.8kDa.
What is the source or expression system of BDNF Protein?
Escherichia Coli.
What is the Purity of BDNF Protein?
BDNF Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
The biological functionality of BDNF Protein will be determined in the future.
What is the amino acid sequence of BDNF Protein?
MGSSHHHHHH SSGLVPRGSH MHSDPARRGE 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.
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 :
ARL1 HumanDescription:
ADP-Ribosylation Factor-Like 1 Human Recombinant
ARFL1.
Product # :
PRO-508Price :
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Description
ARL1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.5 kDa. The ARL1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARL1 solution (0.25mg/ml) containing 20mM Tris-HCl pH-8, 2mM DTT, 100mM NaCl and 40% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ARL1 is part of the ARL (ADP-ribosylation factor-like) family of proteins, which are structurally associated to ADP-ribosylation factors (ARFs). ARFs, described as activators of cholera toxin (CT) ADP-ribosyltransferase activity, control intracellular vesicular membrane trafficking, and stimulate a phospholipase D (PLD) isoform.
ARL1 is a weak stimulator of PLD and CT in a phospholipid dependent manner.
ARL1 is a GTP-binding protein that has low efficiency as allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARL1 is involved in the Golgi apparatus. -
Synonyms
ARFL1.
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Physical Appearance
Sterile filtered colorless solution.
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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 MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI LVVFANKQDM EQAMTSSEMA NSLGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR Q.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OPG Human, Hi-5Description:
Osteoprotegerin Human Recombinant, Hi-5
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
Product # :
CYT-633Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant Osteoprotegerin produced in baculovirus is a signle, glycosylated polypeptide chain containing 389 amino acid residues (22-401 a.a.), having a calculated molecular mass of 44.7 kDa. The Osteoprotegerin is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Hi-5.
Formulation
Osteoprotegerin protein contains PBS pH-7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 8 ng/ml and is measured by its ability to inhibit cytotoxicity using Jurkat human acute T cell leukemia cells in the presence of 2ng/ml of human TRAIL (CAT# cyt-1014).
More Info
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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
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Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
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Physical Appearance
Sterile Filtered colorless clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
ADPETFPPKY LHYDEETSHQ LLCDKCPPGT YLKQHCTAKW KTVCAPCPDH YYTDSWHTSD ECLYCSPVCK ELQYVKQECN RTHNRVCECK EGRYLEIEFC LKHRSCPPGF GVVQAGTPER NTVCKRCPDG FFSNETSSKA PCRKHTNCSV FGLLLTQKGN ATHDNICSGN SESTQKCGID VTLCEEAFFR FAVPTKFTPN WLSVLVDNLP GTKVNAESVE RIKRQHSSQE QTFQLLKLWK HQNKDQDIVK KIIQDIDLCE NSVQRHIGHA NLTFEQLRSL MESLPGKKVG AEDIEKTIKA CKPSDQILKL LSLWRIKNGD QDTLKGLMHA LKHSKTYHFP KTVTQSLKKT IRFLHSFTMY KLYQKLFLEM IGNQVQSVKI SCLSHHHHHH.
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 SalamanderDescription:
Leptin Salamander Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
Product # :
CYT-704Price :
Quantity :
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Shipped at Room temp
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Description
Leptin Salamander Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of 16kDa. The Salamander Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Salamander Leptin was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
By inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity in that test is similar to that of mouse leptin.
More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized recombinant salamander leptin although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of recombinant salamander leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization recombinant salamander leptin can be stored at +4C for at least two weeks.
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Solubility
It is recommended to reconstitute the lyophilized Salamander Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the ten N-terminal amino acids was determined and was found to be Ala-Ile-Met-Val-Asp-Gln-Leu-Arg-Met-Asp.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.104 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).
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 :
IGFBP5 HumanDescription:
Insulin-Like Growth Factor Binding Protein-5 Human Recombinant
IGFBP-5, IBP-5, IGF-binding protein 5.
Product # :
CYT-464Price :
Quantity :
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Shipped at Room temp
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Description
IGFBP5 Human Recombinant produced in E.Coli is non-glycosylated homodimer containing 2x252 amino acids and having a molecular mass of 28.6kDa. IGFBP5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IBP-5 was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium Citrate pH-3.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by its ability to inhibit IGF-II induced proliferation of MCF-7. The expected ED50 for this effect is < 0.4µg/ml, corresponding to a specific activity of > 2500 IU/mg in the presence of 15ng/ml of rHuIGF-II.More Info
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Introduction
IGFBP5 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
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Synonyms
IGFBP-5, IBP-5, IGF-binding protein 5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IBP5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP 5 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 Insulin-Like Growth Factor Binding Protein-5 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
LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE.
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Background
What is the molecular weight/Mw of IGFBP5 HUMAN Protein?
IGFBP5 HUMAN Protein has a total Mw of 28.6kDa.
What is the source or expression system of IGFBP5 HUMAN Protein?
Escherichia Coli.
What is the Purity of IGFBP5 HUMAN Protein?
IGFBP5 HUMAN Protein is >96% pure as determined by SDS-PAGE.
What is the Biological Activity of IGFBP5 HUMAN Protein?
The ED50, calculated by its ability to inhibit IGF-II induced proliferation of MCF-7. The expected ED50 for this effect is < 0.4µg/ml, corresponding to a specific activity of > 2500 IU/mg in the presence of 15ng/ml of rHuIGF-II.
What is the amino acid sequence of IGFBP5 HUMAN Protein?
LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE.
What applications can IGFBP5 HUMAN Protein be used in?
IGFBP5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGFBP5 HUMAN Protein?
The endotoxin level is minimal, IGFBP5 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Leptin PorcineDescription:
Leptin Porcine Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-503Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Porcine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and additional Ala at N-terminus, having a molecular mass of 16kDa. The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized recombinant porcine leptin in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Trp.
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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 0.57 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Porcine 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 :
TWF1 HumanDescription:
Twinfilin-1 Human Recombinant
Twinfilin-1, Protein A6, Protein tyrosine kinase 9, TWF1, PTK9.
Product # :
PRO-1003Price :
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Shipped with Ice Packs
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Description
TWF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-252 a.a.) and having a molecular mass of 31.5kDa. TWF1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
TWF1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Twinfilin (TWF1) is a ubiquitous actin-monomer-binding protein which is composed of two ADF-homology domains. Twinfilin forms a 1:1 complex with ADP-actin-monomers, prevents nucleotide exchange on actin monomers and blocks assembly of the monomer into filaments. TWF1 is composed of 2 ADF/cofilin-like (ADF-H) domains joined by a short linker region and followed by a C-terminal tail of approximately 20 residues. The 2 ADF-H domains are approximately 20% homologous to ADF/cofilin and to each other. TWF1 protein may be an actin monomer-binding protein, and its localization to cortical G-actin-rich structures might be regulated by the small GTPase RAC1.
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Synonyms
Twinfilin-1, Protein A6, Protein tyrosine kinase 9, TWF1, PTK9.
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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 MGSHMMLYAA TRATLKKEFG GGHIKDEVFG TVKEDVSLHG YKKYLLSQSS PAPLTAAEEE LRQIKINEVQ TDVGVDTKHQ TLQGVAFPIS REAFQALEKL NNRQLNYVQL EIDIKNEIII LANTTNTELK DLPKRIPKDS ARYHFFLYKH SHEGDYLESI VFIYSMPGYT CSIRERMLYS SCKSRLLEIV ERQLQMDVIR KIEIDNGDEL TADFLYEEVH PKQHAHKQSF AKPKGPAGKR GIRRLIRGPA ETEATTD.
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 :
GSTP1 MouseDescription:
Glutathione S-Transferase pi 1 Mouse Recombinant
Glutathione S-transferase P 1, Gst P1, GST YF-YF, GST class-pi, GST-piB, Preadipocyte growth factor.
Product # :
ENZ-909Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GSTP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 26kDa. GSTP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GSTP1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 40 units/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.More Info
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Introduction
GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells. -
Synonyms
Glutathione S-transferase P 1, Gst P1, GST YF-YF, GST class-pi, GST-piB, Preadipocyte growth factor.
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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 MGSMPPYTIV YFPVRGRCEA MRMLLADQGQ SWKEEVVTID TWMQGLLKPT CLYGQLPKFE DGDLTLYQSN AILRHLGRSL GLYGKNQREA AQMDMVNDGV EDLRGKYVTL IYTNYENGKN DYVKALPGHL KPFETLLSQN QGGKAFIVGD QISFADYNLL DLLLIHQVLA PGCLDNFPLL SAYVARLSAR PKIKAFLSSP EHVNRPINGN GKQ.
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 :
ATP5F1 HumanDescription:
Synthase Transporting Mitochondrial Fo Complex B1 Human Recombinant
ATP Synthase Proton-Transporting Mitochondrial F(0) Complex Subunit B1, ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit B Isoform 1, ATPase Subunit B, ATP Synthase B Chain Mitochondrial, Cell Proliferation-Inducing Protein 47, PIG47.
Product # :
PRO-1839Price :
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Shipping Method :
Shipped with Ice Packs
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Description
ATP5F1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (83-256) and having a molecular mass of 22.6 kDa. ATP5F1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ATP5F1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
ATP5F1 is a mitochondrial ATP synthase subunit catalyzes ATP synthesis, using an electrochemical gradient of protons all through the inner membrane for the duration of the oxidative phosphorylation. ATP synthase is comprised of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, including the proton channel. The catalytic segment of mitochondrial ATP synthase contains 9 subunits: 3 alpha, 3 beta, and one unit of gamma, delta, and epsilon. The proton route is known to have 9 subunits (a, b, c, d, e, f, g, F6 and 8).
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Synonyms
ATP Synthase Proton-Transporting Mitochondrial F(0) Complex Subunit B1, ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit B Isoform 1, ATPase Subunit B, ATP Synthase B Chain Mitochondrial, Cell Proliferation-Inducing Protein 47, PIG47.
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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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLILYALS KEIYVISAET FTALSVLGVM VYGIKKYGPF VADFADKLNE QKLAQLEEAK QASIQHIQNA IDTEKSQQAL VQKRHYLFDV QRNNIAMALE VTYRERLYRV YKEVKNRLDY HISVQNMMRR KEQEHMINWV EKHVVQSIST QQEKETIAKC IADLKLLAKK AQAQPVM
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 :
HB-EGF MouseDescription:
HB-EGF Mouse Recombinant
DTR, HEGFL, diphtheria toxin receptor, DTSF.
Product # :
CYT-068Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- sds-page
Description
HB-EGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids (63-148 a.a.) and having a molecular mass of 9.8 kDa.The HB-EGF is purified by proprietary chromatographic techniques
Source
Escherichia Coli.
Formulation
The protein was filtered (0.2µm) and lyophilized from a concentrated solution containing 10mM PB and 500mM NaCl, pH7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.sds-page
More Info
-
Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
-
Synonyms
DTR, HEGFL, diphtheria toxin receptor, DTSF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Mouse HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF 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 Mouse HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
DLEGTDLNLF KVAFSSKPQG LATPSKERNG KKKKKGKGLG KKRDPCLRKY KDYCIHGECR YLQEFRTPSC KCLPGYHGHR CHGLTL.
-
Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.8kDa.
What is the source or expression system of HB-EGF Protein?
Escherichia Coli.
What is the Purity of HB-EGF Protein?
HB-EGF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of HB-EGF Protein?
The ED50 was determined by a cell proliferation assay using balb/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.
What is the amino acid sequence of HB-EGF Protein?
DLEGTDLNLF KVAFSSKPQG LATPSKERNG KKKKKGKGLG KKRDPCLRKY KDYCIHGECR YLQEFRTPSC KCLPGYHGHR CHGLTL.
What applications can HB-EGF Protein be used in?
HB-EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-EGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PPM1F AntibodyDescription:
Protein Phosphatase 1F, Mouse Anti Human
Protein phosphatase 1F, Ca(2+)/calmodulin-dependent protein kinase phosphatase, CaM-kinase phosphatase, CaMKPase, Partner of PIX 2, Protein fem-2 homolog, hFem-2, KIAA0015, POPX2, PPM1F, CAMKP, FEM-2.
Product # :
ANT-502Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Protein Phosphatase 1F (PPM1F) is a part of the PP2C family of Ser/Thr protein phosphatases whose members are known to be negative regulators of cell stress response pathways. PPM1F interacts with Rho guanine nucleotide exchange factors (PIX), and as a result blocks the effects of p21-activated kinase 1 (PAK), a protein kinase mediating biological effects downstream of Rho GTPases. Calcium/calmodulin-dependent protein kinase II gamma (CAMK2G/CAMK-II) is one of the substrates of PPM1F. PPM1F is found to be an apoptosis Promoter.
-
Synonyms
Protein phosphatase 1F, Ca(2+)/calmodulin-dependent protein kinase phosphatase, CaM-kinase phosphatase, CaMKPase, Partner of PIX 2, Protein fem-2 homolog, hFem-2, KIAA0015, POPX2, PPM1F, CAMKP, FEM-2.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human PPM1F mAb, clone PAT6D11AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PPM1F protein 1-454 amino acids purified from E. coli.
-
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
-
Clone
PAT6D11AT.
-
Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
PPM1F antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 :
FLT1 D5 HumanDescription:
Vascular Endothelial Growth Factor Receptor-1 D5 Human Recombinant
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Product # :
PKA-239Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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- biological activity
- More Info
Description
Soluble FLT1 D1-5 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 562 amino acids and having a molecular mass of 70 kDa. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
FLT1 D1-5 was lyophilized from a concentrated (1 mg/ml) sterile solution containing no additives.
Purity
Greater than 90.0% as determined by(a)Analysis by RP-HPLC.
(b)Analysis by SDS-PAGE.Biological Activity
The activity of FLT1 D5 was determined by its ability to abolish the binding of iodinated VEGF to solid surfaces or cell surfaces. The ED50 for this effect is typically 10 ng/ml, corresponding to a specific activity of 100,000IU/mg.
In a 13 day CAM-assay sVEGFR-1 is able to inhibit VEGF stimulated sprouting of capillaries at 30 pM.More Info
-
Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
-
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT1 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 FLT1 D5 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
C-JUN Human (241 a.a.)Description:
Jun Proto-Oncogene (1-241 a.a.) Human Recombinant
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
Product # :
PKA-001Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
C-JUN 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 261 amino acids (1-241 a.a.) and having a molecular mass of 27.3kDa. The C-JUN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The C-JUN solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.
-
Synonyms
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
-
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 MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP P.
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 :
IL-10 Human, Sf9Description:
Interleukin 10 Human Recombinant, Sf9, Active
Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.
Product # :
CYT-1147Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IL-10 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 166 amino acids (19-178 aa) and having a molecular mass of 19.4kDa. IL-10 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The IL-10 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using MC/9 mouse mast cells. The ED50 range < 5 ng/ml.
More Info
-
Introduction
Interleukin 10 or IL-10 or human cytokine synthesis inhibitory factor, is a cytokine (anti-inflammatory). IL10 gene is coding for il-10 In humans. Interleukin 10 has a receptor complex that is built from a couple of IL-10 receptor-1 and a couple of IL-10 receptor-2 proteins. therfore, the whole receptor unit consists of four IL-10 receptor molecules. IL-10 binds the receptor and causes STAT3 signalling through the phosphorylation of the cytoplasmic ends of IL-10 receptor 1 and IL-10 receptor 2 through JAK1 and Tyk2.
-
Synonyms
Interleukin-10, IL-10, Cytokine synthesis inhibitory factor, CSIF, IL10, GVHDS, IL10A, TGIF, T-Cell Growth Inhibitory Factor.
-
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
SPGQGTQSEN SCTHFPGNLP NMLRDLRDAF SRVKTFFQMK DQLDNLLLKE SLLEDFKGYL GCQALSEMIQ FYLEEVMPQA ENQDPDIKAH VNSLGENLKT LRLRLRRCHR FLPCENKSKA VEQVKNAFNK LQEKGIYKAM SEFDIFINYI EAYMTMKIRN HHHHHH.
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 :
TCF4 Human, sf9Description:
Transcription Factor 4 Human Recombinant, sf9
Transcription Factor 4, Class B Basic Helix-Loop-Helix Protein 19, Immunoglobulin Transcription Factor 2, SL3-3 Enhancer Factor 2, BHLHb19, ITF-2, SEF-2, TCF-4, ITF2, SEF2, SEF2-1A, SEF2-1B, SEF2-1D, SEF2-1, FECD3, E2-2, PTHS.
Product # :
PRO-2354Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TCF4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 513 amino acids (1-507a.a.) and having a molecular mass of 54.9kDa (Molecular size on SDS-PAGE will appear at approximately 35-100kDa). TCF4 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TCF4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Transcription Factor 4 (TCF4) acts as a transcription factor and takes part in the initiation of neuronal differentiation. TCF4 recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a motif primary identified in immunoglobulin enhancers. TCF4 is mainly expressed in pre-B-cells, even though it is present in other tissues as well.
-
Synonyms
Transcription Factor 4, Class B Basic Helix-Loop-Helix Protein 19, Immunoglobulin Transcription Factor 2, SL3-3 Enhancer Factor 2, BHLHb19, ITF-2, SEF-2, TCF-4, ITF2, SEF2, SEF2-1A, SEF2-1B, SEF2-1D, SEF2-1, FECD3, E2-2, PTHS.
-
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
MKFKQCRCSD TGLCCLDHEG KAEVYAPSAS TADYNRDSPG YPSSKPATST FPSSFFMQDG HHSSDPWSSS SGMNQPGYAG MLGNSSHIPQ SSSYCSLHPH ERLSYPSHSS ADINSSLPPM STFHRSGTNH YSTSSCTPPA NGTDSIMANR GSGAAGSSQT GDALGKALAS IYSPDHTNNS FSSNPSTPVG SPPSLSAGTA VWSRNGGQAS SSPNYEGPLH SLQSRIEDRL ERLDDAIHVL RNHAVGPSTA MPGGHGDMHG IIGPSHNGAM GGLGSGYGTG LLSANRHSLM VGTHREDGVA LRGSHSLLPN QVPVPQLPVQ SATSPDLNPP QDPYRGMPPG LQGQSVSSGS SEIKSDDEGD ENLQDTKSSE DKKLDDDKKD IKSITSNNDD EDLTPEQKAE REKERRMANN ARERLRVRDI NEAFKELGRM VQLHLKSDKP QTKLLILHQA VAVILSLEQQ VRERNLNPKA ACLKRREEEK VSSEPPPLSL AGPHPGMGDA SNHMGQMHHH HHH.
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 :
Eptifibatide HumanDescription:
Eptifibatide Human
Product # :
PRO-358Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Synthetic Eptifibatide is a 6 amino acid peptide having a MW of 832.5 Dalton the following sequence Mpr-Har-Gly-Asp-Trp-Pro-Cys-NH2.
Formulation
Eptifibatide 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
-
Introduction
Eptifibatide binds to the platelet receptor glycoprotein (GP) IIb/IIIa of human platelets and inhibits platelet aggregation. Eptifibatide is a cyclic peptide derived from a protein discovered in the venom of the southeastern pygmy rattlesnake (Sistrurus miliarus barbouri). Eptifibatide belongs to the arginin-glycin-aspartat-mimetics and reversibly binds to platelets.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Eptifibatide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Eptifibatide 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 Eptifibatide in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
EFNA1 Human, HEKDescription:
Ephrin A1 Human Recombinant, HEK
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
Product # :
PRO-2477Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
EFNA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-182) containing 170 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 20.2kDa (calculated).
Source
HEK293 cells.
Formulation
EFNA1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline, pH 7.5 containing 5 % (w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
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Synonyms
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein 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 one week at 4°C.
-
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. EFNA1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
DRHTVFWNSS NPKFRNEDYT IHVQLNDYVD IICPHYEDHS VADAAMEQYI LYLVEHEEYQ LCQPQSKDQV RWQCNRPSAK HGPEKLSEKF QRFTPFTLGK EFKEGHSYYY ISKPIHQHED RCLRLKVTVS GKITHSPQAH DNPQEKRLAA DDPEVRVLHS IGHS HHHHHH.
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 :
ARL4A HumanDescription:
ADP-Ribosylation Factor-Like 4A Human Recombinant
ADP-ribosylation factor-like protein 4A, ARL4A.
Product # :
PRO-895Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ARL4A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200) and having a molecular mass of 24.7 kDa.The ARL4A is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ARL4A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
ARL4A is related Specifically to ARL6 and ARL7 and belongs to the ARF-like protein (ARL) subfamily of small GTPases. However, unlike ARFs, ARL4 does not activate the cholera toxin ADP-ribosyltranferase. ARL4A takes part in neurogenesis during embryonic development and somitogenesis in the early stages of adult spermatogenesis.
-
Synonyms
ADP-ribosylation factor-like protein 4A, ARL4A.
-
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 MGNGLSDQTS ILSNLPSFQS FHIVILGLDC AGKTTVLYRL QFNEFVNTVP TKGFNTEKIK VTLGNSKTVT FHFWDVGGQE KLRPLWKSYT RCTDGIVFVV DSVDVERMEE AKTELHKITR ISENQGVPVL IVANKQDLRN SLSLSEIEKL LAMGELSSST PWHLQPTCAI IGDGLKEGLE KLHDMIIKRR KMLRQQKKKR
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 :
GH ChickenDescription:
GH Chicken Recombinant
GH1, GH, GHN, GH-N, hGH-N,Pituitary GH, GH 1,
Product # :
CYT-430Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GH Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids with an additional Ala at its N-terminus and having a molecular mass of 22255 Dalton. GH Chicken recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.3% NaHCO3 adjusted to pH 8.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SDS-PAGE gel.
(b) Analysis by SEC-HPLC.Biological Activity
GH Chicken Recombinantis fully biologically active in homologous assays and in PDF-P1 3B9 cells stably transfected with rabbit GH receptors.More Info
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Introduction
GH is a member of the prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the GH locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five GHs, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the GH locus. Mutations in or deletions of the gene lead to GH deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary GH, GH 1,
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GH Chicken although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and filter sterilization GH can be stored at 4°C for several weeks. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is recommended.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized GH Chicken Recombinant in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml and not more than 3 mg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Phe-Pro-Ala.
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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 0.75 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). 2. Analysis by RP-HPLC, using a calibrated solution of GH 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 :
IL 9 MouseDescription:
Interleukin-9 Mouse Recombinant
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
Product # :
CYT-373Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
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Description
Interleukin-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa. The IL-9 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution 10mM Na2PO4, pH 7.5.
Purity
Greater than 96.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependant stimulation of human MO7e cells is < 0.5 ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.More Info
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Introduction
Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
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Synonyms
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin 9 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
MQRCSTTWGI RDTNYLIENL KDDPPSKCSC SGNVTSCLCL SVPTDDCTTP CYREGLLQLT NATQKSRLLP VFHRVKRIVE VLKNITCPSF SCEKPCNQTM AGNTMSFLKS LLGTFQKTEM QRQKSRP.
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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 0.6 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 standard solution of IL-9 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 :
CTF1 HumanDescription:
Cardiotrophin-1 Human Recombinant
CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.
Product # :
CYT-944Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Cardiotrophin-1 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 201 amino acids and having a molecular mass of 21.2kDa.The CTF1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CTF-1 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 IU/mg.More Info
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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction. -
Synonyms
CTF1, CT1, CT-1, Cardiophin 1, Cardiotrophin-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CTF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF-1 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 CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.
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Background
Title: Cardiotrophin-1 Human Recombinant: A Potential Therapeutic Target for Cardiovascular Diseases
Abstract:
Cardiotrophin-1 (CT-1) is a cytokine that plays a crucial role in cardiac development and homeostasis. This research paper provides a comprehensive analysis of human recombinant CT-1, focusing on its production, characterization, and potential therapeutic implications in cardiovascular diseases. The paper discusses the significance of CT-1 in cardiac cell survival, hypertrophy, and regeneration. Furthermore, it elucidates the ongoing research and clinical trials exploring the therapeutic potential of recombinant CT-1 in cardiovascular disorders. The information presented in this paper aims to enhance the understanding of human recombinant CT-1 and its utility as a research tool and a potential therapeutic agent for cardiovascular diseases.Introduction:
Cardiotrophin-1 (CT-1) is a member of the interleukin-6 cytokine family, primarily produced by cardiac cells. It exerts its effects by binding to the CT-1 receptor complex, leading to the activation of various signaling pathways. Human recombinant CT-1, produced through genetic engineering techniques, provides researchers with a valuable tool to explore its biological functions and therapeutic potential.Production and Characterization:
Recombinant CT-1 is typically produced using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CT-1.Role in Cardiovascular Physiology:
CT-1 plays a critical role in cardiac cell survival, hypertrophy, and regeneration. It promotes cardiomyocyte growth and survival, contributing to the adaptation of the heart to stress and injury. CT-1 also exhibits angiogenic properties, stimulating the formation of new blood vessels in the heart. These functions make recombinant CT-1 an important tool for studying cardiac physiology and exploring potential therapeutic interventions.Therapeutic Implications:
The dysregulation of CT-1 signaling has been implicated in various cardiovascular diseases, including heart failure, myocardial infarction, and cardiac hypertrophy. Recombinant CT-1 holds promise as a potential therapeutic agent for these conditions. Clinical trials are underway to evaluate the safety and efficacy of CT-1-based therapies, including recombinant CT-1 administration and gene therapy approaches.Conclusion:
Human recombinant CT-1 is a valuable research tool and a potential therapeutic target for cardiovascular diseases. Its production, characterization, and applications in cardiac cell signaling contribute to our understanding of cardiovascular physiology and the development of novel treatments. Continued research and clinical trials exploring the therapeutic potential of recombinant CT-1 hold promise for improving outcomes in patients with cardiovascular disorders.What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.2kDa.
What is the source or expression system of CTF1 Protein?
Escherichia Coli.
What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF1 Protein?
The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0×106 IU/mg.
What is the amino acid sequence of CTF1 Protein?
MSRREGSLED PQTDSSVSLL PHLEAKIRQT HSLAHLLTKY AEQLLQEYVQ LQGDPFGLPS FSPPRLPVAG LSAPAPSHAG LPVHERLRLD AAALAALPPL LDAVCRRQAE LNPRAPRLLR RLEDAARQAR ALGAAVEALL AALGAANRGP RAEPPAATAS AASATGVFPA KVLGLRVCGL YREWLSRTEG DLGQLLPGGS A.
What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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 :
MMP 3 HumanDescription:
Matrix Metalloproteinase-3 Human Recombinant
CHDS6, MMP-3, SL-1, STMY, STMY1, STR1, Stromelysin-1, Matrix metalloproteinase-3, Transin-1, MMP3.
Product # :
ENZ-774Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
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Description
MMP 3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (100-477a.a) and having a molecular mass of 45.2kDa. MMP 3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP 3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.
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Synonyms
CHDS6, MMP-3, SL-1, STMY, STMY1, STR1, Stromelysin-1, Matrix metalloproteinase-3, Transin-1, MMP3.
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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 MGSFRTFPGI PKWRKTHLTY RIVNYTPDLP KDAVDSAVEK ALKVWEEVTP LTFSRLYEGE ADIMISFAVR EHGDFYPFDG PGNVLAHAYA PGPGINGDAH FDDDEQWTKD TTGTNLFLVA AHEIGHSLGL FHSANTEALM YPLYHSLTDL TRFRLSQDDI NGIQSLYGPP PDSPETPLVP TEPVPPEPGT PANCDPALSF DAVSTLRGEI LIFKDRHFWR KSLRKLEPEL HLISSFWPSL PSGVDAAYEV TSKDLVFIFK GNQFWAIRGN EVRAGYPRGI HTLGFPPTVR KIDAAISDKE KNKTYFFVED KYWRFDEKRN SMEPGFPKQI AEDFPGIDSK IDAVFEEFGF FYFFTGSSQL EFDPNAKKVT HTLKSNSWLN C.
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 :
AIF1L HumanDescription:
Allograft Inflammatory Factor 1 Like Human Recombinant
Allograft Inflammatory Factor 1-like, IBA2, FLJ12783, Ionized calcium-binding adapter molecule 2, C9orf58, chromosome 9 open reading frame 58, MGC29466.
Product # :
CYT-007Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
AIF1L produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150a.a.) and having a molecular mass of 19.2kDa.AIF1L is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AIF1L protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 0.1mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
sds-page
More Info
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Synonyms
Allograft Inflammatory Factor 1-like, IBA2, FLJ12783, Ionized calcium-binding adapter molecule 2, C9orf58, chromosome 9 open reading frame 58, MGC29466.
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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 MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP.
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Background
Allograft Inflammatory Factor 1-Like Human Recombinant: Investigating its Role in Immune Responses and Potential Therapeutic Applications
1. Abstract
This paper seeks to provide an in-depth overview of Allograft Inflammatory Factor 1-Like Human Recombinant (AIF-1L), a significant protein involved in the regulation of inflammatory responses. By delving into the structure, biological functions, and pathological implications of AIF-1L, we attempt to shed light on its potential as a therapeutic target in immune-mediated disorders.
2. Introduction
AIF-1L belongs to the allograft inflammatory factor protein family and is implicated in immune responses. With its intricate interaction with a multitude of immune cells and involvement in various inflammatory and immune-related diseases, it serves as a pivotal point of interest for therapeutic intervention research.
3. Structure and Signaling of AIF-1L
AIF-1L shares a conserved EF-hand calcium-binding motif with its counterpart AIF-1, suggesting similar calcium-dependent activities. While its signaling pathway remains largely elusive, the protein is believed to modulate macrophage activation, an integral part of immune response regulation.
4. Biological Functions of AIF-1L
AIF-1L is fundamentally involved in immune response modulation, especially in the context of macrophage activation. It plays key roles in managing inflammation, cell proliferation, survival, and differentiation.
5. AIF-1L in Disease Pathology
AIF-1L is linked with a range of inflammatory and immune-related disorders, including but not limited to rheumatoid arthritis, atherosclerosis, and certain cancers. This association underscores its profound physiological relevance and potential as a therapeutic target.
6. Therapeutic Potential of AIF-1L
Given its central role in immune responses, AIF-1L presents a promising target for therapeutic strategies. Manipulating AIF-1L activity could pave the way for novel treatments of various inflammatory and immune-mediated diseases.
7. Conclusion and Future Perspectives
Though our comprehension of AIF-1L has made significant strides, there is still much terrain left to explore. Future research directed at the precise molecular mechanisms and pathological roles of AIF-1L will undoubtedly contribute to the development of novel therapeutic strategies.
What is the molecular weight/Mw of AIF1L Protein?
AIF1L Protein has a total Mw of 19.2kDa.
What is the source or expression system of AIF1L Protein?
Escherichia Coli.
What is the Purity of AIF1L Protein?
AIF1L Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of AIF1L Protein?
The biological functionality of AIF1L Protein will be determined in the future.
What is the amino acid sequence of AIF1L Protein?
MGSSHHHHHH SSGLVPRGSH MSGELSNRFQ GGKAFGLLKA RQERRLAEIN REFLCDQKYS DEENLPEKLT AFKEKYMEFD LNNEGEIDLM SLKRMMEKLG VPKTHLEMKK MISEVTGGVS DTISYRDFVN MMLGKRSAVL KLVMMFEGKA NESSPKPVGP PPERDIASLP.
What applications can AIF1L Protein be used in?
AIF1L Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for AIF1L Protein?
The endotoxin level is minimal, AIF1L 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.