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1000 results found for “Gluteradoxin”
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Name :
Leptin tA HumanDescription:
Leptin Antagonist Triple Mutant Human Recombinant
Product # :
CYT-352Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GLOD4 HumanDescription:
Glyoxalase Domain Containing 4 Human Recombinant
Glyoxalase domain containing protein 4, HC71, C17orf25, CGI-150, Chromosome 17 open reading frame 25.
Product # :
PRO-894Price :
Quantity :
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Shipped with Ice Packs
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Description
GLOD4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298) and having a molecular mass of 35.3 kDa.The GLOD4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GLOD4 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GLOD4 is a part of the glyoxalase system which is a group of enzymes that is in charge of the detoxification of methylglyoxal and other reactive aldehydes that are usually produced in metabolism. The mitochondrial protein GLOD4 is known to interact with NUDT9.
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Synonyms
Glyoxalase domain containing protein 4, HC71, C17orf25, CGI-150, Chromosome 17 open reading frame 25.
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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 MAARRALHFV FKVGNRFQTA RFYRDVLGMK VLRHEEFEEG CKAACNGPYD GKWSKTMVGF GPEDDHFVAE LTYNYGVGDY KLGNDFMGIT LASSQAVSNA RKLEWPLTEV AEGVFETEAP GGYKFYLQNR SLPQSDPVLK VTLAVSDLQK SLNYWCNLLG MKIYEKDEEK QRALLGYADN QCKLELQGVK GGVDHAAAFG RIAFSCPQKE LPDLEDLMKR ENQKILTPLV SLDTPGKATV QVVILADPDG HEICFVGDEA FRELSKMDPE GSKLLDDAMA ADKSDEWFAK HNKPKASG
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 :
GFPT1 HumanDescription:
Glutamine--Fructose-6-Phosphate Transaminase 1 Human Recombinant
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1, D-fructose-6-phosphate amidotransferase 1, Glutamine:fructose-6-phosphate amidotransferase 1, GFAT 1, GFAT1, Hexosephosphate aminotransferase 1, GFPT1, GFAT, GFPT, CMSTA1, GFA, GFAT1m, GFPT1L, MSLG, Glutamine--Fructose-6-Phosphate Transaminase 1.
Product # :
ENZ-818Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GFPT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (332-699 a.a) and having a molecular mass of 43.7kDa.GFPT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GFPT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Glutamine--Fructose-6-Phosphate Transaminase 1 (GFPT1) participates in the hexosamine pathway and controls the glucose fluidity into the hexosamine pathway. GFPT1 regulates the availability of precursors for N- and O-linked glycosylation of proteins. GFPT1 controls the circadian expression of clock genes ARNTL/BMAL1 and CRY1.
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Synonyms
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1, D-fructose-6-phosphate amidotransferase 1, Glutamine:fructose-6-phosphate amidotransferase 1, GFAT 1, GFAT1, Hexosephosphate aminotransferase 1, GFPT1, GFAT, GFPT, CMSTA1, GFA, GFAT1m, GFPT1L, MSLG, Glutamine--Fructose-6-Phosphate Transaminase 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQQIMKGN FSSFMQKEIF EQPESVVNTM RGRVNFDDYT VNLGGLKDHI KEIQRCRRLI LIACGTSYHA GVATRQVLEE LTELPVMVEL ASDFLDRNTP VFRDDVCFFL SQSGETADTL MGLRYCKERG ALTVGITNTV GSSISRETDC GVHINAGPEI GVASTKAYTS QFVSLVMFAL MMCDDRISMQ ERRKEIMLGL KRLPDLIKEV LSMDDEIQKL ATELYHQKSV LIMGRGYHYA TCLEGALKIK EITYMHSEGI LAGELKHGPL ALVDKLMPVI MIIMRDHTYA KCQNALQQVV ARQGRPVVIC DKEDTETIKN TKRTIKVPHS VDCLQGILSV IPLQLLAFHL AVLRGYDVDF PRNLAKSVTV E.
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 :
GDF11 HumanDescription:
Growth and Differentiation factor 11 Human Recombinant
Growth Differentiation Factor 11, GDF-11, Bone Morphogenetic Protein 11, BMP11.
Product # :
CYT-402Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GDF11 Human Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2x109 amino acids and having a total molecular mass of 25kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, determined by the ability to inhibit alkaline phosphatase activity in ATDC5 cells, is typically less than 1 ng/mL. This corresponds to a specific activity of 1x106 units/mg.Citations
More Info
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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
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Synonyms
Growth Differentiation Factor 11, GDF-11, Bone Morphogenetic Protein 11, BMP11.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF11 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 GDF11 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
NLGLDCDEHS SESRCCRYPL TVDFEAFGWD WIIAPKRYKA NYCSGQCEYM FMQKYPHTHLVQQANPRGSA GPCCTPTKMS PINMLYFNDK QQIIYGKIPG MVVDRCGCS
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Background
What is the molecular weight/Mw of GDF11 HUMAN Protein?
GDF11 HUMAN Protein has a total Mw of 25kDa.
What is the source or expression system of GDF11 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF11 HUMAN Protein?
GDF11 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF11 HUMAN Protein?
The ED50, determined by the ability to inhibit alkaline phosphatase activity in ATDC5 cells, is typically less than 1 ng/mL. This corresponds to a specific activity of 1x106 units/mg.
What is the amino acid sequence of GDF11 HUMAN Protein?
NLGLDCDEHS SESRCCRYPL TVDFEAFGWD WIIAPKRYKA NYCSGQCEYM FMQKYPHTHL
VQQANPRGSA GPCCTPTKMS PINMLYFNDK QQIIYGKIPG MVVDRCGCS.
What applications can GDF11 HUMAN Protein be used in?
GDF11 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF11 HUMAN Protein?
The endotoxin level is minimal, GDF11 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 :
GDF11 Human, HisDescription:
Growth and Differentiation factor 11 Human Recombinant, His Tag
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
Product # :
CYT-887Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa. GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF11 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
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Synonyms
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
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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 MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
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Background
What is the molecular weight/Mw of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein has a total Mw of 14.8kDa.
What is the source or expression system of GDF11 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF11 HUMAN, HIS Protein?
The biological functionality of GDF11 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of GDF11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
What applications can GDF11 HUMAN, HIS Protein be used in?
GDF11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF11 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF11 HUMAN, HIS 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 :
GDF15 D HumanDescription:
Growth and Differentiation Factor 15 D-Variant Human Recombinant
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Product # :
CYT-314Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GDF15 D-variant (His substitutes Asp at position 7) Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.5kDa. The GDF15 D-variant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF15 D-variant is lyophilized without additives.
Purity
Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
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Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF15 D-variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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 GDF15 D-variant in sterile 5mM AcOH (acetic Acid) at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MARNGDDCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
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Background
What is the molecular weight/Mw of GDF15 D HUMAN Protein?
GDF15 D HUMAN Protein has a total Mw of 24.5kDa.
What is the source or expression system of GDF15 D HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF15 D HUMAN Protein?
GDF15 D HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 D HUMAN Protein?
The biological functionality of GDF15 D HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF15 D HUMAN Protein?
MARNGDDCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
What applications can GDF15 D HUMAN Protein be used in?
GDF15 D HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF15 D HUMAN Protein?
The endotoxin level is minimal, GDF15 D 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 :
HBsAg adwDescription:
Hepatitis B Surface Antigen, adw Recombinant
Product # :
HBS-872Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.
Source
Pichia Pastoris.
Formulation
Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.
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Physical Appearance
Sterile Filtered pale solution.
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Stability
HBsAg Should be stored at 4°C.DO NOT FREEZE.
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 :
Adiponectin Mouse, TrimericDescription:
Adiponectin Mouse Recombinant, Trimeric form
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-247Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.
Source
HEK293 (Human embryonic kidney cell line).
Formulation
Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.
Purity
Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered white lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse 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
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GDA Human, ActiveDescription:
Guanine Deaminase Human Recombinant, Active
Guanine Deaminase, Guanine Aminohydrolase, Guanine Aminase, P51-Nedasin, EC 3.5.4.3, GUANASE, GAH, Cytoplasmic PSD95 Interactor, KIAA1258, NEDASIN, CYPIN.
Product # :
ENZ-982Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GDA Human Recombinant produced in E. coli is a single polypeptide chain containing 477 amino acids (1-454) and having a molecular mass of 53kDa.GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol, 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,000 pmol/min/ug, and is defined as the amount of enzyme that convert guanine to xanthine per minute at pH 8.0 at 37C.Citations
More Info
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Introduction
GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.
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Synonyms
Guanine Deaminase, Guanine Aminohydrolase, Guanine Aminase, P51-Nedasin, EC 3.5.4.3, GUANASE, GAH, Cytoplasmic PSD95 Interactor, KIAA1258, NEDASIN, CYPIN.
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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 MGSMCAAQMP PLAHIFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE ASQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHASQ YSFAGSSIDL PLLEWLTKYT FPAEHRFQNI DFAEEVYTRV VRRTLKNGTT TACYFATIHT DSSLLLADIT DKFGQRAFVG KVCMDLNDTF PEYKETTEES IKETERFVSE MLQKNYSRVK PIVTPRFSLS CSETLMGELG NIAKTRDLHI QSHISENRDE VEAVKNLYPS YKNYTSVYDK NNLLTNKTVM AHGCYLSAEE LNVFHERGAS IAHCPNSNLS LSSGFLNVLE VLKHEVKIGL GTDVAGGYSY SMLDAIRRAV MVSNILLINK VNEKSLTLKE VFRLATLGGS QALGLDGEIG NFEVGKEFDA ILINPKASDS PIDLFYGDFF GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.
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 :
Chitinase ProteinDescription:
Chitinase Clostridium Paraputrificum Recombinant
Product # :
ENZ-031Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Chitinase Clostridium Paraputrificum Recombinant fused with a His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 582 amino acids and having a molecular mass of 64.2kDa. The Chitinase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Chitinase lyophilized from a 0.2µm filtered concentrated solution in PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Chitinase is a digestive enzyme which breaks down glycosidic bonds in chitin. Due to chitin being a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are usually found in organisms that either need to remake their own chitin or to dissolve and digest the chitin of fungi or animals. Chitinivorous organisms include many bacteria genuses such as Aeromonas, Bacillus, Vibrio, among others, which may be pathogenic or detritivorous. Chitinase expression is mediated by the NPR1 gene and the salicylic acid pathway, both of which are involved in resisting fungal and insect attack. Human chitinases appear in gastric juices. They are likely to be digestive chitinases, for catabolic activity. Chitinase activity is identified systemically in humans, in the blood, and possibly cartilage. Chitinase has been related to allergies, asthma in particular has been linked to enhanced chitinase expression levels, also dust mites and mold spores which are both chitin covered.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Chitinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Chitinase 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 Chitinase 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
MRGSGSHHHH HHMYYGDWSI WGGQGNFYPK DIPADKLTHL NFAFMDFNSS GELIYCDKDA AIGHPLGNLG VTYGDVNGGI LNAFQVLKSE NPNLKIGVSL GGWSKSGDFS TIAATPSIRA KFVENVMKFI KYTNMDFVDI DWEYPGDYRE PDKTDNINDE GTPNASAGDK ENYILLLQDL KEALNKQGKE LGKVYELSVA LPAGVSKIEK GIDVDKLFNI VDFANIMTYD MAGAWSTTSG HQTALYTNPN APEEYKGLSV DESVKYYISQ GAEREKIVVG AAYYTRGWEQ VSDKGTDPNN PGLFGEAAVV NKDADLSPTP GALNEAPMKN GEGGRAGGVW GYNALDKLKS KYTGLKEYWD DSAKAPYLYN SETGAFFTYD NIRSIQEKAK YVKENNLGGI IGWMASQDAT TNSTKRDELT TATKESLFGK EDLPKYEIKY TENDITCTVT PVKQSWGSGG VLKMSITNNE KLDESGEVLS TVETSAKTVK NMKVYIKTDG IAITGSQYPA GPVTKEGDYY VIDFGKISDG KLMKAGITFT FDLNLDKAIE DTNNIISIEV SQRMYQTSPE FNRQTIWENT NS.
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 :
QPCT HumanDescription:
Glutaminyl-Peptide Cyclotransferase Human Recombinant
Glutaminyl-Peptide Cyclotransferase, Glutaminyl Cyclase, QC, Glutaminyl-TRNA Cyclotransferase, Glutamyl Cyclase, EC 2.3.2.5, SQC, EC, GCT, Glutaminyl-peptide cyclotransferase.
Product # :
ENZ-912Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
QPCT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 339 amino acids (29-361a.a.) and having a molecular mass of 38.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). QPCT is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
QPCT protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Glutaminyl-Peptide Cyclotransferase, also known as QPCT is a member of the glutaminyl-peptide cyclotransferase family. QPCT is responsible for the biosynthesis of pyroglutamyl peptides. Furthermore, QPCT is partial against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length following the second residue. QPCT catalyzes N-terminal pyroglutamate formation, also in vitro, it catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid.
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Synonyms
Glutaminyl-Peptide Cyclotransferase, Glutaminyl Cyclase, QC, Glutaminyl-TRNA Cyclotransferase, Glutamyl Cyclase, EC 2.3.2.5, SQC, EC, GCT, Glutaminyl-peptide cyclotransferase.
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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
VSPSASAWPE EKNYHQPAIL NSSALRQIAE GTSISEMWQN DLQPLLIERY PGSPGSYAAR QHIMQRIQRL QADWVLEIDT FLSQTPYGYR SFSNIISTLN PTAKRHLVLA CHYDSKYFSH WNNRVFVGAT DSAVPCAMML ELARALDKKL LSLKTVSDSK PDLSLQLIFF DGEEAFLHWS PQDSLYGSRH LAAKMASTPH PPGARGTSQL HGMDLLVLLD LIGAPNPTFP NFFPNSARWF ERLQAIEHEL HELGLLKDHS LEGRYFQNYS YGGVIQDDHI PFLRRGVPVL HLIPSPFPEV WHTMDDNEEN LDESTIDNLN KILQVFVLEY LHLHHHHHH.
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 :
Ganirelix peptideDescription:
Ganirelix
Product # :
HOR-276Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Ganirelix acetate is a synthetic decapeptide with high antagonistic activity against naturally occurring gonadotropin-releasing hormone (GnRH). Ganirelix acetate is derived from native GnRH with substitutions of amino acids at positions 1, 2, 3, 6, 8, and 10 to form the following molecular formula of the peptide: N-acetyl-3-(2-napthyl)-D-alanyl-4-chloro-D-phenylalanyl-3-(3-pyridyl)-D-alanyl-L-seryl-L-tyrosyl-N 9 ,N 10 -diethyl- D-homoarginyl-L-leucyl-N 9 ,N 10 -diethyl-L-homoarginyl-L-prolyl-D-alanylamide acetate. The molecular weight for Ganirelix acetate is 1570.4 Dalton as an anhydrous free base.
Formulation
The Ganirelix hormone (0.5mg/ml) contains 0.1mg acetic acid and 23.5mg mannitol pH-5.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Physical Appearance
Sterile Filtered colorless liquid formulation.
-
Stability
Ganirelix should be stored between 2°C- 8°C at all time. DO NOT FREEZE.
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Background
What is the molecular weight/Mw of GANIRELIX PEPTIDE Protein?
GANIRELIX PEPTIDE Protein has a total Mw of 1.57kDa.
What is the Purity of GANIRELIX PEPTIDE Protein?
GANIRELIX PEPTIDE Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GANIRELIX PEPTIDE Protein?
The biological functionality of GANIRELIX PEPTIDE Protein will be determined in the future.
What applications can GANIRELIX PEPTIDE Protein be used in?
GANIRELIX PEPTIDE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GANIRELIX PEPTIDE Protein?
The endotoxin level is minimal, GANIRELIX PEPTIDE 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 :
GDF10 HumanDescription:
Growth differentiation factor 10 Human Recombinant
Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.
Product # :
CYT-659Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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- sds-page
- Citations
Description
GDF10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (369-478 a.a.) and having a total molecular mass of 12.5 kDa. GDF10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GDF10 solution (1mg/ml) contains 10mM Sodium citrate (pH 3.5), 1mM DTT, 40% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
GDF10 is a member of the BMP family and the TGF-beta superfamily. GDF10 is expressed in femur, brain, lung, skeletal, muscle, pancreas and testis, and has a role in head formation and possibly multiple roles in skeletal morphogenesis. In humans, GDF10 mRNA is found in the cochlea and lung of fetuses, and in testis, retina, pineal gland, and other neural tissues of adults. The BMP family members are regulators of cell growth and differentiation in both embryonic and adult tissues. These proteins are characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing 7 conserved cysteine residues.
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Synonyms
Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.
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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
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.
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Background
What is the molecular weight/Mw of GDF10 HUMAN Protein?
GDF10 HUMAN Protein has a total Mw of 12.5kDa.
What is the source or expression system of GDF10 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF10 HUMAN Protein?
GDF10 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF10 HUMAN Protein?
The biological functionality of GDF10 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF10 HUMAN Protein?
MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.
What applications can GDF10 HUMAN Protein be used in?
GDF10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF10 HUMAN Protein?
The endotoxin level is minimal, GDF10 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LGALS9 HumanDescription:
Galectin-9 Human Recombinant
Lectin galactoside-binding soluble 9, Urate transporter/channel protein, LGALS9A, MGC125973, HUAT, Ecalectin, Galectin-9, MGC117375, MGC125974, HOM-HD-21, LGALS9.
Product # :
CYT-708Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- Citations
Description
LGALS9 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (1-148 a.a.) and having a molecular mass of 18.5 kDa. Galectin-9 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LGALS9 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
-
Introduction
LGLAS9 binds galactosides and has high affinity for the Forssman pentasaccharide. LGLAS9 participates in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. LGLAS9 is a ligand for HAVCR2/TIM3. LGLAS9 Induces T-helper type 1 lymphocyte (Th1) death. LGLAS9 performs as an eosinophil chemoattractant LGLAS9 is an S-type lectin which is over-expressed in Hodgkin's disease tissue and takes part in the interaction between the H&RS cells with their surrounding cells.
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Synonyms
Lectin galactoside-binding soluble 9, Urate transporter/channel protein, LGALS9A, MGC125973, HUAT, Ecalectin, Galectin-9, MGC117375, MGC125974, HOM-HD-21, LGALS9.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAFSGSQAPY LSPAVPFSGT IQGGLQDGLQ ITVNGTVLSS SGTRFAVNFQ TGFSGNDIAF HFNPRFEDGG YVVCNTRQNG SWGPEERKTH MPFQKGMPFD LCFLVQSSDF KVMVNGILFV QYFHRVPFHR VDTISVNGSV QLSYISFQ.
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Background
What is the molecular weight/Mw of LGALS9 HUMAN Protein?
LGALS9 HUMAN Protein has a total Mw of 18.5kDa.
What is the source or expression system of LGALS9 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS9 HUMAN Protein?
LGALS9 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS9 HUMAN Protein?
The biological functionality of LGALS9 HUMAN Protein will be determined in the future.
What is the amino acid sequence of LGALS9 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MAFSGSQAPY LSPAVPFSGT IQGGLQDGLQ ITVNGTVLSS SGTRFAVNFQ TGFSGNDIAF HFNPRFEDGG YVVCNTRQNG SWGPEERKTH MPFQKGMPFD LCFLVQSSDF KVMVNGILFV QYFHRVPFHR VDTISVNGSV QLSYISFQ.
What applications can LGALS9 HUMAN Protein be used in?
LGALS9 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS9 HUMAN Protein?
The endotoxin level is minimal, LGALS9 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin qA Human, PEGDescription:
Leptin Quadruple Antagonist Pegylated Human Recombinant
Product # :
CYT-1251Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.
Citations
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin-A TilapiaDescription:
Leptin-A Tilapia Recombinant
Product # :
CYT-1109Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin-A Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 16,491 Dalton. The Leptin-A Tilapia is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.
Citations
More Info
-
Introduction
Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin-A Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-A Tilapia should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin-A Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The first six N-terminal amino acids of recombinant Tilapia leptin A are Ala-Pro-Leu-Pro-Val-Glu.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.33 for 1 mg/ml Leptin-A Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.
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 :
PRDX2 MouseDescription:
Eukaryotic Translation Initiation Factor 4E Mouse Recombinant
PRDX2, Peroxiredoxin-2 (EC:1.11.1.15), TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Prdx2, Tdpx1, Tpx.
Product # :
ENZ-1061Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PRDX2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-198 a.a) and having a molecular mass of 24.3kDa. PRDX2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PRDX2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% Glycerol 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 700 pmol/min/ug, Activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25C for minute.
Citations
More Info
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Introduction
PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer. -
Synonyms
PRDX2, Peroxiredoxin-2 (EC:1.11.1.15), TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Prdx2, Tdpx1, Tpx.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMASGNA QIGKSAPDFT ATAVVDGAFK EIKLSDYRGK YVVLFFYPLD FTFVCPTEII AFSDHAEDFR KLGCEVLGVS VDSQFTHLAW INTPRKEGGL GPLNIPLLAD VTKSLSQNYG VLKNDEGIAY RGLFIIDAKG VLRQITVNDL PVGRSVDEAL RLVQAFQYTD EHGEVCPAGW KPGSDTIKPN VDDSKEYFSK HN
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Adiponectin Porcine, HEKDescription:
Adiponectin Porcine Recombinant, HEK derived
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-696Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
The Acrp30 Porcine Recombinant contains a total of 238 amino acids having a molecular Mass of 26kDa. The Porcine Adiponectin is fused to a 13 amino acid long N-terminal FLAG tag.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
Sterile filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 90% as determined by SDS PAGE.
Citations
More Info
-
Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Stability
For long term, store lyophilized AdipoQ 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.The lyophilized protein remains stable for 24 months when stored at -20°C.
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Solubility
Add deionized water and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
HVDYKDDDDK PAGETTEKPG ALLPMPKGAC AGWMAGIPGH PGHNGTPGRD GRDGVPGEKG EKGDTGLTGP KGDTGESGVT GVEGPRGFPG IPGRKGEPGE SAYVYRSAFS VGLETRVTVP NMPIRFTKIF YNQQNHYDVT TGKFHCNIPG LYYFSFHITV LKDVKVSLYK DKAVLFTYDQ QDKNVDQASG VLLYLEKGDQ WLQAYGDEEN GVYADNVNDS FTGFLLYHNIE.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
HVDYKDDDDK PAGETTEKPG ALLPMPKGAC AGWMAGIPGH PGHNGTPGRD GRDGVPGEKG EKGDTGLTGP KGDTGESGVT GVEGPRGFPG IPGRKGEPGE SAYVYRSAFS VGLETRVTVP NMPIRFTKIF YNQQNHYDVT TGKFHCNIPG LYYFSFHITV LKDVKVSLYK DKAVLFTYDQ QDKNVDQASG VLLYLEKGDQ WLQAYGDEEN GVYADNVNDS FTGFLLYHNIE.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CTSA MouseDescription:
Cathepsin-A Mouse Recombinant
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
Product # :
ENZ-945Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CTSA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) and having a molecular mass of 52.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CTSA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect cells.
Formulation
CTSA protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Cathepsin-A (CTSA) is a protective protein which is crucial for both the activity of beta-galactosidase and neuraminidase, CTSA associates with these enzymes and exerts a protective function required for their stability and activity. The CTSA protein is also a carboxypeptidase and can deamidate tachykinins. CTSA is a component of the lysosomal multienzyme complex along with beta-galactosidase and sialidase Neu1. CTSA is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities.
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Synonyms
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
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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
APDQDEIDCL PGLAKQPSFR QYSGYLRASD SKHFHYWFVE SQNDPKNSPV VLWLNGGPGC SSLDGLLTEH GPFLIQPDGV TLEYNPYAWN LIANVLYIES PAGVGFSYSD DKMYVTNDTE VAENNYEALK DFFRLFPEYK DNKLFLTGES YAGIYIPTLA VLVMQDPSMN LQGLAVGNGL ASYEQNDNSL VYFAYYHGLL GNRLWTSLQT HCCAQNKCNF YDNKDPECVN NLLEVSRIVG KSGLNIYNLY APCAGGVPGR HRYEDTLVVQ DFGNIFTRLP LKRRFPEALM RSGDKVRLDP PCTNTTAPSN YLNNPYVRKA LHIPESLPRW DMCNFLVNLQ YRRLYQSMNS QYLKLLSSQK YQILLYNGDV DMACNFMGDE WFVDSLNQKM EVQRRPWLVD YGESGEQVAG FVKECSHITF LTIKGAGHMV PTDKPRAAFT MFSRFLNKEP YVEHHHHHH.
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 :
AKR1C1 HumanDescription:
Aldo-Keto Reductase Family 1 Member C1 Human Recombinant
DDH1, DDH, HAKRC, 20-alpha-HSD, DD1/DD2, HBAB, C9, DD1, H-37, MBAB, MGC8954, 2-ALPHA-HSD, AKR1C1, Aldo-keto reductase family 1 member C1, 20-alpha-hydroxysteroid dehydrogenase, Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, Indanol dehydrogenase, Dihydrodiol dehydrogenase 1/2, Chlordecone reductase homolog HAKRC, High-affinity hepatic bile acid-binding protein
Product # :
ENZ-1130Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AKR1C1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-323) and having a molecular mass of 36.7 kDa.AKR1C1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1C1 solution (1mg/ml) contains 20% Glycerol, 0.1M NaCl and 20mM Tris-HCl buffer (pH 8.5).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 500pmol/min/ug. It is defined by the amount of enzyme that catalyzes oxidation of 1.0pmole 1-Acenaphthenol in the presence of NADP per minute at pH 8.8 at 25˚C.
Citations
More Info
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Introduction
Aldo-keto reductase family 1 member C1 or AKR1C1 is an enzyme, part of the aldo/keto reductase family that holds over 40 familiar proteins. AKR1C1 promotes the conversion of ketones & aldehydes to their alcohol forms by using cofactors such as NADH & NADPH. AKR1C1 promotes the progesterone reduction to its inactive molecule form 20-alpha-hydroxy-progesterone.
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Synonyms
DDH1, DDH, HAKRC, 20-alpha-HSD, DD1/DD2, HBAB, C9, DD1, H-37, MBAB, MGC8954, 2-ALPHA-HSD, AKR1C1, Aldo-keto reductase family 1 member C1, 20-alpha-hydroxysteroid dehydrogenase, Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, Indanol dehydrogenase, Dihydrodiol dehydrogenase 1/2, Chlordecone reductase homolog HAKRC, High-affinity hepatic bile acid-binding protein
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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
MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEATKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCNSH RPELVRPALE RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA VEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHPYFNQR KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV
LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN RNVRYLTLDI FAGPPNYPFS DEY
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Inhibin a HumanDescription:
Inhibin Alpha Human Recombinant
Product # :
HOR-303Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE analysis.
Citations
More Info
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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development. -
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
Alpha chain:
STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.
Beta Chain:
GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.
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 :
GATM HumanDescription:
Glycine Amidinotransferase Human Recombinant
Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.
Product # :
ENZ-583Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GATM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (38-423) and having a molecular mass of 46.9kDa (Molecular size on SDS-PAGE will appear higher).GATM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GATM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Glycine amidinotransferase mitochondrial (GATM) is a mitochondrial enzyme which is a member of the amidinotransferase family. The GATM enzyme is involved in creatine biosynthesis, where it catalyzes the transfer of a guanido group from L-arginine to glycine, resulting in guanidinoacetic acid, the immediate precursor of creatine, which has an imperative role in energy metabolism in muscle tissues. GATM is significant in embryonic and central nervous system development. GATM gene mutations cause arginine:glycine amidinotransferase deficiency, an inborn error of creatine synthesis characterized by mental retardation, language impairment, and behavioral disorders.
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Synonyms
Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.
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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 MGSMSTQAAT ASSRNSCAAD DKATEPLPKD CPVSSYNEWD PLEEVIVGRA ENACVPPFTI EVKANTYEKY WPFYQKQGGH YFPKDHLKKA VAEIEEMCNI LKTEGVTVRR PDPIDWSLKY KTPDFESTGL YSAMPRDILI VVGNEIIEAP MAWRSRFFEY
RAYRSIIKDY FHRGAKWTTA PKPTMADELY NQDYPIHSVE DRHKLAAQGK FVTTEFEPCF DAADFIRAGR DIFAQRSQVT NYLGIEWMRR HLAPDYRVHI ISFKDPNPMH IDATFNIIGP GIVLSNPDRP CHQIDLFKKA GWTIITPPTP IIPDDHPLWM SSKWLSMNVL MLDEKRVMVD
ANEVPIQKMF EKLGITTIKV NIRNANSLGG GFHCWTCDVR RRGTLQSYLD.
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 :
GCA HumanDescription:
Grancalcin Human Recombinant
Grancalcin EF-hand calcium binding protein, GCL, Grancalcin penta-EF-hand protein.
Product # :
PRO-080Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GCA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217.a.) and having a molecular mass of 26.1kDa. GCA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GCA protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Grancalcin is calcium-binding protein which is particularly abundant in human neutrophils. GCA is a member of the penta EF-hand (PEF) subfamily of EF-hand proteins, who also comprises calpain, sorcin, peflin, and ALG-2. GCA undergoes essential conformational changes upon binding of calcium, which subsequently exposes hydrophobic amino acid residues, that direct the protein to hydrophobic surfaces. GCA cooperates with L-plastin, a protein known to have actin bundling activity, which suggests that GCA has a part in the regulation of neutrophils adhesion.
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Synonyms
Grancalcin EF-hand calcium binding protein, GCL, Grancalcin penta-EF-hand protein.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAYPGYGGGF GNFSIQVPGM QMGQPVPETG PAILLDGYSG PAYSDTYSSA GDSVYTYFSA VAGQDGEVDA EELQRCLTQS GINGTYSPFS LETCRIMIAM LDRDHTGKMG FNAFKELWAA LNAWKENFMT VDQDGSGTVE HHELRQAIGL MGYRLSPQTL TTIVKRYSKN GRIFFDDYVA CCVKLRALTD FFRKRDHLQQ GSANFIYDDF LQGTMAI
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 :
GPC4 HumanDescription:
Glypican-4 Human Recombinant
Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.
Product # :
PRO-1912Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
GPC4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (401-529a.a) and having a molecular mass of 18kDa.GPC4 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GPC4 protein solution (0.25 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.
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Synonyms
Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-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.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSSSLP SNVCNDERMA AGNGNEDDCW NGKGKSRYLF AVTGNGLANQ GNNPEVQVDT SKPDILILRQ IMALRVMTSK MKNAYNGNDV DFFDISDESS GEGSGSGCEY QQCPSEFDYN ATDHAGKSAN EKADS
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.