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1000 results found for “Hepatitis D”
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Name :
Pfu-sso7d DNA PolymeraseDescription:
Pfu-sso7d DNA Polymerase Recombinant
DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.
Product # :
ENZ-1202Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Pfu-sso7d DNA Polymerase is derived from E. coli, having a molecular mass of 100 kDa. The Pfu-sso7d DNA Polymerase possesses the following activities: 5´→3´ DNA polymerase activity and 3´→5´ exonuclease activity. It generates blunt ends in the amplification products. The Pfu-ssod7 DNA Polymerase brings together a Pyrococcus furiosus DNA polymerase with a proc+essivity-enhancing domain Ssod7.
Source
Escherichia Coli.
Formulation
20mM Tris-HCl (pH 8.0), 50% glycerol, 0.1mM EDTA, 100mM KCl, 1mM DTT, 0.1% Tween20 and 0.1% NP-40.
Purity
Greater than 95 % as determined by SDS-PAGE analyses
Citations
More Info
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Synonyms
DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.
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Physical Appearance
Sterile liquid formulation.
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Stability
Store Pfu-sso7d DNA Polymerase 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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Applications
It is applicable for amplification reaction of genomic DNA, cDNA, dU-containing DNA and crude samples as templates.
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Background
The Pfu-sso7d DNA Polymerase preforms very well for all major PCR applications. The Pfu-sso7d DNA Polymerase generates long amplicons with accuracy and speed. The high fidelity makes the Pfu-sso7d DNA Polymerase a great choice for cloning. The error rate of Pfu-sso7d DNA Polymerase is approximately 50 fold lower than that of the Thermus aquaticus DNA polymerase. It generates blunt ends in the amplification products.
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Unit Definition
1U of enzyme catalyzes the incorporation of 10nmol of dNTP into polynucleotide fraction in 30 minutes at 74°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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Description:
SARS-Associated Coronavirus Nuclecapsid (340-390 a.a.) Recombinant, His Tag
Product # :
SARS-006Price :
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Description
The E.coli derived recombinant protein contains the Nucleocapsid C-Terminal protein 340-390 amino acids immunodominant regions fused to 6xHis tag at C-terminal.
Source
Escherichia Coli.
Formulation
SARS Nucleocapsid protein solution is supplied in PBS.
Purity
Protein is >90% pure as determined SDS-PAGE.
Citations
More Info
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Introduction
SARS-Associated Coronavirus Nuclecapsid is an enveloped viral componentthat contains three external structural antigens, the mains are membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a membrenal receptor and mediates membrane fusion to grant viral entry into the target cells. therefore, S-protein has a crucial part in virus infection cycle and is the main target of neutralizing antibodies.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Protein is shipped on ice packs. Upon arrival, Store at -20°C.
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Specificity
Immunoreactive with sera of SARS-infected individuals.
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Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CoV-2 Spike (1000-1200)Description:
Coronavirus 2019 Spike (1000-1200 a.a.) Recombinant
Product # :
SARS-017Price :
Quantity :
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Shipped with Ice Packs
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Description
The E.Coli derived recombinant protein contains the Coronavirus 2019 Spike (1000-1200 a.a.) immunodominant regions, fused to 6xHis tag at C-terminal.
Source
Escherichia Coli.
Formulation
CoV 2019 Spike Protein 1mg/ml solution is supplied in 1x PBS.
Purity
CoV 2019 Spike Protein is >90% pure as determined SDS-PAGE.
Citations
More Info
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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
CoV 2019 Spike Protein is shipped on ice packs. Upon arrival, Store at -20°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 :
DGCR6L HumanDescription:
DiGeorge Syndrome Critical Region Gene 6-Like Human Recombinant
Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.
Product # :
PRO-1454Price :
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Shipped with Ice Packs
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Description
DGCR6L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27.3kDa.DGCR6L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DGCR6L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 1mM DTT and 250mM Imidazole.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
DiGeorge syndrome critical region 6-like protein (DGCR6L) shares homology with the Drosophila gonadal protein, it is expressed in gonadal tissues and germ cells, and with the human laminin gamma-1 chain which functions in cell attachment and migration. DGCR6L is located in a region of chromosome 22 involved in the DiGeorge syndrome, one aspect of a wider collection of anomalies referred to as the CATCH 22 syndrome. Moreover, it is one of two functional genes encoding nearly identical proteins which have analogous expression patterns.
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Synonyms
Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.
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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 MGSMERYAAA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVVQA AQQRELEAVE HRIREEQRAM DQKIILELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCRAGNAA LGLGGPWQSP AAQCDQKGSP VPP.
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 :
DNAJC15 HumanDescription:
DnaJ (Hsp40) Homolog, Subfamily C, Member 15 Human Recombinant
DnaJ homolog subfamily C member 15, Cell growth-inhibiting gene 22 protein, Methylation-controlled J protein, MCJ, DNAJC15, DNAJD1, GIG22, HSD18.
Product # :
HSP-057Price :
Quantity :
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Shipped with Ice Packs
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Description
DNAJC15 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 116 amino acids (58-150 a.a.) and having a molecular mass of 12.8 kDa.DNAJC15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DNAJC15 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
DNAJC15 which is expressed ubiquitously and located on the membrane contains 1 J domain. In many advanced cases of ovarian adenocarcinoma DNAJC15 is absent or down-regulated, due to hypermethylation and allelic loss. Loss of expression correlates with increased resistance to antineoplastic drugs, such as cisplatin. DNAJC15is a crucial component of the TIM23 translocase complex and stimulates the ATPase activity of HSPA9.
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Synonyms
DnaJ homolog subfamily C member 15, Cell growth-inhibiting gene 22 protein, Methylation-controlled J protein, MCJ, DNAJC15, DNAJD1, GIG22, HSD18.
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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 MGSFRIWKPL EQVITETAKK ISTPSFSSYY KGGFEQKMSR REAGLILGVS PSAGKAKIRT AHRRVMILNH PDKGGSPYVA AKINEAKDLL ETTTKH.
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 :
NQO1 Human, ActiveDescription:
NAD(P)H Dehydrogenase Quinone 1, Active 1 Human Recombinant
NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.
Product # :
ENZ-1107Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NQO1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids ( 1-274aa ) and having a molecular mass of 33.0 kDa. NQO1 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NQO1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,000 pmol/min/ug. One unit will convert 1 pmoles resazurin to resorufin per minute at pH 7.5 at 25°C.
Citations
More Info
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Introduction
NQO1 belongs to the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 acts as an imperative part of cellular antioxidant defense by detoxifying quinines therefore preventing the formation of reactive oxygen species. It seems that NQO1 serves as a quinone reductase relating to conjugation reactions of hydroquinons involved in detoxification pathways in addition to biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Altered NQO1 expression is seen in many tumors and also linked to Alzheimer’s disease. NQO1 gene mutations are linked to tardive dyskinesia which is an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer.
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Synonyms
NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.
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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 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES
DLYAMNFNPI ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF
QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG
IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP
LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK
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 :
TDO2 HumanDescription:
Tryptophan 2,3-Dioxygenase Human Recombinant
Tryptophan 2,3-dioxygenase, TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase, TDO2, TPH2.
Product # :
ENZ-081Price :
Quantity :
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Shipped with Ice Packs
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Description
TDO2 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 426 amino acids (1-406 a.a.) and having a molecular mass of 50kDa. The TDO2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TDO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT, 1mM EDTA and 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TDO2 is a ferrous heme enzyme that catalyzes the first and rate-limiting step in the kynurenine pathway which is the major pathway of tryptophan metabolism. TDO2 integrates oxygen into the indole moiety of tryptophan. TDO2 has broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin.
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Synonyms
Tryptophan 2,3-dioxygenase, TDO, Tryptamin 2,3-dioxygenase, Tryptophan oxygenase, TO, TRPO, Tryptophan pyrrolase, Tryptophanase, TDO2, TPH2.
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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 MSGCPFLGNN FGYTFKKLPV EGSEEDKSQT GVNRASKGGL IYGNYLHLEK VLNAQELQSE TKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VVSRMHRVSV ILKLLVQQFS ILETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQN MRVPYNRRHY RDNFKGEENE LLLKSEQEKT LLELVEAWLE RTPGLEPHGF NFWGKLEKNI TRGLEEEFIR IQAKEESEEK EEQVAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYRALQ GALMIYFYRE EPRFQVPFQL LTSLMDIDSL MTKWRYNHVC MVHRMLGSKA GTGGSSGYHY LRSTVSDRYK VFVDLFNLST YLIPRHWIPK MNPTIHKFLY TAEYCDSSYF SSDESD.
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 :
CD300C Human, Sf9Description:
CD300C Human Recombinant, Sf9
CLM-6, CMRF-35, CMRF-35A, CMRF35, CMRF35-A1, CMRF35A, CMRF35A1, IGSF16, LIR, CMRF35-like molecule 6, CD300 antigen-like family member C, Immunoglobulin superfamily member, CD300C.
Product # :
PRO-2401Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD300C Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 163 amino acids (29-183a.a.) and having a molecular mass of 18kDa (Molecular size on SDS-PAGE will appear at approximately 28-40 kDa). CD300C is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD300C protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CMRF35-like molecule 6 (CD300C), is a member of the CD300 family. The CMRF35 antigen was identified by reactivity with a monoclonal antibody and present on monocytes, neutrophils, and some T and B lymphocytes.
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Synonyms
CLM-6, CMRF-35, CMRF-35A, CMRF35, CMRF35-A1, CMRF35A, CMRF35A1, IGSF16, LIR, CMRF35-like molecule 6, CD300 antigen-like family member C, Immunoglobulin superfamily member, CD300C.
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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
MTVAGPVGGS LSVQCRYEKE HRTLNKFWCR PPQILRCDKI VETKGSAGKR NGRVSIRDSP ANLSFTVTLE NLTEEDAGTY WCGVDTPWLR DFHDPIVEVE VSVFPAGTTT ASSPQSSMGT SGPPTKLPVH TWPSVTRKDS PEPSPHPGSL FSNVRLEHHH 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.
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Name :
DnaK SBDDescription:
DnaK Substrate Binding Domain E.Coli Recombinant
HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
Product # :
HSP-008Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant DnaK Substrate Binding domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing (385-546 a.a.) 163 amino acids and having a molecular mass of 17.7 kDa.
Source
Escherichia Coli.
Formulation
The protein contains 25mM Tris-HCl, pH7.5, 2mM B-ME and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. Dnak(residues 508-638) of the substrate binding domain is a-helical and appears to act as a lid covering the substrate binding cleft. DnaK(amino acid 508-638) was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.
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Synonyms
HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
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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
MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQG ERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HST.
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 :
CD27 Human, HEKDescription:
CD27 Human Recombinant, HEK
Tumor Necrosis Factor Receptor Superfamily Member 7, T-Cell Activation Antigen CD27, CD27 Molecule, CD27 Antigen, T Cell Activation Antigen S152, CD27L Receptor, TNFRSF7, S152, Tp55, T14.
Product # :
PRO-2751Price :
Quantity :
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Shipped with Ice Packs
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Description
CD27 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (20-191 a.a) containing a total of 411 amino acids, having a molecular mass of 46.2kDa. CD27 is fused to a 239 amino acid hIgG-His-Tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The CD27 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
ED50 range is ≤ 0.8 ug/ml. Defined by its binding ability in a functional ELISA with Human CD27 Ligand/TNFSF7 (CAT# cyt-953).
Citations
More Info
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Introduction
CD27 belongs to the TNF-receptor superfamily. CD27 is necessary for initiation and long-term maintenance of T cell immunity. CD27 binds to ligand CD70, and has a crucial role in regulating B-cell activation and immunoglobulin synthesis. The CD27 receptor transduces signals which result in the activation of NF-kappaB and MAPK8/JNK. Adaptor proteins TRAF2 and TRAF5 mediate the signaling process of CD27. CD27-binding protein (SIVA), which is a proapoptotic protein, can bind to the CD27 receptor and is believed to have a significant role in the apoptosis induced by CD27.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 7, T-Cell Activation Antigen CD27, CD27 Molecule, CD27 Antigen, T Cell Activation Antigen S152, CD27L Receptor, TNFRSF7, S152, Tp55, T14.
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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
ATPAPKSCPE RHYWAQGKLC CQMCEPGTFL VKDCDQHRKA AQCDPCIPGV SFSPDHHTRP HCESCRHCNS GLLVRNCTIT ANAECACRNG WQCRDKECTE CDPLPNPSLT ARSSQALSPH PQPTHLPYVS EMLEARTAGH MQTLADFRQL PARTLSTHWP PQRSLCSSDF IRLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Tamm HorsfallDescription:
Recombinant Human Tamm Horsfall Glycoprotein
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
Product # :
ENZ-1206Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa.
Source
HEK293
Formulation
The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE analysis.
SDS-PAGE
Citations
More Info
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Introduction
Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
Reduced Uromodulin levels is associated with chronic kidney disease.
UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.
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Synonyms
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at -18C. Upon reconstitution UMOD should be stored at 4C between 2-7 days and for future use below -18C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH
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Background
Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.
What is the molecular weight/Mw of UMOD Protein?
UMOD Protein has a total Mw of 65kDa.
What is the source or expression system of UMOD Protein?
HEK293.
What is the Purity of UMOD Protein?
UMOD Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of UMOD Protein?
The biological functionality of UMOD Protein will be determined in the future.
What is the amino acid sequence of UMOD Protein?
UMOD Protein is composed from 595 amino acids.
What applications can UMOD Protein be used in?
UMOD Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for UMOD Protein?
The endotoxin level is minimal, UMOD 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 :
GDF15 Human, HisDescription:
Growth and Differentiation Factor 15 Human Recombinant, His Tag
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-691Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GDF15 protein solution contains 10mM sodium citrate, pH-3.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
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 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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
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Background
What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein has a total Mw of 16.7kDa.
What is the source or expression system of GDF15 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 HUMAN, HIS Protein?
The biological functionality of GDF15 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
What applications can GDF15 HUMAN, HIS Protein be used in?
GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and
Lateral Flow.
What is the endotoxin level for GDF15 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF15 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.
- View Data Sheet
Name :
HBZ MouseDescription:
Hemoglobin-Zeta Mouse Recombinant
Hemoglobin subunit zeta, Hba-x, Hbz1, AI450015, Alpha-like embryonic globin chain x, Zeta-globin.
Product # :
PRO-2517Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
HBZ Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-142 a.a) and having a molecular mass of 18.3kDa.HBZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HBZ protein solution (0.25mg/ml) containing 20mM MES(pH6.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Hemoglobin Subunit Zeta (Hbz) or Hba-x is a alpha-like hemoglobin and part of the globin family. The protein is expressed and produced in the the yolk sac in early stages of embryonic development. Hemoglobin subunit zeta has 2 pseudogenes and 5 functional genes.
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Synonyms
Hemoglobin subunit zeta, Hba-x, Hbz1, AI450015, Alpha-like embryonic globin chain x, Zeta-globin.
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Physical Appearance
Sterile Filtered clear colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSLMKNERAI IMSMWEKMAA QAEPIGTETL ERLFCSYPQT KTYFPHFDLH HGSQQLRAHG FKIMTAVGDA VKSIDNLSSA LTKLSELHAY ILRVDPVNFK LLSHCLLVTM AARFPADFTP EVHEAWDKFM SILSSILTEK YR.
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 :
Dengue NS1 ST4, InsectDescription:
Dengue Virus NS1 Subtype 4 Recombinant, Insect Cells
Product # :
DEN-032Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
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Description
Recombinant Dengue Virus NS1 Subtype 4 produced in Insect Cells is a polypeptide chain containing amino acids 776-1130 and having a molecular weight of approximately 50kDa. Dengue NS1 ST4 is purified by proprietary chromatographic technique.
Source
Insect cells.
Formulation
Dengue NS1 ST4 protein solution in 1xD-PBS, pH7.4, 0.1% Thimerosal, 5mM EDTA, 1?g/ml of Leupeptin, Aprotinin and Pepstatin A.
Purity
Protein is >95% pure as determined by 12.5% SDS-PAGE.
Citations
More Info
-
Introduction
Caused by one of four closely related virus serotypes of the genus Flavivirus, family Flaviviridae, each serotype is sufficiently different that there is no cross-protection and epidemics caused by multiple serotypes (hyperendemicity) can occur. In cell culture experiments and mice Morpholino antisense oligos have shown specific activity against Dengue virus.
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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.
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 :
IFI30 HumanDescription:
IFN Gamma-Inducible protein 30 Human Recombinant
IFI30, Gamma-IFN-Inducible Lysosomal Thiol Reductase, IFN Gamma-Inducible Protein 30 Preproprotein, Gamma-IFN-Inducible Protein IP-30, Legumaturain, GILT, IP30, IFI-30, MGC32056, EC 1.8.
Product # :
CYT-183Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- Citations
Description
IFI30 Human Recombinant produced in E. coli is a single polypeptide chain containing 199 amino acids (58-232) and having a molecular mass of 22.5 kDa. IFI30 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The IFI30 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
-
Introduction
IFNI30 inducible lysosomal thiol reductase (IFI30), is a part of the GILT family. IFI30 is a lysosomal thiol reductase which at low pH is capable of decreasing protein’s disulfide bonds. IFI30 is expressed constitutively in antigen-presenting cells and induced by gamma-IFN in other cell types. Also, IFI30 plays an important role in MHC class II-restricted antigen processing. IFI30 facilitates the generation of MHC class II-restricted epitopes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds and Also facilitates MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or cross-presentation.
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Synonyms
IFI30, Gamma-IFN-Inducible Lysosomal Thiol Reductase, IFN Gamma-Inducible Protein 30 Preproprotein, Gamma-IFN-Inducible Protein IP-30, Legumaturain, GILT, IP30, IFI-30, MGC32056, EC 1.8.
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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 MGSMNAPLVN VTLYYEALCG GCRAFLIREL FPTWLLVMEI LNVTLVPYGN AQEQNVSGRW EFKCQHGEEE CKFNKVEACV LDELDMELAF LTIVCMEEFE DMERSLPLCL QLYAPGLSPD TIMECAMGDR GMQLMHANAQ RTDALQPPHE YVPWVTVNGK PLEDQTQLLT LVCQLYQGK.
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Background
What is the molecular weight/Mw of IFI30 HUMAN Protein?
IFI30 HUMAN Protein has a total Mw of 22.5kDa.
What is the source or expression system of IFI30 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFI30 HUMAN Protein?
IFI30 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFI30 HUMAN Protein?
The biological functionality of IFI30 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IFI30 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNAPLVN VTLYYEALCG GCRAFLIREL FPTWLLVMEI LNVTLVPYGN AQEQNVSGRW EFKCQHGEEE CKFNKVEACV LDELDMELAF LTIVCMEEFE DMERSLPLCL QLYAPGLSPD TIMECAMGDR GMQLMHANAQ RTDALQPPHE YVPWVTVNGK PLEDQTQLLT LVCQLYQGK.
What applications can IFI30 HUMAN Protein be used in?
IFI30 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFI30 HUMAN Protein?
The endotoxin level is minimal, IFI30 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 :
NQO1 HumanDescription:
NAD(P)H Dehydrogenase Quinone 1 Human Recombinant
NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.
Product # :
ENZ-448Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
NQO1 Human Recombinant fused with a 20 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids (1-274 a.a.) and having a molecular mass of 33kDa.The NQO1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NQO1 solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
NQO1 belongs to the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 acts as an imperative part of cellular antioxidant defense by detoxifying quinines therefore preventing the formation of reactive oxygen species. It seems that NQO1 serves as a quinone reductase relating to conjugation reactions of hydroquinons involved in detoxification pathways in addition to biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Altered NQO1 expression is seen in many tumors and also linked to Alzheimer’s disease. NQO1 gene mutations are linked to tardive dyskinesia which is an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer.
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Synonyms
NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.
-
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 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK.
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 :
IL13 Rat 109 a.a.Description:
Interleukin-13 109 a.a. Rat Recombinant
NC300, ALRH, BHR1, P600, IL-13.
Product # :
CYT-182Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
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Description
Interleukin-13 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids and having a molecular mass of 11.9 kDa. The IL-13 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) was lyophilized in PBS, pH7.4.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
ED50 range = 40ng/ml, corresponding to a specific activity of > 25,000IU/mg as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.Citations
More Info
-
Introduction
IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.
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Synonyms
NC300, ALRH, BHR1, P600, IL-13.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 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 13 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
VRRSTSPPVA LRELIEELSN ITQDQKTSLC NSSIVWSVDI TAGGFCAALE SLTNISSCNA IHRTQRILNG LCNQKASDVA SSPPDTKIEV AQFISKLLNY SKQLFRYGH.
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Background
What is the molecular weight/Mw of IL13 RAT 109 A.A. Protein?
IL13 RAT 109 A.A. Protein has a total Mw of 11.9kDa.
What is the source or expression system of IL13 RAT 109 A.A. Protein?
Escherichia Coli.
What is the Purity of IL13 RAT 109 A.A. Protein?
IL13 RAT 109 A.A. Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL13 RAT 109 A.A. Protein?
ED50 range = 40ng/ml, corresponding to a specific activity of > 25,000IU/mg as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.
What is the amino acid sequence of IL13 RAT 109 A.A. Protein?
VRRSTSPPVA LRELIEELSN ITQDQKTSLC NSSIVWSVDI TAGGFCAALE SLTNISSCNA IHRTQRILNG LCNQKASDVA SSPPDTKIEV AQFISKLLNY SKQLFRYGH.
What applications can IL13 RAT 109 A.A. Protein be used in?
IL13 RAT 109 A.A. Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL13 RAT 109 A.A. Protein?
The endotoxin level is minimal, IL13 RAT 109 A.A. Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL13 RAT 109 A.A. that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL13 RAT 109 A.A.?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets
-
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-13 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL13 Rhesus MacaqueDescription:
Interleukin-13 Rhesus Macaque Recombinant
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
Product # :
CYT-175Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
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Description
IL 13 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 114 amino acids and having a molecular mass of 12.6kDa.The IL 13 Rhesus Macaque is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 containing 3% trehalose.
Purity
Greater than 98.0% as determined by SDS-PAGE and HPLC analyses.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was < 5ng/ml, corresponding to a specific activity of > 2×105IU/mg.
Citations
More Info
-
Introduction
IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.
-
Synonyms
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IL-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-13 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized IL-13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SPSPVPRSTA LKELIEELVN ITQNQKAPLC NGSMVWSINL TAGVYCAALE SLINVSGCSA IEKTQRMLNG FCPHKVSAGQ FSSLRVRDTK IEVAQFVKDL LVHLKKLFRE GRFN
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Background
What is the molecular weight/Mw of IL13 RHESUS MACAQUE Protein?
IL13 RHESUS MACAQUE Protein has a total Mw of 12.6kDa.
What is the source or expression system of IL13 RHESUS MACAQUE Protein?
Escherichia Coli.
What is the Purity of IL13 RHESUS MACAQUE Protein?
IL13 RHESUS MACAQUE Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IL13 RHESUS MACAQUE Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was < 5ng/ml, corresponding to a specific activity of > 2×105IU/mg.
What is the amino acid sequence of IL13 RHESUS MACAQUE Protein?
SPSPVPRSTA LKELIEELVN ITQNQKAPLC NGSMVWSINL TAGVYCAALE SLINVSGCSA IEKTQRMLNG FCPHKVSAGQ FSSLRVRDTK IEVAQFVKDL LVHLKKLFRE GRFN.
What applications can IL13 RHESUS MACAQUE Protein be used in?
IL13 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL13 RHESUS MACAQUE Protein?
The endotoxin level is minimal, IL13 RHESUS MACAQUE Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL13 RHESUS MACAQUE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL13 RHESUS MACAQUE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TNFRSF8 igG-His HumanDescription:
CD30 Ligand Receptor, IgG-His Tag Human Recombinant
Tumor Necrosis Factor Receptor Superfamily Member 8, Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1.
Product # :
CYT-983Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
TNFRSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 613 amino acids (19-379 a.a.) and having a molecular mass of 66.7kDa (Molecular size on SDS-PAGE will appear at approximately 25-100kDa). TNFRSF8 is expressed with a 252 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFRSF8 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.
Citations
More Info
-
Introduction
Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 8, Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-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
ADPFPQDRPF EDTCHGNPSH YYDKAVRRCC YRCPMGLFPT QQCPQRPTDC RKQCEPDYYL DEADRCTACV TCSRDDLVEK TPCAWNSSRV CECRPGMFCS TSAVNSCARC FFHSVCPAGM IVKFPGTAQK NTVCEPASPG VSPACASPEN CKEPSSGTIP QAKPTPVSPA TSSASTMPVR GGTRLAQEAA SKLTRAPDSP SSVGRPSSDP GLSPTQPCPE GSGDCRKQCE PDYYLDEAGR CTACVSCSRD DLVEKTPCAW NSSRTCECRP GMICATSATN SCARCVPYPI CAAETVTKPQ DMAEKDTTFE APPLGTQPDC NPTPENGEAP ASTSPTQSLL VDSQASKTLP IPTSAPVALS STGKAAAFES RACSLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH 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.
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Name :
SARS MERS, HEKDescription:
SARS MERS Spike Glycoprotein-S1, Recombinant
Product # :
SARS-023Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The HEK293 derived recombinant protein contains the SARS MERS Spike Glycoprotein S1, amino acids 18-725 fused to dimeric Fc tag at N-terminal having a total Mw of 215.7 kDa.
Source
HEK293
Formulation
SARS MERS S1 protein solution is supplied in PBS.
Purity
Protein is >85% pure as determined SDS-PAGE.
Citations
More Info
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Introduction
SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
SARS MERS Protein is shipped on ice packs. Upon arrival, Store at -20°C.
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Purification Method
Purified by Protein-G chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL7 Human, HEKDescription:
Interleukin-7 Human Recombinant, HEK
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Product # :
CYT-197Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL-7 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 19-30kDa due to glycosylation.The IL-7 is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The IL7 was lyophilized from 1mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.Citations
More Info
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Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
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Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 IL-7 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
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Background
What is the molecular weight/Mw of IL7 HUMAN, HEK Protein?
IL7 HUMAN, HEK Protein has a total Mw of 24.5kDa.
What is the source or expression system of IL7 HUMAN, HEK Protein?
HEK.
What is the Purity of IL7 HUMAN, HEK Protein?
IL7 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL7 HUMAN, HEK Protein?
The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.
What applications can IL7 HUMAN, HEK Protein be used in?
IL7 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL7 HUMAN, HEK Protein?
The endotoxin level is minimal, IL7 HUMAN, HEK Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL7 HUMAN, HEK that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL7 HUMAN, HEK?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GST Monoclonal antibodyDescription:
Glutathione-S-Transferase, Mouse antibody
Product # :
ANT-219Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Monoclonal antibodies are produced by immunizing mouse with GST protein.
Formulation
1×PBS & 50% glycerol.
Citations
More Info
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Introduction
GST family of enzymes comprises a long list of cytosolic, mitochondrial, and microsomal proteins that are 45-55 kDa (dimer form) size and are capable of multiple reactions with a multitude of substrates, both endogenous and xenobiotic. GST catalyses the conjugation of reduced glutathione meaning the sulfhydryl group, to electrophilic centers on a wide variety of substrates. This activity is useful in the detoxification of endogenous compounds such as peroxidised lipids, as well as the metabolism of xenobiotics. GST binds toxins and function as transport protein. Glutathione S-transferase is used to create the so-called 'GST gene fusion system'. The GST is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's multiple cloning sites results in expression of a fusion protein - the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. Fusion proteins offer an important biological assay for direct protein-to-protein interactions. The GST tag has the size of 220 amino acids, which, compared to other tags like the myc- or the FLAG-tag, is quite big. It is fused to the N-terminus of a protein. However, many commercially-available sources of GST-tagged plasmids include a thrombin domain for cleavage of the GST tag during protein purification. A GST-tag is often used to separate and purify proteins that contain the GST-fusion. GST-fusion proteins can be produced in Escherichia coli, as recombinant proteins.
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Ig Subclass
Mouse IgG2b.
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Clone
PGSTSHG.
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Applications
Western Blot, Immunoprecipitation.
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Titer
Western Blotting: 1μg/ml.
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Type
Mouse Antibody Monoclonal.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ALDH3A1 HumanDescription:
Aldehyde Dehydrogenase 3 Family Member A1 Human Recombinant
Aldehyde dehydrogenase 3 family member A1, aldehyde dehydrogenase, dimeric NADP-preferring, ALDH-3, aldehyde dehydrogenase isozyme, ALDHIII, MGC104062, aldehyde dehydrogenase type III, Aldehyde dehydrogenase, stomach aldehyde dehydrogenase, EC 1.2.1.53, aldehyde dehydrogenase 3A, Aldehyde dehydrogenase.
Product # :
ENZ-479Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ALDH3A1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 473 amino acids (1-453 a.a.) and having a molecular mass of 52.5 kDa. ALDH3A1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ALDH3A1 solution containing 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity was found to be < 1 units/ml. Activity was obtained by measuring the increase of NADP in absorbance at 340 nm resulting from the reduction of NAD. 1 unit will oxidize 1umole of acetaldehyde to acetic acid per minute at pH 8 at 25°C in the presence of beta-NAD, potassium and thiols.Citations
More Info
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Introduction
ALDH3A1 is involved in the detoxification of alcohol-derived acetaldehyde. ALDH3A1 participates in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. ALDH3A1 oxidizes aromatic aldehyde substrates and toxic aldehydes. ALDH3A1 forms a cytoplasmic homodimer that oxidizes aromatic and medium-chain saturated and unsaturated aldehyde substrates. ALDH3A1 promotes resistance to UV and 4-hydroxy-2-nonenal-induced oxidative damage in the cornea.
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Synonyms
Aldehyde dehydrogenase 3 family member A1, aldehyde dehydrogenase, dimeric NADP-preferring, ALDH-3, aldehyde dehydrogenase isozyme, ALDHIII, MGC104062, aldehyde dehydrogenase type III, Aldehyde dehydrogenase, stomach aldehyde dehydrogenase, EC 1.2.1.53, aldehyde dehydrogenase 3A, Aldehyde dehydrogenase.
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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 MSKISEAVKR ARAAFSSGRT RPLQFRIQQL EALQRLIQEQ EQELVGALAA DLHKNEWNAY YEEVVYVLEE IEYMIQKLPE WAADEPVEKT PQTQQDELYI HSEPLGVVLV IGTWNYPFNL TIQPMVGAIA AGNAVVLKPS ELSENMASLL ATIIPQYLDK DLYPVINGGV PETTELLKER FDHILYTGST GVGKIIMTAA AKHLTPVTLE LGGKSPCYVD KNCDLDVACR RIAWGKFMNS GQTCVAPDYI LCDPSIQNQI VEKLKKSLKE FYGEDAKKSR DYGRIISARH FQRVMGLIEG QKVAYGGTGD AATRYIAPTI LTDVDPQSPV MQEEIFGPVLPIVCVRSLEE AIQFINQREK PLALYMFSSN DKVIKKMIAE TSSGGVAAND VIVHITLHSL PFGGVGNSGM GSYHGKKSFE TFSHRRSCLV RPLMNDEGLK VRYPPSPAKM TQH.
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 :
HK3 HumanDescription:
Hexokinase-3 Human Recombinant
Hexokinase-3, EC 2.7.1.1, Hexokinase type III, HK III, HXK3, HK3.
Product # :
PKA-229Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HK-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain fused to His tag at the N-terminal encoding the sequence of 943 amino acids and having a molecular mass of 101.1 kDa.HXK3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris pH 8.0 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. HK3 encodes hexokinase 3. Similar to hexokinases 1 and 2, this allosteric enzyme is inhibited by its product glucose-6-phosphate. Hexokinase3 lacks the hydrophobic N-terminal sequence critical for targeting to mitochondria. Hexpkinase3 may have anabolic functions, providing H6P for glycogen or lipid synthesis.
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Synonyms
Hexokinase-3, EC 2.7.1.1, Hexokinase type III, HK III, HXK3, HK3.
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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). Please avoid freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDSIGSSGLR QGEETLSCSE EGLPGPSDSSE LVQECLQQFKVTRAQLQQI QASLLGSMEQ ALRGQASPAP AVRMLPTYVG STPHGTEQGD FVVLELGATG ASLRVLWVTL TGIEGHRVEP RSQEFVIPQE VMLGAGQQLF DFAAHCLSEF LDAQPVNKQGLQLGFSFSFP CHQTGLDRST LISWTKGFRC SGVEGQDVVQ LLRDAIRRQG AYNIDVVAVV NDTVGTMMGC EPGVRPCEVG LVVDTGTNAC YMEEARHVAV LDEDRGRVCV SVEWGSFSDD GALGPVLTTF DHTLDHESLN PGAQRFEKMI GGLYLGELVR LVLAHLARCG VLFGGCTSPA LLSQGSILLE HVAEMEDPST GAARVHAILQ DLGLSPGASD VELVQHVCAA VCTRAAQLCA AALAAVLSCL QHSREQQTLQ VAVATGGRVC ERHPRFCSVL QGTVMLLAPE CDVSLIPSVDGGGRGVAMVT AVAARLAAHR RLLEETLAPF RLNHDQLAAV QAQMRKAMAK GLRGEASSLR MLPTFVRATP DGSERGDFLA LDLGGTNFRV LLVRVTTGVQ ITSEIYSIPE TVAQGSGQQL FDHIVDCIVD FQQKQGLSGQ SLPLGFTFSF PCRQLGLDQG ILLNWTKGFK ASDCEGQDVV SLLREAITRR QAVELNVVAI VNDTVGTMMS CGYEDPRCEI GLIVGTGTNA CYMEELRNVAGVPGDSGRMC INMEWGAFGD DGSLAMLSTR FDASVDQASI NPGKQRFEKM ISGMYLGEIV RHILLHLTSL GVLFRGQQIQ RLQTRDIFKT KFLSEIESDS LALRQVRAIL EDLGLPLTSDDALMVLEVCQ AVSQRAAQLC GAGVAAVVEK IRENRGLEEL AVSVGVDGTL YKLHPRFSSL VAATVRELAP RCVVTFLQSE DGSGKGAALV TAVACRLAQL TRV.
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.