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1000 results found for “ferritin”
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Name :
EIF3I Human, Sf9Description:
Eukaryotic Translation Initiation Factor 3I Human Recombinant, Sf9
eIF3-beta, eIF3-p36, EIF3S2, PRO2242, TRIP-1, TRIP1, Eukaryotic translation initiationfactor 3 subunit I, eIF3i, TGF-beta receptor-interacting protein 1, eIF-3-beta.
Product # :
PRO-2611Price :
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Shipped with Ice Packs
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Description
EIF3I Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (1-325 a.a) and having a molecular mass of 37.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).EIF3I is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EIF3I protein solution (0.25mg/ml) 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% Glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Eukaryotic translation initiation factor 3, subunit I (EIF3I) is part of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is essential for numerous steps in the initiation of protein synthesis. The eIF-3 complex links with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2: GTP: methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also essential for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3I are clonorchiasis, and tonsillitis.
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Synonyms
eIF3-beta, eIF3-p36, EIF3S2, PRO2242, TRIP-1, TRIP1, Eukaryotic translation initiation
factor 3 subunit I, eIF3i, TGF-beta receptor-interacting protein 1, eIF-3-beta. -
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
MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA
DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC
FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV
LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN
YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY SSGGEDGYVR IHYFDPQYFE FEFEAHHHHH 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 :
SPINT2 HumanDescription:
Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant
DIAR3, FLJ45571, HAI-2, HAI2, Kop, PB, Kunitz-type protease inhibitor 2, Hepatocyte growth factor activator inhibitor type 2, Placental bikunin, SPINT2.
Product # :
PRO-1296Price :
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Description
SPINT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (28-197 a.a.) and having a molecular mass of 21.8kDa.SPINT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SPINT2 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
SPINT2 is a transmembrane protein acts as an inhibitor of HGF activator. SPINT2 inhibits plasmin, plasma and tissue kallikrein, and factor XIa. SPINT2 has two extracellular Kunitz domains that inhibit few serine proteases. SPINT2 is assumed tumor suppressor, mutations in SPINT2 leads to a congenital sodium diarrhea.
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Synonyms
DIAR3, FLJ45571, HAI-2, HAI2, Kop, PB, Kunitz-type protease inhibitor 2, Hepatocyte growth factor activator inhibitor type 2, Placental bikunin, SPINT2.
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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 MGSHMADRER SIHDFCLVSK VVGRCRASMP RWWYNVTDGS CQLFVYGGCD GNSNNYLTKE ECLKKCATVT ENATGDLATS RNAADSSVPS APRRQDSEDH SSDMFNYEEY CTANAVTGPC RASFPRWYFD VERNSCNNFI YGGCRGNKNS YRSEEACMLR CFRQQENPPL PLGSK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NTS Human, sf9Description:
Neurotensin Human Recombinant, sf9
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
Product # :
PRO-2374Price :
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Description
NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NTS protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
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Synonyms
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OSM RatDescription:
Oncostatin-M Rat Recombinant
Oncostatin-M, OSM, OncoM.
Product # :
CYT-169Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
OSM Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 214 amino acids and having a molecular mass of 24.3kDa.The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of rat C6 cells is < 5.0 µg/ml, corresponding to a specific activity of > 200 units/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
Oncostatin-M, OSM, OncoM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M 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
KRGCSSSSPK LLSQLKSQAN ITGNTASLLE PYILHQNLNT LTLRAACTEH PVAFPSEDML RQLSKPDFLS TVHATLGRVW HQLGAFRQQF PKIQDFPELE RARQNIQGIR NNVYCMARLL HPPLEIPEPT QADSGTSRPT TTAPGIFQIK IDSCRFLWGY HRFMGSVGRV FEEWGDGSRR SR RHSPLWAW LKGDHRIRPS RSSQSAMLRS LVPR.
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 :
STMN3 HumanDescription:
Stathmin Like-3 Human Recombinant
Stathmin-3, SCG10-like protein, STMN3, SCLIP
Product # :
PRO-838Price :
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Shipped with Ice Packs
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Description
STMN3 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (39-180 a.a.) and having a molecular mass of 18.9 kDa. The STMN3 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STMN3 Human solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
STMN3 is a neuronal specific protein which belongs to the stathmin/oncoprotein 18 family of microtubule-destabilizing phosphoproteins. It is similar to the SCG10 protein and is involved in signal transduction and regulation of microtubule dynamics.
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Synonyms
Stathmin-3, SCG10-like protein, STMN3, SCLIP
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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 MDMEVKQLDK RASGQSFEVI LKSPSDLSPE SPMLSSPPKK KDTSLEELQK RLEAAEERRK TQEAQVLKQL AERREHEREV LHKALEENNN FSRQAEEKLN YKMELSKEIR EAHLAALRER LREKELHAAE VRRNKEQREE MSG.
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 :
FAM19A5 HumanDescription:
Family With Sequence Similarity 19 Member-A5 Human Recombinant
Family With Sequence Similarity 19 (Chemokine (C-C Motif)-Like), Member A5, Chemokine-Like Protein TAFA-5, TAFA5, TAFA Protein 5, QLLK5208, UNQ5208, TAFA-5, FAM19A5.
Product # :
CHM-284Price :
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Shipped with Ice Packs
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Description
FAM19A5 Human Recombinant (isoform 2) produced in E.Coli is a single, non-glycosylated, polypeptide chain (Gln26-Ser125) containing 110 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 12.2kDa.
Source
Escherichia Coli.
Formulation
FAM19A5 filtered (0.4µm) solution in 20mM Tris buffer, 50mM NaCl, pH 7.5 and 10% (w/v) glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Family With Sequence Similarity 19 Member-A5 (FAM19A5) belongs to the TAFA family which is comprised of 5 highly homologous genes encoding small secreted proteins. These proteins have conserved cysteine residues at fixed positions, and are remotely related to MIP-1alpha, which is a member of the CC-chemokine family. The TAFA proteins are primarily expressed in specific regions of the brain, and are assumed to serve as brain-specific chemokines or neurokines which act as regulators of immune and nervous cells.
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Synonyms
Family With Sequence Similarity 19 (Chemokine (C-C Motif)-Like), Member A5, Chemokine-Like Protein TAFA-5, TAFA5, TAFA Protein 5, QLLK5208, UNQ5208, TAFA-5, FAM19A5.
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Physical Appearance
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
MKHHHHHHASQFLKEGQLAA GTCEIVTLDR DSSQPRRTIA RQTARCACRK GQIAGTTRAR PACVDARIIK TKQWCDMLPC LEGEGCDLLI NRSGWTCTQP GGRIKTTTVS.
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Background
What is the molecular weight/Mw of FAM19A5 HUMAN Protein?
FAM19A5 HUMAN Protein has a total Mw of 12.2kDa.
What is the source or expression system of FAM19A5 HUMAN Protein?
Escherichia Coli.
What is the Purity of FAM19A5 HUMAN Protein?
FAM19A5 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FAM19A5 HUMAN Protein?
The biological functionality of FAM19A5 HUMAN Protein will be determined in the future.
What is the amino acid sequence of FAM19A5 HUMAN Protein?
MKHHHHHHASQFLKEGQLAA GTCEIVTLDR DSSQPRRTIA RQTARCACRK GQIAGTTRAR PACVDARIIK TKQWCDMLPC LEGEGCDLLI NRSGWTCTQP GGRIKTTTVS.
What applications can FAM19A5 HUMAN Protein be used in?
FAM19A5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FAM19A5 HUMAN Protein?
The endotoxin level is minimal, FAM19A5 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 :
FAM3B HumanDescription:
Family with Sequence Similarity 3, Member B Human Recombinant
Family with Sequence Similarity 3 member B, C21orf11, C21orf76, Cytokine-like protein 2-21, ORF9, PANDER, PRED44, Chromosome 21 open reading frame 11, Pancreatic-derived factor.
Product # :
PRO-139Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
FAM3B Protein is a 24.1 kDa protein containing 216 amino acids fused to a 10 aa N-Terminal His-tag
Source
E. coli
Formulation
FAM3B Human was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS, 50mM NaCl, pH 7.5
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
FAM3B Protein induces apoptosis of alpha and beta cells in a quantity and time dependent way.
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Synonyms
Family with Sequence Similarity 3 member B, C21orf11, C21orf76, Cytokine-like protein 2-21, ORF9, PANDER, PRED44, Chromosome 21 open reading frame 11, Pancreatic-derived factor.
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Stability
Store lyophilized FAM3B uman at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted FAM3B an be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS ELIPDAPLSS AAYSIRSIGE RPVLKAPVPK RQKCDHWTPC PSDTYAYRLL SGGGRSKYAK ICFEDNLLMG EQLGNVARGI NIAIVNYVTG NVTATRCFDM YEGDNSGPMT KFIQSAAPKS LLFMVTYDDG STRLNNDAKN AIEALGSKEI RNMKFRSSWV FIAAKGLELP SEIQREKINH SDAKNNRYSG WPAEIQIEGC IPKERS
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 :
FBXO2 HumanDescription:
F-Box Protein 2 Human Recombinant
F-box only protein 2, FBXO2, F-Box Protein 2, FBX2, FBG1, Fbs1, NFB42, OCP1.
Product # :
PRO-2017Price :
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Shipped with Ice Packs
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Description
FBXO2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 319 amino acids (1-296 a.a.) and having a molecular mass of 35.7kDa.FBXO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FBXO2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
F-Box Protein 2 (FBXO2) is a part of the F-box protein family. The F-box proteins are one of the 4 subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which takes part in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes. FBXO2 belongs to the Fbxs class which contains either different protein-protein interaction modules or no recognizable motifs. FBXO2 is extremely similar to the rat neural F Box 42 kDa protein which is enriched in the nervous system and plays a role in maintaining neurons in a postmitotic state.
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Synonyms
F-box only protein 2, FBXO2, F-Box Protein 2, FBX2, FBG1, Fbs1, NFB42, OCP1.
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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 MGSMDGDGDP ESVGQPEEAS PEEQPEEASA EEERPEDQQE EEAAAAAAYL DELPEPLLLR VLAALPAAEL VQACRLVCLR WKELVDGAPL WLLKCQQEGL VPEGGVEEER DHWQQFYFLS KRRRNLLRNP CGEEDLEGWC DVEHGGDGWR VEELPGDSGV EFTHDESVKK YFASSFEWCR KAQVIDLQAE GYWEELLDTT QPAIVVKDWY SGRSDAGCLY ELTVKLLSEH ENVLAEFSSG QVAVPQDSDG GGWMEISHTF TDYGPGVRFV RFEHGGQDSV YWKGWFGARV TNSSVWVEP.
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 :
PF4V1 HumanDescription:
Platelet Factor 4 Variant 1 Human Recombinant
PF4V1, Platelet Factor 4 Variant 1, CXCL4L1, CXCL4V1, PF4alt, PF4var1, SCYB4V1, PF4-ALT, PF4A, C-X-C Motif Chemokine 4, Platelet Factor 4 Variant, Platelet Factor 4, Variant 1 (PF4-Like) , C-X-C Motif Chemokine 4 Variant.
Product # :
CHM-027Price :
Quantity :
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Shipped with Ice Packs
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Description
PF4V1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (31-104 a.a.) and having a molecular mass of 10.6kDa.PF4V1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PF4V1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Platelet Factor 4 Variant 1 (PF4V1) is a member of the intercrine alpha (chemokine CxC) family. PF4V1 is an inhibitor of angiogenesis and inhibitor of endothelial cell chemotaxis (in vitro).
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Synonyms
PF4V1, Platelet Factor 4 Variant 1, CXCL4L1, CXCL4V1, PF4alt, PF4var1, SCYB4V1, PF4-ALT, PF4A, C-X-C Motif Chemokine 4, Platelet Factor 4 Variant, Platelet Factor 4, Variant 1 (PF4-Like) , C-X-C Motif Chemokine 4 Variant.
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Physical Appearance
Sterile Filtered colorless clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. 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 MGSFARAEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.
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 :
PIGR HumanDescription:
Polymeric Immunoglobulin Receptor Human Recombinant
Polymeric immunoglobulin receptor, PIGR, PIgR, Poly-Ig receptor, Hepatocellular carcinoma-associated protein TB6, polymeric immunoglobulin receptor precursor.
Product # :
PRO-2671Price :
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Shipped with Ice Packs
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Description
PIGR Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 629 amino acids (19-638 aa) and having a molecular mass of 68.9 kDa.PIGR is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PIGR protein solution (1mg/ml) containing Phosphate-Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human IgM. The ED50 range ≤10 ug/ml.
More Info
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Introduction
Polymeric immunoglobulin receptor (PIGR) is responsible for transcytosis of soluble dimeric IgAs and immune. PIGR binds polymeric IgA and IgM at the basolateral surface of epithelial cells, then the complex is transported across the cell to be secreted at the apical surface.cytokines, hormones, and pathogenic stimuliregulate PIGR expression. The expression of PIGR is critically regulated by the pro-inflammatory cytokines, such as IL-1, IL-4, TNF-α, and IFN-γ.
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Synonyms
Polymeric immunoglobulin receptor, PIGR, PIgR, Poly-Ig receptor, Hepatocellular carcinoma-associated protein TB6, polymeric immunoglobulin receptor precursor.
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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
ADLKSPIFGP EEVNSVEGNS VSITCYYPPT SVNRHTRKYW CRQGARGGCI TLISSEGYVS SKYAGRANLT NFPENGTFVV NIAQLSQDDS GRYKCGLGIN SRGLSFDVSL EVSQGPGLLN DTKVYTVDLG RTVTINCPFK TENAQKRKSL YKQIGLYPVL VIDSSGYVNP NYTGRIRLDI QGTGQLLFSV VINQLRLSDA GQYLCQAGDD SNSNKKNADL QVLKPEPELV YEDLRGSVTF
HCALGPEVAN VAKFLCRQSS GENCDVVVNT LGKRAPAFEG RILLNPQDKD GSFSVVITGL RKEDAGRYLC GAHSDGQLQE GSPIQAWQLF VNEESTIPRS PTVVKGVAGG SVAVLCPYNR KESKSIKYWC LWEGAQNGRC PLLVDSEGWV KAQYEGRLSL LEEPGNGTFT VILNQLTSRD AGFYWCLTNG DTLWRTTVEI KIIEGEPNLK VPGNVTAVLG ETLKVPCHFP CKFSSYEKYW
CKWNNTGCQA LPSQDEGPSK AFVNCDENSR LVSLTLNLVT RADEGWYWCG VKQGHFYGET AAVYVAVEER KAAGSRDVSL AKADAAPDEK VLDSGFREIE NKAIQDPRLF AEEKAVADTR DQADGSRASV DSGSSEEQGG SSRHHHHHH
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 :
FLT1 Human, HisDescription:
Vascular Endothelial Growth Factor receptor-1 Human Recombinant, His Tag
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Product # :
PKA-354Price :
Quantity :
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Shipped with Ice Packs
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Description
FLT1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 298 amino acids fragment (31-328) corresponding to the IgG like domains 1-3 from the mature soluble FLT1 protein, having a total molecular mass of 43kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The FLT1 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FLT1 His-Tag protein is supplied in 1x PBS and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
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Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
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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.
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 :
TREM2 Human, HEKDescription:
Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant, HEK
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
Product # :
PRO-2773Price :
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Description
TREM2 Human Recombinant is a single, glycosylated, polypeptide chain (19-174 a.a) containing a total of 162 amino acids, having a molecular mass of 18.2 kDa. TREM2 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The TREM2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
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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
HNTTVFQGVA GQSLQVSCPY DSMKHWGRRK AWCRQLGEKG PCQRVVSTHN LWLLSFLRRW NGSTAITDDT LGGTLTITLR NLQPHDAGLY QCQSLHGSEA DTLRKVLVEV LADPLDHRDA GDLWFPGESE SFEDAHVEHS ISRSLLEGEI PFPPTSHHHH HH.
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Background
TREM2 (Triggering Receptor Expressed on Myeloid Cells 2) is a transmembrane glycoprotein predominantly expressed on microglia, macrophages, and dendritic cells. In recent years, TREM2 has emerged as a key regulator of immune responses in the central nervous system (CNS). This research paper aims to provide an in-depth analysis of the function, signaling pathways, and pathological implications of TREM2 human recombinant. Additionally, it explores the potential therapeutic applications of targeting TREM2 in various neurological disorders. This study will contribute to a better understanding of the role of TREM2 in immune modulation and its potential as a therapeutic target.
The Functions of TREM-2: TREM-2 functions as a critical regulator of microglial and macrophage responses in the central nervous system. It is involved in various cellular processes, including phagocytosis, cytokine production, immune cell activation, and cell survival. Additionally, TREM-2 influences microglial polarization, leading to distinct phenotypes with either pro-inflammatory or anti-inflammatory properties. Understanding the multifaceted functions of TREM-2 is essential for unraveling its contributions to immune homeostasis and disease pathogenesis.
Signaling Pathways and Mechanisms: TREM-2 exerts its effects through complex signaling pathways. Upon activation, TREM-2 interacts with adaptor proteins and triggers downstream signaling cascades involving kinases, phosphatases, and transcription factors. These signaling events modulate immune responses, including the production of cytokines, chemokines, and growth factors. Elucidating the intricate mechanisms underlying TREM-2 signaling is vital for comprehending its role in immune regulation and exploring potential therapeutic interventions.
Implications in Neurodegenerative Diseases: TREM-2 has emerged as a key player in neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and frontotemporal dementia. Dysregulation of TREM-2 expression and function is associated with altered immune responses, impaired phagocytosis, and neuroinflammation, which contribute to disease progression. Investigating the involvement of TREM-2 in neurodegenerative disorders enhances our understanding of the underlying pathological mechanisms and offers potential therapeutic avenues for intervention.
Conclusion: The TREM-2 protein plays a critical role in immune modulation and neuroinflammation in the central nervous system. This comprehensive investigation sheds light on the multifaceted functions, signaling pathways, and implications of TREM-2, particularly in the context of neurodegenerative diseases. Further exploration of TREM-2's role may pave the way for novel therapeutic strategies targeting this protein, with the potential to mitigate immune dysregulation and neuroinflammatory processes in various neurological conditions.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on TREM-2 for a comprehensive list of references and sources.
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 :
M CSF Rat HEKDescription:
Macrophage Colony Stimulating Factor Rat Recombinant HEK
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
Product # :
CYT-046Price :
Quantity :
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Description
MCSF Rat Recombinant produced in HEK-293 cells is a secreted protein (amino acids Glu33-Arg254). M-CSF is disulfide-linked homodimer containing 2 x 222 a.a chains.
Source
HEK293
Formulation
The recombinant MCSF was lyophilized after extensive dialysis against PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of mouse M-NFS-60 cells.More Info
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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
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Synonyms
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 MCSF in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Clusterin MouseDescription:
Apolipoprotein-J Mouse Recombinant
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
Product # :
CYT-1172Price :
Quantity :
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Shipped at Room temp
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Description
Clusterin Mouse Recombinant is a single, glycosylated polypeptide chain containing 433 amino acids (22-448a.a) and having a molecular mass of 50.2kDa (calculated). Clusterin is fused to a 6 a.a His tag at C-terminal.
Source
HEK293
Formulation
Clusterin filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer and 50 mM NaCl, pH 7.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Clusterin also known as Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by 5 disulfide bridges and are flanked by 2 predicted coiled-coil a-helices and 3 predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% -80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
Clusterin is up/down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others. -
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
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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.
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Amino Acid Sequence
EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH
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Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 50.2kDa.
What is the source or expression system of CLUSTERIN Protein?
HEK293
What is the Purity of CLUSTERIN Protein?
CLUSTERIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CLUSTERIN Protein?
The biological functionality of CLUSTERIN Protein will be determined in the future.
What is the amino acid sequence of CLUSTERIN Protein?
EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH
What applications can CLUSTERIN Protein be used in?
CLUSTERIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin qA Ovine, PEGDescription:
Leptin Quadruple Antagonist Pegylated Ovine Recombinant
Product # :
CYT-1246Price :
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Description
Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CFB Human, NativeDescription:
Complement Factor B Human
CFB, C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, BF, BFD, AHUS4, ARMD14, CFAB, CFBD, FB, FBI12, GBG, H2-Bf.
Product # :
PRO-2698Price :
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Description
Human Complement Factor B produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 93kDa.
Source
Human Plasma.
Formulation
CFB protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.
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Synonyms
CFB, C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, BF, BFD, AHUS4, ARMD14, CFAB, CFBD, FB, FBI12, GBG, H2-Bf.
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Physical Appearance
Sterile filtered solution.
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Stability
CFB Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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 :
HBXIP HumanDescription:
Hepatitis B Virus x Interacting Protein Human Recombinant
Ragulator complex protein LAMTOR5, Hepatitis B virus X-interacting protein, HBV X-interacting protein, HBX-interacting protein, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5, LAMTOR5, HBXIP, XIP.
Product # :
HBV-235Price :
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Description
HBXIP Human Recombinant produced in E. coli is a single polypeptide chain containing 197 amino acids (aa 1-173) and having a molecular mass of 20.7kDa.HBXIP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HBXIP solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM EDTA.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Hepatitis B virus x interacting protein (HBXIP) forms a complex with the C-terminus of hepatitis B virus X (HBX) protein. HBXIP negatively regulates HBX activity and changes the replicative life cycle of the virus. Furthermore, HBXIP is involved in bipolar spindle formation and regulates centrosome dynamics and cytokinesis in cells, possibly due to interaction with Dynein light chain. HBXIP is highly expressed in the skeletal and cardiac muscle, followed by pancreas, kidney, liver, brain, placenta and lung. HBXIP has elevated levels in both cancerous and non-cancerous liver tissue of patients with chronic HBV infection compared with hepatic tissue without HBV infection.
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Synonyms
Ragulator complex protein LAMTOR5, Hepatitis B virus X-interacting protein, HBV X-interacting protein, HBX-interacting protein, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5, LAMTOR5, HBXIP, XIP.
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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 MGSHMEPGAG HLDGHRAGSP SLRQALCDGS AVMFSSKERG RCTVINFVPL EAPLRSTPRS RQVTEACGGE GRAVPLGSEP EWSVGGMEAT LEQHLEDTMK NPSIVGVLCT DSQGLNLGCR GTLSDEHAGV ISVLAQQAAK LTSDPTDIPV VCLESDNGNI MIQKHDGITV AVHKMAS.
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 :
MIF RatDescription:
Macrophage Migration Inhibitory Factor Rat Recombinant
Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
Product # :
CYT-193Price :
Quantity :
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Shipped at Room temp
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Description
MIF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa. The MIF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF 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 MIF 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
MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.
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 :
ERH HumanDescription:
Enhancer of Rudimentary Human Recombinant
Enhancer of rudimentary homolog, ERH, DROER, FLJ27340.
Product # :
PRO-121Price :
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Description
ERH 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 127 amino acids (1-104 a.a.) and having a molecular mass of 14.6kDa. The ERH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ERH solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Enhancer of rudimentary homolog (ERH) is a ubiquitously expressed transcriptional coregulator which is highly conserved among eukaryotes. ERH may have a role in cell cycle regulation and pyrimidine biosynthesis. ERH has two casein kinase II phosphorylation sites which are thought to upset the ability of ERH to dimerize.
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Synonyms
Enhancer of rudimentary homolog, ERH, DROER, FLJ27340.
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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 MGSMSHTILL VQPTKRPEGR TYADYESVNE CMEGVCKMYE EHLKRMNPNS PSITYDISQL FDFIDDLADL SCLVYRADTQ TYQPYNKDWI KEKIYVLLRR QAQQAGK.
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 :
IL1F10 Human HisDescription:
Interleukin 1 Family, Member 10 Human Recombinant, His Tag
Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.
Product # :
CYT-783Price :
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Description
IL1F10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-152) and having a molecular mass of 19.1kDa.IL1F10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IL1F10 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Human interleukin family 1, member 10 (IL1F10) belongs to the interleukin 1 cytokine family. IL1F10 is expressed in the fetal skin, spleen and tonsil, generally in the basal epithelia of skin and in proliferating B-cells of the tonsil. IL1F10 binds soluble IL1 receptor type 1 and may be implicated in the regulation of adapted and innate immune responses.
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Synonyms
Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.
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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 MCSLPMARYY IIKYADQKAL YTRDGQLLVG DPVADNCCAE KICTLPNRGL DRTKVPIFLG IQGGSRCLAC VETEEGPSLQ LEDVNIEELY KGGEEATRFT FFQSSSGSAF RLEAAAWPGW FLCGPAEPQQ PVQLTKESEP SARTKFYFEQ SW
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 :
IRF2 HumanDescription:
IFN Regulatory Factor-2 Human Recombinant
IRF-2, IRF2, MAR, DKFZp686F0244, IFN regulatory factor 2.
Product # :
CYT-534Price :
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Shipped with Ice Packs
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- SDS-PAGE
Description
IFN Regulatory Factor-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 133 amino acids (1-113) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml in 20mM Tris pH-8, 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
IFN regulatory factor 2 is a member of the IFN regulatory transcription factor (IRF) family. IRF2 competitively inhibits the IRF1-mediated transcriptional activation of IFNs alpha and beta, and presumably other genes that employ IRF1 for transcription activation. However, IRF2 also functions as a transcriptional activator of histone H4. IRF2 binds to the upstream regulatory region of type-1 IFN and IFN-inducible MHC class-1 genes (the IFN consensus sequence (ics) and represses those genes.
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Synonyms
IRF-2, IRF2, MAR, DKFZp686F0244, IFN regulatory factor 2.
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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 MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMHAARHGWDVEK DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIKKGNNAFRVYR MLP.
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Background
What is the molecular weight/Mw of IRF2 HUMAN Protein?
IRF2 HUMAN Protein has a total Mw of 15kDa.
What is the source or expression system of IRF2 HUMAN Protein?
Escherichia Coli.
What is the Purity of IRF2 HUMAN Protein?
IRF2 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IRF2 HUMAN Protein?
The biological functionality of IRF2 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IRF2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMHAARHGWDVEK DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIKKGNNAFRVYR MLP.
What applications can IRF2 HUMAN Protein be used in?
IRF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IRF2 HUMAN Protein?
The endotoxin level is minimal, IRF2 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 :
HAVCR2 HumanDescription:
Hepatitis A Virus Cellular Receptor 2 Human Recombinant
Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, TIMD-3, T-cell membrane protein 3, TIM-3, HAVCR2, TIM3, TIMD3, TIM3, KIM-3.
Product # :
HAV-224Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
Recombinant Human HAVCR2 produced in E. coli is a single polypeptide chain containing 206 amino acids (aa 22-202) and having a molecular mass of 22.7kDa.HAVCR2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HAVCR2 solution (1mg/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
Hepatitis A Virus Cellular Receptor 2 (HAVCR2) is a member of the immunoglobulin superfamily. HACVR2 controls macrophage activation. HACVR2 inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and stimulates immunological tolerance.
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Synonyms
Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, TIMD-3, T-cell membrane protein 3, TIM-3, HAVCR2, TIM3, TIMD3, TIM3, KIM-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 MGSHMSEVEY RAEVGQNAYL PCFYTPAAPG NLVPVCWGKG ACPVFECGNV VLRTDERDVN YWTSRYWLNG DFRKGDVSLT IENVTLADSG IYCCRIQIPG IMNDEKFNLK LVIKPAKVTP APTLQRDFTA AFPRMLTTRG HGPAETQTLG SLPDINLTQI STLANELRDS RLANDLRDSG ATIRIG.
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 :
ZNF32 HumanDescription:
Zinc Finger Protein 32 Human Recombinant
KOX30, Zinc finger protein 32, C2H2-546, Zinc finger protein KOX30, ZNF32.
Product # :
PRO-1983Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
ZNF32 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273 a.a) and having a molecular mass of 33.4kDa. ZNF32 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ZNF32 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Zinc Finger Protein 32 (ZNF32) is a part of the krueppel C2H2-type zinc-finger protein family. ZNF32 which contains seven C2H2-type zinc fingers takes part in transcriptional regulation.
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Synonyms
KOX30, Zinc finger protein 32, C2H2-546, Zinc finger protein KOX30, ZNF32.
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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 MGSMFGFPTA TLLDCHGRYA QNVAFFNVMT EAHHKYDHSE ATGSSSWDIQ NSFRREKLEQ KSPDSKTLQE DSPGVRQRVY ECQECGKSFR QKGSLTLHER IHTGQKPFEC THCGKSFRAK GNLVTHQRIH TGEKPYQCKE CGKSFSQRGS LAVHERLHTG QKPYECAICQ RSFRNQSNLA VHRRVHSGEK PYRCDQCGKA FSQKGSLIVH IRVHTGLKPY ACTQCRKSFH TRGNCILHGK IHTGETPYLC GQCGKSFTQR GSLAVHQRSC SQRLTL.
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 :
SBDS HumanDescription:
Shwachman-Bodian-Diamond Syndrome Human Recombinant
SDS, SWDS, Shwachman-Bodian-Diamond syndrome, Ribosome Maturation protein SBDS.
Product # :
PRO-272Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
SBDS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids (1-250a.a.) and having a molecular mass of 30.9kDa.SBDS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SBDS protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 2mM DTT, 50mM NaCl, 0.1mM EDTA, and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
SBDS is part of an extremely preserved protein family which exists from archaea to vertebrates and plants. SBDS protein functions in RNA metabolism and has a role in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Shwachman-Diamond syndrome is a rare autosomal recessive disorder produced by mutations in the SBDS gene.
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Synonyms
SDS, SWDS, Shwachman-Bodian-Diamond syndrome, Ribosome Maturation protein SBDS.
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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 MSIFTPTNQI RLTNVAVVRM KRAGKRFEIA CYKNKVVGWR SGVEKDLDEV LQTHSVFVNV SKGQVAKKED LISAFGTDDQ TEICKQILTK GEVQVSDKER HTQLEQMFRD IATIVADKCV NPETKRPYTV ILIERAMKDI HYSVKTNKST KQQALEVIKQ LKEKMKIERA HMRLRFILPV NEGKKLKEKL KPLIKVIESE DYGQQLEIVC LIDPGCFREI DELIKKETKG KGSLEVLNLK DVEEGDEKFE
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.