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1000 results found for “nucleopurin”
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Name :
S.Typhi OMPDescription:
Salmonella Typhi Outer Membrane Protein Recombinant
Product # :
STY-002Price :
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Description
Recombinant Salmonella Typhi Outer Membrane Protein produced in E.coli contains 315 amino acids, and fused to a 6 His Tag at C-terminus, migrating as a 33kDa band on SDS-PAGE.S. typhi outer membrane protein is a central pathogen in S. typhi infection, and is directly exposed to the outside to interact with the human immune system.
Source
Escherichia Coli.
Formulation
Sterile Filtered solution containing 10mM Tris-HCl, 1mM EDTA and 50mM arginine.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
More Info
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Introduction
Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.
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Physical Appearance
Sterile Filtered solution.
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Stability
S.Typhi OMP although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IBV-NPDescription:
Influenza B Virus Nucleoprotein Recombinant
Product # :
IHA-038Price :
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Description
Recombinant Influenza B Virus Nucleoprotein produced in E. coli having a Mw of 76.8kDa. IBV-NP is fused to a 6xHis tag at its C terminal is and purified by proprietary chromatographic technique.
Source
E. coli.
Formulation
IBV-NP protein solution contains 25mM K2CO3 and PBS.
More Info
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
HMSNMDIDGMNTGTIDKTPEEITSGTSGTTRPIIRPATLAPPSNKRTRNPSPDRTTTSSE
DDVGRKAQKKQTPTEIKKSVYNMVVKLGEFYNQMMVKAGLNDDMERNLIQNAHAVERILL
AATDDKKTEFQKKKNARDVKEGKEEIDHNKTGGTFYKMVRDDKTIYFSPIRITFLKEEVKT
MYKTTMGSDGFSGLNHIMIGHSQMNDVCFQRSKALKRVGLDPSLISTFAGSTVPRRSGATGV
AIKGGGTLVAEAIRFIGRAMADRGLLRDIKAKTAYEKILLNLKNKCSAPQQKALVDQVIGSRN
PGIADIEDLTLLARSMVVVRPSVASKVVLPISIYAKIPQLGFNVEEYSMVGYEAMALYNMATP
VSILRMGDDAKDKSQLFFMSCFGAAYEDLRVLSALTGTEFKPRSALKCKGFHVPAKEQVEGMGA
ALMSIKLQFWAPMTRSGGNEVGGDGGSGQISCSPVFAVERPIALSKQAVRRMLSMNIEGRDADV
KGNLLKMMNDSMAKKTSGNAFIGKKMFQISDKNKTNPIEIPIKQTIPNFFFGRDTAEDYDDLDYLE.
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Background
Influenza B virus, often overshadowed by its influenza A counterpart, remains a substantial contributor to seasonal influenza infections and poses a considerable public health challenge. In the quest for effective countermeasures, Influenza B Virus Nucleoprotein Recombinant has emerged as a focal point in the ongoing battle against this resilient virus. This research endeavors to unveil the intricacies of the Nucleoprotein Recombinant, delving into its structural nuances, immunogenic capabilities, and applications in vaccine development and antiviral therapies. By dissecting the properties of the Nucleoprotein Recombinant, scientists aspire to fortify our defenses against Influenza B, potentially reshaping strategies for broader influenza immunity.
Structural Insights into Nucleoprotein Recombinant:
Engineered to replicate key viral components, the Influenza B Virus Nucleoprotein Recombinant serves as a molecular mirror, allowing a comprehensive study of the virus's genetic material. Understanding its three-dimensional structure and conformational intricacies is crucial, not only for decoding the virus's replication mechanisms but also for tailoring interventions like vaccines and antiviral drugs to specific vulnerabilities.
Immunogenic Potential and Vaccine Development:
The challenge of Influenza B's seasonal variability necessitates innovative approaches to vaccine development. Nucleoprotein Recombinant, designed to induce potent immune responses, emerges as a promising candidate. By presenting conserved viral elements to the immune system, the recombinant protein seeks to instigate robust and durable immunity, countering the virus's propensity for antigenic drift and promoting broader protection.
Application in Antiviral Therapies:
In addition to its role in vaccination, the Influenza B Virus Nucleoprotein Recombinant holds potential in antiviral therapies. The recombinant protein's ability to provoke immune responses can be harnessed for the development of immunotherapies. Monoclonal antibodies derived from the Nucleoprotein Recombinant may offer targeted treatments, providing a dynamic approach to mitigating the impact of Influenza B infections.
Challenges and Future Directions:
Despite the promises held by the Nucleoprotein Recombinant, challenges persist. The virus's ability to undergo genetic reassortment and antigenic drift requires ongoing vigilance and adaptability in recombinant strategies. Considerations of vaccine safety, efficacy, and public acceptance demand continual exploration to optimize the translational success of Nucleoprotein Recombinant-based interventions.
Influenza B Virus Nucleoprotein Recombinant stands as a beacon in the scientific quest against influenza, offering a pathway to a more comprehensive and resilient immunity. Its structural insights, immunogenic potential, and applications in vaccine development and antiviral therapies position it as a central player. As researchers delve deeper into the molecular intricacies of Nucleoprotein Recombinant, they not only fortify our defenses against Influenza B but potentially pave the way for a paradigm shift in our approach to influenza prevention and control, influencing the landscape of global health preparedness.
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 :
T.pallidum p41 MosaicDescription:
Treponema pallidum p41 Mosaic Recombinant
Product # :
TRP-244Price :
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Description
The E.coli derived recombinant protein contains the outer membrane T.Pallidum p41 immunodominant regions. The protein is fused with a GST tag.
Source
Escherichia Coli.
Formulation
25mM Tris-HCl pH-8, 60mM NaCl & 50% glycerol.
Purity
Treponema Pallidum protein is >90% pure as determined by 10% PAGE (coomassie staining).
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Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
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Stability
Treponema Pallidum protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Treponema Pallidum protein is suitable for ELISA and Western blots, excellent antigen for detection of T. Pallidum with minimal specificity problems.
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Specificity
Immunoreactive with sera of T.Pallidum infected individuals.
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Purification Method
Treponema Pallidum protein was 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 :
CTDSP1 HumanDescription:
CTD Small Phosphatase 1 Human Recombinant
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1, Nuclear LIM interactor-interacting factor 3, NLI-IF, NLI-interacting factor 3, Small C-terminal domain phosphatase 1, SCP1, Small CTD phosphatase 1, CTDSP1, NIF3, NLIIF.
Product # :
ENZ-110Price :
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Shipped with Ice Packs
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Description
CTDSP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 280 amino acids (1-260 a.a.) and having a molecular mass of 31.2kDa.CTDSP1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CTDSP1 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CTDSP1 is a class 2C phosphatase with activity dependent on the conserved DxD motif. CTDSP1 preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. In addition, CTDSP1 negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation.
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Synonyms
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1, Nuclear LIM interactor-interacting factor 3, NLI-IF, NLI-interacting factor 3, Small C-terminal domain phosphatase 1, SCP1, Small CTD phosphatase 1, CTDSP1, NIF3, NLIIF.
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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 MDSSAVITQI SKEEARGPLR GKGDQKSAAS QKPRSRGILH SLFCCVCRDD GEALPAHSGA PLLVEENGAI PKTPVQYLLP EAKAQDSDKI CVVIDLDETL VHSSFKPVNN ADFIIPVEID GVVHQVYVLK RPHVDEFLQR MGELFECVLF TASLAKYADP VADLLDKWGA FRARLFRESC VFHRGNYVKD LSRLGRDLRR VLILDNSPAS YVFHPDNAVP VASWFDNMSD TELHDLLPFF EQLSRVDDVY SVLRQPRPGS.
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 :
Cyclophilin A RatDescription:
Cyclophilin-A Rat Recombinant
Peptidyl-prolyl cis-trans isomerase A, EC:5.2.1.8, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, p1B15, p31, Ppia.
Product # :
ENZ-938Price :
Quantity :
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Shipped at Room temp
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Description
Cyclophilin-A Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val2-Leu164) containing 173 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 19kDa.
Source
Escherichia Coli.
Formulation
Cyclophilin-A was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5%(w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidyl-prolyl cis-trans isomerase A, EC:5.2.1.8, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, p1B15, p31, Ppia.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Cyclophilin-A 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
MKHHHHHHASVNPTVFFDIT ADGEPLGRVC FELFADKVPK TAENFRALST GEKGFGYKGS SFHRIIPGFM CQGGDFTRHN GTGGKSIYGE KFEDENFILK HTGPGILSMA NAGPNTNGSQ FFICTAKTEW LDGKHVVFGK VKEGMSIVEA MERFGSRNGK TSKKITISDC GQL.
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 :
DCN MouseDescription:
Decorin Mouse Recombinant
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
Product # :
PRO-2234Price :
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Description
DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (17-354 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 344 amino acids and having a molecular mass of 38.8kDa.DCN shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
DCN protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
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Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN.
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Physical Appearance
Sterile filtered colorless solution.
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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
GPFEQRGLFD FMLEDEASGI IPYDPDNPLI SMCPYRCQCH LRVVQCSDLG LDKVPWDFPP DTTLLDLQNN KITEIKEGAF KNLKDLHTLI LVNNKISKIS PEAFKPLVKL ERLYLSKNQL KELPEKMPRT LQELRVHENE ITKLRKSDFN GLNNVLVIEL GGNPLKNSGI ENGAFQGLKS LSYIRISDTN ITAIPQGLPT SLTEVHLDGN KITKVDAPSL KGLINLSKLG LSFNSITVME NGSLANVPHL RELHLDNNKL LRVPAGLAQH KYIQVVYLHN NNISAVGQND FCRAGHPSRK ASYSAVSLYG NPVRYWEIFP NTFRCVYVRS AIQLGNYKHH HHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AMBPDescription:
Alpha-1 Microglobulin Human Recombinant
Alpha-1-microglobulin/bikunin precursor, HCP, ITIL, ITI, EDC1, HI30, IATIL, ITILC, UTI, A1M, bikunin, complex-forming glycoprotein heterogeneous in charge, growth-inhibiting protein 19, inter-alpha-trypsin inhibitor light chain, protein AMBP, protein HC, trypstatin, uristatin, uronic-acid-rich protein.
Product # :
PRO-957Price :
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Shipped with Ice Packs
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Description
AMBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (20-203) and having a molecular mass of 23.1 kDa.AMBP is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The AMBP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species.
A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore.
Half of all human plasma A1M (approximately 0.03mg/ml) forms a 1:1 complex with about 5% of plasma immunoglobulin A. The resulting macromolecular complexes’ molecular weight is 200000, and a plasma concentration of 0.3mg/ml. The complex can exhibit both antibody activity and affect many of the biological actions of free Alpha-1-microglobulin.
Alpha-1-microglobulin was first discovered in pathological human urine.
It was suggested that A1M might be involved in tissue defense against reactive oxygen species, oxidation by heme and kynurenin. Evidence also suggests that A1M functions in the regulation of the immune system. Other functions include inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis. -
Synonyms
Alpha-1-microglobulin/bikunin precursor, HCP, ITIL, ITI, EDC1, HI30, IATIL, ITILC, UTI, A1M, bikunin, complex-forming glycoprotein heterogeneous in charge, growth-inhibiting protein 19, inter-alpha-trypsin inhibitor light chain, protein AMBP, protein HC, trypstatin, uristatin,
uronic-acid-rich protein. -
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 MGPVPTPPDN IQVQENFNIS RIYGKWYNLA IGSTCPWLKK IMDRMTVSTL VLGEGATEAE ISMTSTRWRK GVCEETSGAY EKTDTDGKFL YHKSKWNITM ESYVVHTNYD EYAIFLTKKF SRHHGPTITA KLYGRAPQLR ETLLQDFRVV AQGVGIPEDS IFTMADRGEC VPGEQEPEPI LIPRV.
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 :
ANP32A HumanDescription:
Acidic Nuclear Phosphoprotein 32 Family Member A Human Recombinant
I1PP2A, LANP, MAPM, PHAP1, Leucine-rich acidic nuclear protein, PP32, Mapmodulin.
Product # :
PRO-252Price :
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Description
ANP32A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 269 amino acids (1-249a.a.) and having a molecular mass of 30.7kDa. ANP32A is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANP32A solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 100mM NaCl, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
ANP32A often cooperate with MAP1B, TAF1A and Protein SET. ANP32A is involved in several cellular processes, such as proliferation, differentiation, caspase-dependent and caspase-independent apoptosis. Mapmodulin takes a part in E4F1-mediated transcriptional repression.
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Synonyms
I1PP2A, LANP, MAPM, PHAP1, Leucine-rich acidic nuclear protein, PP32, Mapmodulin.
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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 MEMGRRIHLE LRNRTPSDVK ELVLDNSRSN EGKLEGLTDE FEELEFLSTI NVGLTSIANL PKLNKLKKLE LSDNRVSGGL EVLAEKCPNL THLNLSGNKI KDLSTIEPLK KLENLKSLDL FNCEVTNLND YRENVFKLLP QLTYLDGYDR DDKEAPDSDA EGYVEGLDDE EEDEDEEEYD EDAQVVEDEE DEDEEEEGEE EDVSGEEEED EEGYNDGEVD DEEDEEELGE EERGQKRKRE PEDEGEDDD.
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 :
DNAJB2 HumanDescription:
DnaJ (Hsp40) homolog, subfamily B, member 2 Human Recombinant
DnaJ homolog subfamily B member 2, DnaJ protein homolog 1, Heat shock 40 kDa protein 3, Heat shock protein J1, HSJ-1, DNAJB2, HSJ1, HSPF3.
Product # :
HSP-035Price :
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Shipped with Ice Packs
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Description
DNAJB2 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 300 amino acids (1-277 a.a.) and having a molecular mass of 33kDa. The DNAJB2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DNAJB2 solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DnaJB2 is a member of the DnaJ family. The DnaJ family is one of the largest of all the chaperone families which has evolved with diverse cellular localization and functions. DnaJB2 are important mediators of proteolysis which are involved in the regulation of protein degradation, exocytosis and endocytosis. The DnaJ proteins play a significant role in the HSP70 chaperone machine by interacting with HSP70 to stimulate ATP hydrolysis. DnaJB2 is expressed almost solely in the brain, with the highest levels in the frontal cortex and hippocampus.
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Synonyms
DnaJ homolog subfamily B member 2, DnaJ protein homolog 1, Heat shock 40 kDa protein 3, Heat shock protein J1, HSJ-1, DNAJB2, HSJ1, HSPF3.
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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 MGSMASYYEI LDVPRSASAD DIKKAYRRKA LQWHPDKNPD NKEFAEKKFK EVAEAYEVLS DKHKREIYDR YGREGLTGTG TGPSRAEAGS GGPGFTFTFR SPEEVFREFF GSGDPFAELF DDLGPFSELQ NRGSRHSGPF FTFSSSFPGH SDFSSSSFSF SPGAGAFRSV STSTTFVQGR RITTRRIMEN GQERVEVEED GQLKSVTING VPDDLALGLE LSRREQQPSV TSRSGGTQVQ QTPASCPLDS DLSEDEDLQL AMAYSLSEME AAGKKPADVF.
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 :
NDRG3 HumanDescription:
N-Myc Downstream Regulated 3 Human Recombinant
Protein NDRG3, N-myc downstream-regulated gene 3 protein, NDRG3, N-Myc Downstream Regulated 3.
Product # :
PRO-2100Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NDRG3 Human Recombinant produced in E. coli is a single polypeptide chain containing 386 amino acids (1-363) and having a molecular mass of 42.4 kDa.NDRG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NDRG3 solution (0.25mg/1ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
N-Myc Downstream Regulated 3, also known as NDRG3, is a protein coding gene which is a part of the NDRG family and is expressed greatly in brain. NDRG2 is an important paralog of NDRG3.
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Synonyms
Protein NDRG3, N-myc downstream-regulated gene 3 protein, NDRG3, N-Myc Downstream Regulated 3.
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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 MGSMDELQDV QLTEIKPLLN DKEHDIETTH GVVHVTIRGL PKGNRPVILT YHDIGLNHKS CFNAFFNFED MQEITQHFAV CHVDAPGQQE GAPSFPTGYQ YPTMDELAEM LPPVLTHLSL KSIIGIGVGA GAYILSRFAL NHPELVEGLV LINVDPCAKG WIDWAASKLS GLTTNVVDII LAHHFGQEEL QANLDLIQTY RMHIAQDINQ DNLQLFLNSY NGRRDLEIER PILGQNDNKS KTLKCSTLLV VGDNSPAVEA VVECNSRLNP INTTLLKMAD CGGLPQVVQP GKLTEAFKYF LQGMGYIPSA SMTRLARSRT HSTSSSLGSG ESPFSRSVTS NQSDGTQESC ESPDVLDRHQ TMEVSC.
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 :
NENF HumanDescription:
Neudesin Neurotrophic Factor Human Recombinant
Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.
Product # :
CYT-778Price :
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Description
NENF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 32-172) containing 151 amino acids including a 10 a.a N-terminal His tag and having a molecular mass of 16.9kDa.
Source
Escherichia Coli.
Formulation
NENF was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Neudesin Neurotrophic Factor (NENF) is a member of the cytochrome b5 family, MAPR subfamily. NENF contains 1 cytochrome b5 heme-binding domain. NENF exhibits neurotrophic activity and activates phosphorylation of MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT in primary cultured neurons. NENF doesn’t have mitogenic activity in primary cultured astrocytes. NENF may play a part in neuronal differentiation and may have a transient influence on neural cell proliferation in neural precursor cells. NENF neurotrophic activity is increased by binding to heme. NENF is up-regulated in immortal cells and induced in estrogen receptor positive breast cancer expressing progesterone receptor.
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Synonyms
Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. NENF 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
MKHHHHHHASGQTPRPAERG PPVRLFTEEE LARYGGEEED QPIYLAVKGV VFDVTSGKEF YGRGAPYNAL TGKDSTRGVA KMSLDPADLT HDTTGLTAKE LEALDEVFTK VYKAKYPIVG YTARRILNED GSPNLDFKPE DQPHFDIKDE F.
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 :
SNRPB HumanDescription:
Small Nuclear Ribonucleoprotein Polypeptides B & B1 Human Recombinant
Small nuclear ribonucleoprotein-associated proteins B and B', snRNP-B, Sm protein B/B', Sm-B/B', SmB/B', SNRPB, COD, SNRPB1, SmB/SmB'.
Product # :
PRO-1511Price :
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Description
SNRPB Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 25.4 kDa which migrates at 30kDa on SDS-PAGE. SNRPB is expressed with a -6x His tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
SNRPB is supplied in 20mM HEPES buffer pH-7.5, 0.01mM EDTA and 0.02% SDS.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
SNRPB is one of several nuclear proteins which are found in common among U1, U2, U4/U6, and U5 small ribonucleoprotein particles (snRNPs). These snRNPs are involved in pre-mRNA splicing, and the SNRPB protein may also have a role in pre-mRNA splicing or snRNP structure. SNRPB binds to the downstream cleavage product (DCP) of histone pre-mRNA in a U7 snRNP dependent manner. SNRPB functions in the U7 snRNP complex which is involved in histone 3'-end processing.
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Synonyms
Small nuclear ribonucleoprotein-associated proteins B and B', snRNP-B, Sm protein B/B', Sm-B/B', SmB/B', SNRPB, COD, SNRPB1, SmB/SmB'.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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 :
Noggin Human, Sf9Description:
Noggin Human Recombinant, Sf9
SYM1, SYNS1, NOG.
Product # :
CYT-1119Price :
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Description
Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids and having a molecular mass of 47.9kDa under non-reducing conditions. (Molecular size on SDS-PAGE will appear at approximately 50-80kDa).Noggin is purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20 and 5% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cellsans was fount to be 0.04‑0.2 μg/mL in the presence of 50 ng/mL of Recombinant Human BMP‑4.
More Info
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Introduction
Nogginwhich is encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may play and important role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. Noggin was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. There are several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1). All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Noggin 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
QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC.
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 :
RCVRN MouseDescription:
Recoverin Mouse Recombinant
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.
Product # :
PRO-2547Price :
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Description
Recoverin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-202a.a.) and having a molecular mass of 25.8kDa. Recoverin Mouse is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Recoverin is a member of the recoverin family of neuronal calcium sensors. Recoverin is a heterogeneously acylated calcium-binding and intracellular signal transduction 23kDa protein in the photoreceptor cells of retina. Recoverin contains four EF-hands, of which two bind Ca. Ca-induced extrusion of the acyl group from a hydrophobic cleft in the protein drives the translocation of recoverin from solution to the disc membrane. Recoverin may prolong the termination of the phototransduction cascade in the retina by blocking the phosphorylation of photo-activated rhodopsin. Recoverin plays a key role in the inhibition of rhodopsin kinase, a molecule that regulates the phosphorylation of rhodopsin. This in due course controls the ability of the eye to adapt to, and recover from, exposure to the presence of light. Recoverin is a detectable serologic protein that is expressed in patients with cancer-associated retinopathy, a paraneoplastic syndrome.
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Synonyms
RCV1, Cancer-associated retinopathy protein, Protein CAR, RCVRN, Recoverin, S-modulin.
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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 MGSMGNSKSG ALSKEILEEL QLNTKFTEEE LSAWYQSFLK ECPSGRITRQ EFESIYSKFF PDSDPKAYAQ HVFRSFDANS DGTLDFKEYV IALHMTTAGK PTQKLEWAFS LYDVDGNGTI SKNEVLEIVM AIFKMIKPED VKLLPDDENT PEKRAEKIWA FFGKKEDDKL TEEEFIEGTL ANKEILRLIQ FEPQKVKERI KEKKQ.
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 :
RPS16 HumanDescription:
Ribosomal Protein S16 Human Recombinant
Ribosomal Protein S16, 40S Ribosomal Protein S16, S16.
Product # :
PRO-1555Price :
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Description
RPS16 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-146) and having a molecular mass of 18.8kDa.RPS16 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RPS16 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Ribosomes are the organelles which catalyze protein synthesis and comprised of a small 40S subunit and a large 60S subunit. Combined, the small 40S and large 60S subunits are composed of 4 RNA types and about 80 structurally distinct proteins. RPS16, a ribosomal protein, is a component of the 40S subunit and a member of the S9P family of ribosomal proteins. RPS16 is situated in the cytoplasm. Just like other genes encoding ribosomal proteins, there are numerous processed pseudogenes of RPS16 spread through the genome.
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Synonyms
Ribosomal Protein S16, 40S Ribosomal Protein S16, S16.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPSKGPL QSVQVFGRKK TATAVAHCKR GNGLIKVNGR PLEMIEPRTL QYKLLEPVLL LGKERFAGVD IRVRVKGGGH VAQIYAIRQS ISKALVAYYQ KYVDEASKKE IKDILIQYDR TLLVADPRRC ESKKFGGPGA RARYQKSYR
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 :
HCV NS4 a+b RhodamineDescription:
Hepatitis C Virus NS4 a+b Rhodamine Labeled Recombinant
Product # :
HCV-226Price :
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Description
The E.coli derived 19 kDa recombinant protein rhodamine labeled contains the HCV NS4 immunodominant regions, amino acids 1658-1863. The protein is fused with b-galactosidase (114 kDa) at N-terminus.
Formulation
20mM Tris-Hcl pH 8, 8M urea and 10mM B-ME.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6). -
Stability
HCV NS4 a+b Rhodamine although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Antigen in ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
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Specificity
Immunoreactive with sera of HCV-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 :
SPP1 HumanDescription:
Osteopontin Human Recombinant
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
Product # :
CYT-635Price :
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Description
Secreted Phosphoprotein-1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 321 amino acids fragment (17-314) and having a total molecular mass of 36.2 kDa(molecular weight on SDS-PAGE will shift up). The SPP1 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Osteopontin is supplied in 20mM Tris-HCl buffer pH-7.5, 1mM DTT, 2mM EDTA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases. -
Synonyms
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
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Physical Appearance
Sterile Filtered clear 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 RSMIPVKQAD SGSSEEKQLY NKYPDAVATW LNPDPSQKQN LLAPQNAVSS EETNDFKQET LPSKSNESHD HMDDMDDEDD DDHVDSQDSI DSNDSDDVDD TDDSHQSDES HHSDESDELV TDFPTDLPAT EVFTPVVPTV DTYDGRGDSV VYGLRSKSKK FRRPDIQYPD ATDEDITSHM ESEELNGAYK AIPVAQDLNA PSDWDSRGKD SYETSQLDDQ SAETHSHKQS RLYKRKANDE SNEHSDVIDS QELSKVSREF HSHEFHSHED MLVVDPKSKE EDKHLKFRIS HELDSASSEV N.
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 :
NANA E.ColiDescription:
N-Acetylneuraminate Lyase E.Coli Recombinant
N-acetylneuraminate lyase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, NALase, Sialate lyase, Sialic acid aldolase, Sialic acid lyase, nanA, npl, b3225, JW3194.
Product # :
ENZ-128Price :
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Description
NANA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a.) and having a molecular mass of 34.7kDa.NANA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NANA protein solution (1mg/ml) 20mM Tris-HCl buffer (pH8.0) and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
N-acetylneuraminate lyase (NanA) is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NanA catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. NanA is inhibited by reduction with NaBH4 in the presence of the substrate, which indicates that it belongs to the Schiff-base-forming Class I aldolases. NanA is strongly inhibited by Cu2+ ions, p-chloromercuribenzoate and N-bromosuccinimide, it is also inhibited competitively by the reaction product, pyruvate, and its structurally related compounds, dihydroxyacetone and DL-glyceraldehyde.
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Synonyms
N-acetylneuraminate lyase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, NALase, Sialate lyase, Sialic acid aldolase, Sialic acid lyase, nanA, npl, b3225, JW3194.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATNLRGVMA ALLTPFDQQQ ALDKASLRRL VQFNIQQGID GLYVGGSTGE AFVQSLSERE QVLEIVAEEA KGKIKLIAHV GCVSTAESQQ LAASAKRYGF DAVSAVTPFY YPFSFEEHCD HYRAIIDSAD GLPMVVYNIP ALSGVKLTLD QINTLVTLPG
VGALKQTSGD LYQMEQIRRE HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VKALKEGDIQ TAQKLQTECN KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFGPVDEK YLPELKALAQ QLMQERG.
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 :
CXCL7 95 a.a HumanDescription:
Neutrophil Activating Protein-2 (CXCL7) Human Recombinant, 95 a.a.
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
Product # :
CHM-277Price :
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Description
NAP 2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (35-128) and having a molecular mass of 10.3 kDa.The NAP 2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAP 2 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-7.5, 1mM DTT and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.
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Synonyms
Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.
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Physical Appearance
NAP 2 is supplied as a sterile filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD
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Background
What is the molecular weight/Mw of CXCL7 95 A.A HUMAN Protein?
CXCL7 95 A.A HUMAN Protein has a total Mw of 10.3kDa.
What is the source or expression system of CXCL7 95 A.A HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL7 95 A.A HUMAN Protein?
CXCL7 95 A.A HUMAN Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL7 95 A.A HUMAN Protein?
The biological functionality of CXCL7 95 A.A HUMAN Protein will be determined in the future.
What is the amino acid sequence of CXCL7 95 A.A HUMAN Protein?
MSSTKGQTKR NLAKGKEESL DSDLYAELRC MCIKTTSGIH PKNIQSLEVI GKGTHCNQVE VIATLKDGRK ICLDPDAPRI KKIVQKKLAG DESAD
What applications can CXCL7 95 A.A HUMAN Protein be used in?
CXCL7 95 A.A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL7 95 A.A HUMAN Protein?
The endotoxin level is minimal, CXCL7 95 A.A 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 :
DNAL1 HumanDescription:
Dynein Axonemal Light Chain 1 Human Recombinant
Dynein light chain 1, axonemal, C14orf168, CILD16, DNAL1.
Product # :
PRO-1357Price :
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Description
DNAL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 213 amino acids (1-190) and having a molecular mass of 23.9 kDa. DNAL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The DNAL1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Dynein Axonemal Light Chain 1 (DNAL1) functions as a component of the outer dynein arms complex. DNAL1 acts as the molecular motor which supplies the force to move cilia in an ATP-dependent manner. DNAL1 is expressed in tissues with motile cilia or flagella and takes part in the movement of sperm flagella. Alternate splicing results in numerous transcript variants.
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Synonyms
Dynein light chain 1, axonemal, C14orf168, CILD16, DNAL1.
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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 MGSMAKATTI KEALARWEEK TGQRPSEAKE IKLYAQIPPI EKMDASLSML ANCEKLSLST NCIEKIANLN GLKNLRILSL GRNNIKNLNG LEAVGDTLEE LWISYNFIEK LKGIHIMKKL KILYMSNNLV KDWAEFVKLA ELPCLEDLVF VGNPLEEKHS AENNWIEEAT KRVPKLKKLD GTPVIKGDEE EDN.
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 :
ARL2BP HumanDescription:
ADP-Ribosylation Factor-Like 2 Binding Protein Human Recombinant
ADP-ribosylation factor-like protein 2-binding protein, ARF-like 2-binding protein, Binder of ARF2 protein 1, ARL2BP, BART, BART1.
Product # :
PRO-274Price :
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Description
ARL2BP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-163) and having a molecular mass of 20.9 kDa. The ARL2BP is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ARL2BP solution (1 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5) and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ARL2BP is an effector of ADP-ribosylation factor-like 2(ARL2) which is vital for nuclear retention of STAT3. The ARL2BP protein binds to ARL2.GTP with high affinity but does not interact with ARL2.GDP, activated ARF, or RHO proteins. Though primarily cytosolic, ARL2BP can enter the mitochondria and bind the adenine nucleotide transporter while bound to ARL2. Accordingly, it may also be involved in mitochondria transport and apoptosis.
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Synonyms
ADP-ribosylation factor-like protein 2-binding protein, ARF-like 2-binding protein, Binder of ARF2 protein 1, ARL2BP, BART, BART1.
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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 MDALEGESFA LSFSSASDAE FDAVVGYLED IIMDDEFQLL QRNFMDKYYL EFEDTEENKL IYTPIFNEYI SLVEKYIEEQ LLQRIPEFNM AAFTTTLQHH KDEVAGDIFD MLLTFTDFLA FKEMFLDYRA EKEGRGLDLS SGLVVTSLCK SSSLPASQNN LRH.
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 :
NMI HumanDescription:
N-Myc Interactor Human Recombinant
N-myc (and STAT) Interactor.
Product # :
PRO-070Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NMI produced in E.Coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-307a.a.) and having a molecular mass of 37.2kDa.NMI is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NMI protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT and 20% glycerol.Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
N-myc-interactor belongs to the oncogene Myc family which has a significant part in cell proliferation, differentiation, and neoplastic transformation. In Addition, NMI cooperates with all STATs except STAT2 and augments STAT-mediated transcription in response to cytokines IL2 and IFN-gamma. The NMI mRNA is expressed in small quantities in all human fetal and adult tissues tested except brain and but in large quantities in cancer cell line-myeloid leukemias.
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Synonyms
N-myc (and STAT) Interactor.
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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 MEADKDDTQQ ILKEHSPDEF IKDEQNKGLI DEITKKNIQLK KEIQKLETE LQEATKEFQI KEDIPETKMK FLSVETPEND SQLSNISCSF QVSSKVPYEI QKGQALITFE KEEVAQNVVS MSKHHVQIKDV NLEVTAKPV PLNSGVRFQV YVEVSKMKIN VTEIPDTLRE DQMRDKLELS FSKSRNGGGE VDRVDYDRQS GSAVITFVEI GVADKILKKKEYPLYINQTC HRVTVSPYTE IHLKKYQIFS GTSKRTVLLT GMEGIQMDEE IVEDLINIHF QRAKNGGGEV DVVKCSLGQP HIAYFEE
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 :
NUDCD2 HumanDescription:
NudC Domain Containing 2 Human Recombinant
NudC Domain Containing 2, NudC Domain-Containing Protein 2, NudC-Like Protein 2.
Product # :
PRO-1881Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NUDCD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (1-157 a.a) and having a molecular mass of 20kDa.NUDCD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NUDCD2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
NudC Domain Containing 2 also known as NUDCD2 contains 1 CS domain and interacts with LIS1. NUDCD2 regulates the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone.
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Synonyms
NudC Domain Containing 2, NudC Domain-Containing Protein 2, NudC-Like Protein 2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSAPFEE RSGVVPCGTP WGQWYQTLEE VFIEVQVPPG TRAQDIQCGL QSRHVALSVG GREILKGKLF DSTIADEGTW TLEDRKMVRI VLTKTKRDAA NCWTSLLESE YAADPWVQDQ MQRKLTLERF QKENPGFDFS GAEISGNYTK GGPDFSNLEK
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 :
NUTF2 HumanDescription:
Nuclear Transport Factor 2 Human Recombinant
Nuclear transport factor 2, NTF-2, Placental protein 15, PP15, NUTF2, NTF2.
Product # :
PRO-844Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NUTF2 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids (1-127 a.a.) and having a molecular mass of 16.6 kDa. The NUTF2 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NUTF2 Human solution containing 20mM Tris HCL pH-8, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NUTF2 assists in protein transport into the nucleus and interacts with the nucleoporin p62 and with Ran. NUTF2 plays a role at a relatively late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope. NUTF2 is part of a multicomponent system of cytosolic factors that come together at the pore complex during nuclear import.
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Synonyms
Nuclear transport factor 2, NTF-2, Placental protein 15, PP15, NUTF2, NTF2.
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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 MGDKPIWEQI GSSFIQHYYQ LFDNDRTQLG AIYIDASCLT WEGQQFQGKA AIVEKLSSLP FQKIQHSITA QDHQPTPDSC IISMVVGQLK ADEDPIMGFH QMFLLKNIND AWVCTNDMFR LALHNFG.
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.