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1000 results found for “Hepatocyte Growth Factor”
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Name :
HSF2BP HumanDescription:
Heat Shock Transcription Factor 2 Binding Protein Human Recombinant
Heat Shock Transcription Factor 2 Binding Protein, Heat Shock Factor 2 Binding Protein, HSF2BP.
Product # :
HSP-062Price :
Quantity :
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Shipped with Ice Packs
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Description
HSF2BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-334 a.a) and having a molecular mass of 40kDa.HSF2BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HSF2BP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 30% glycerol and 2mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HSF2BP, also known as HSF2 binding protein links with HSF2. This interaction takes place between the trimerization domain of HSF2 and the amino terminal hydrophilic region of HSF2BP which contains two leucine zipper motifs. Therefore, HSF2BP is involved in modulating HSF2 activation.
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Synonyms
Heat Shock Transcription Factor 2 Binding Protein, Heat Shock Factor 2 Binding Protein, HSF2BP.
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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 MGSMGEAGAA EEACRHMGTK EEFVKVRKKD LERLTTEVMQ IRDFLPRILN GEVLESFQKL KIVEKNLERK EQELEQLKMD CEHFKARLET VQADNIREKK EKLALRQQLN EAKQQLLQQA EYCTEMGAAA CTLLWGVSSS EEVVKAILGG DKALKFFSIT GQTMESFVKS LDGDVQELDS DESQFVFALA GIVTNVAAIA CGREFLVNSS RVLLDTILQL LGDLKPGQCT KLKVLMLMSL YNVSINLKGL KYISESPGFI PLLWWLLSDP DAEVCLHVLR LVQSVVLEPE VFSKSASEFR SSLPLQRILA MSKSRNPRLQ TAAQELLEDL RTLEHNV.
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 :
BCAT2 HumanDescription:
Branched Chain Amino-Acid Transaminase 2 Human Recombinant
Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.
Product # :
ENZ-606Price :
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Shipped with Ice Packs
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Description
BCAT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (28-392) and having a molecular mass of 43.9kDa.BCAT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCAT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 10% glycerol, 0.2M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Branched Chain Amino-Acid Transaminase 2 (BCAT2) is a member of the class-IV pyridoxal-phosphate-dependent aminotransferase family. BCAT2 is a branched chain aminotransferase found in mitochondria. BCAT2 forms a dimer which catalyzes the first step in the production of the branched chain amino acids leucine, isoleucine, and valine. In addition, BCAT2 may actn as a transporter of branched chain alpha-keto acids.
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Synonyms
Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.
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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 MGSHMASSSF KAADLQLEMT QKPHKKPGPG EPLVFGKTFT DHMLMVEWND KGWGQPRIQP FQNLTLHPAS SSLHYSLQLF EGMKAFKGKD QQVRLFRPWL NMDRMLRSAM RLCLPSFDKL ELLECIRRLI EVDKDWVPDA AGTSLYVRPV LIGNEPSLGV SQPTRALLFV ILCPVGAYFP GGSVTPVSLL ADPAFIRAWV GGVGNYKLGG NYGPTVLVQQ EALKRGCEQV LWLYGPDHQL TEVGTMNIFV YWTHEDGVLE LVTPPLNGVI LPGVVRQSLL DMAQTWGEFR VVERTITMKQ LLRALEEGRV REVFGSGTAC QVCPVHRILY KDRNLHIPTM ENGPELILRF QKELKEIQYG IRAHEWMFPV.
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 :
C10ORF54 HumanDescription:
Chromosome 10 Open Reading Frame 54 Human Recombinant
C10orf54, Chromosome 10 Open Reading Frame 54, V-Domain Ig Suppressor Of T Cell Activation, Stress-Induced Secreted Protein-1, Sisp-1, SISP1, Stress Induced Secreted Protein 1, Death Domain1alpha, DD1alpha, PP2135, B7-H5, VISTA, B7H5, GI24.
Product # :
PRO-2259Price :
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Description
C10ORF54 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (33-194 a.a) and having a molecular mass of 19.1kDa. (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). C10ORF54 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
C10ORF54 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Chromosome 10 Open Reading Frame 54, also known as C10ORF54 is part of the immunoglobulin superfamily. Like a transmembrane molecule, C10ORF54 is expressed in the bone on embryonic stem cells (ESCs), and on tumor cell surface as well. Accordingly, C10ORF54 supports the differentiation of ESC and ehhances BMP4 induced signaling in ESC, however C10ORF54 is also down regulated following to BMP4 exposure.
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Synonyms
C10orf54, Chromosome 10 Open Reading Frame 54, V-Domain Ig Suppressor Of T Cell Activation, Stress-Induced Secreted Protein-1, Sisp-1, SISP1, Stress Induced Secreted Protein 1, Death Domain1alpha, DD1alpha, PP2135, B7-H5, VISTA, B7H5, GI24.
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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
FKVATPYSLY VCPEGQNVTL TCRLLGPVDK GHDVTFYKTW YRSSRGEVQT CSERRPIRNL TFQDLHLHHG GHQAANTSHD LAQRHGLESA SDHHGNFSIT MRNLTLLDSG LYCCLVVEIR HHHSEHRVHG AMELQVQTGK DAPSNCVVYP SSSQDSENIT AAVEHHHHHH.
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 :
PPARG HumanDescription:
Peroxisome Proliferator Activated Receptor Gamma Human Recombinant
Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.
Product # :
PKA-228Price :
Quantity :
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Description
Peroxisome Proliferator Activated Receptor Gamma Human Recombinant is expressed in E.coli having a molecular weight of 59.2 kDa and fused to an amino terminal hexahistidine tag.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl and 50% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
The peroxisome proliferator activated receptors (PPARs) are ligandactivated transcription factors within the nuclear receptor superfamily, which play important roles in adipogenesis, glucose homeostasis andinflammation. Three different isotypes can be distinguished; alpha, beta and gamma. PPARg, is mainly expressed in adipose tissue and to lesser extent in colon, the immune system and the retina. Whereas PPARg operates in the catabolism of fatty acids in the liver, PPARg influences the storage of fatty acids in the adipose tissue and plays a role in adipocyte differentiation. PPARg binds to DNA as a heterodimer with retinoid X receptor (RXR), activating expression of target genes after binding ligand.
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Synonyms
Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.
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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 :
EEF1G HumanDescription:
Eukaryotic Translation Elongation Factor 1 Gamma Human Recombinant
EF1G, GIG35, Elongation factor 1-gamma, Eukaryotic Translation Elongation Factor 1 Gamma, EEF1G, EF-1-gamma, eEF-1B gamma, PRO1608.
Product # :
PRO-2048Price :
Quantity :
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Shipped with Ice Packs
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Description
EEF1G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 460 amino acids (1-437) and having a molecular mass of 52.5 kDa.EEF1G is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EEF1G solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Eukaryotic Translation Elongation Factor 1 Gamma (EEF1G) takes part in anchoring the complex to additional cellular components. EEF1G is a multi-protein complex which is in charge of the delivery of aminoacyl-tRNAs to the ribosome. Over expression of EEF1G is linked with pancreatic cancer, due to the role of EEF1G protein in the oncogenic transformation process.
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Synonyms
EF1G, GIG35, Elongation factor 1-gamma, Eukaryotic Translation Elongation Factor 1 Gamma, EEF1G, EF-1-gamma, eEF-1B gamma, PRO1608.
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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 MGSMAAGTLY TYPENWRAFK ALIAAQYSGA QVRVLSAPPH FHFGQTNRTP EFLRKFPAGK VPAFEGDDGF CVFESNAIAY YVSNEELRGS TPEAAAQVVQ WVSFADSDIV PPASTWVFPT LGIMHHNKQA TENAKEEVRR ILGLLDAYLK TRTFLVGERV TLADITVVCT LLWLYKQVLE PSFRQAFPNT NRWFLTCINQ PQFRAVLGEV KLCEKMAQFD AKKFAETQPK KDTPRKEKGS REEKQKPQAE RKEEKKAAAP APEEEMDECE QALAAEPKAK DPFAHLPKST FVLDEFKRKY SNEDTLSVAL PYFWEHFDKD GWSLWYSEYR FPEELTQTFM SCNLITGMFQ RLDKLRKNAF ASVILFGTNN SSSISGVWVF RGQELAFPLS PDWQVDYESY TWRKLDPGSE ETQTLVREYF SWEGAFQHVG KAFNQGKIFK.
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 :
C1QTNF5 HumanDescription:
Complement C1q Tumor Necrosis Factor-Related Protein 5 Human Recombinant
CTRP5, MFRP.
Product # :
PRO-2599Price :
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Description
C1QTNF5 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (16-243.a.a) and having a molecular mass of 26.4kDa. C1QTNF5 Human is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The C1QTNF5 protein solution (0.25 mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.5) containing 30% glycerol and 0.2M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Complement C1q Tumor Necrosis Factor-Related Protein 5 (C1QTNF5) encodes a short-chain collagen which is expressed mainly in sub-retinal pigment epithelium, ciliary epithelium and adipose tissue. C1QTNF5 is increased in mtDNA-depleted myocytes and stimulates the phosphorylation of AMP activated protein kinase. C1QTNF5 takespart in the adhesion of the retinal pigment epithelium (RPE) to the Bruch Membrane. Mutations in C1QTNF5 have been associated with late-onset retinal degeneration.
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Synonyms
CTRP5, MFRP.
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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 MGSHMSPPLD DNKIPSLCPG HPGLPGTPGH HGSQGLPGRD
GRDGRDGAPG APGEKGEGGR PGLPGPRGDP GPRGEAGPAG PTGPAGECSV PPRSAFSAKR
SESRVPPPSD APLPFDRVLV NEQGHYDAVT GKFTCQVPGV YYFAVHATVY RASLQFDLVK
NGESIASFFQ FFGGWPKPAS LSGGAMVRLE PEDQVWVQVG VGDYIGIYAS IKTDSTFSGF LVYSDWHSSP VFA.
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 :
TFRC HumanDescription:
Transferrin Receptor Human Recombinant
Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD_antigen: CD71, Transferrin receptor, serum form, sTfR, TFRC, CD71.
Product # :
PRO-2180Price :
Quantity :
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Shipped with Ice Packs
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Description
TFRC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 696 amino acids (89-760 a.a) and having a molecular mass of 77.7 kDa.TFRC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TFRC protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Transferrin receptor protein 1 (TFRC) is required for iron delivery from transferring to cells. The TFRC protein is a transmembrane glycoprotein comprised of 2 disulfide-linked monomers joined by 2 disulfide bonds. Each monomer will bind one holo-transferrin molecule producing an iron-Tf-TfR complex which enters the cell by endocytosis.
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Synonyms
Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD_antigen: CD71, Transferrin receptor, serum form, sTfR, TFRC, CD71.
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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 MGSMCKGVEP KTECERLAGT ESPVREEPGE DFPAARRLYW DDLKRKLSEK LDSTDFTGTI KLLNENSYVP REAGSQKDEN LALYVENQFR EFKLSKVWRD QHFVKIQVKD SAQNSVIIVD KNGRLVYLVE NPGGYVAYSK AATVTGKLVH ANFGTKKDFE DLYTPVNGSI VIVRAGKITF AEKVANAESL NAIGVLIYMD QTKFPIVNAE LSFFGHAHLG TGDPYTPGFP SFNHTQFPPS RSSGLPNIPV QTISRAAAEK LFGNMEGDCP SDWKTDSTCR MVTSESKNVK LTVSNVLKEI KILNIFGVIK GFVEPDHYVV VGAQRDAWGP GAAKSGVGTA LLLKLAQMFS DMVLKDGFQP SRSIIFASWS AGDFGSVGAT EWLEGYLSSL HLKAFTYINL DKAVLGTSNF KVSASPLLYT LIEKTMQNVK HPVTGQFLYQ DSNWASKVEK LTLDNAAFPF LAYSGIPAVS FCFCEDTDYP YLGTTMDTYK ELIERIPELN KVARAAAEVA GQFVIKLTHD VELNLDYERY NSQLLSFVRD LNQYRADIKE MGLSLQWLYS ARGDFFRATS RLTTDFGNAE KTDRFVMKKL NDRVMRVEYH FLSPYVSPKE SPFRHVFWGS GSHTLPALLE NLKLRKQNNG AFNETLFRNQ LALATWTIQG AANALSGDVW DIDNEF.
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 :
CBX5 HumanDescription:
Chromobox Homolog 5 Human Recombinant
Chromobox homolog 5 (HP1 alpha homolog, Drosophila), Heterochromatin protein 1 homolog alpha, HP1Hs alpha, HP1 alpha homolog.
Product # :
PRO-1062Price :
Quantity :
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Description
CBX5 Human Recombinant produced in E. coli is a single polypeptide chain containing 215 amino acids (1-191) and having a molecular mass of 24.8kDa.CBX5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CBX5 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CBX5 belongs to the heterochromatin protein family. CBX5 is enriched in the heterochromatin and linked with centromeres. CBX5 takes part in the creation of functional kinetochore by interaction with important kinetochore proteins. CBX5 has a pseudogene situated on chromosome 3. Additionaly, The CBX5 proteins reconnect with chromatin at the end of mitosis, as Histone H3 is dephosphorylated.
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Synonyms
Chromobox homolog 5 (HP1 alpha homolog, Drosophila), Heterochromatin protein 1 homolog alpha, HP1Hs alpha, HP1 alpha homolog.
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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 MGSHMGKKTK RTADSSSSED EEEYVVEKVL DRRVVKGQVE YLLKWKGFSE EHNTWEPEKN LDCPELISEF MKKYKKMKEG ENNKPREKSE SNKRKSNFSN SADDIKSKKK REQSNDIARG FERGLEPEKI IGATDSCGDL MFLMKWKDTD EADLVLAKEA NVKCPQIVIA FYEERLTWHA YPEDAENKEK ETAKS.
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 :
GCAT HumanDescription:
Glycine C-Acetyltransferase Human Recombinant
2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.
Product # :
ENZ-705Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GCAT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 419 amino acids (22-419 a.a) and having a molecular mass of 45kDa.GCAT is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GCAT protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
L-threonine to glycine degradation consists of a two-step biochemical pathway which involvs the enzymes L-threonine dehydrogenase and 2-amino-3-ketobutyrate coenzyme A ligase. L-Threonine is initially converted into 2-amino-3-ketobutyrate by L-threonine dehydrogenase. Glycine C-Acetyltransferase (GCAT) is the 2nd enzyme in this pathway, which subsequently catalyzes the reaction between 2-amino-3-ketobutyrate and coenzyme A to form glycine and acetyl-CoA. The GCAT enzyme is regard as a class II pyridoxal-phosphate-dependent aminotransferase. GCAT is strongly expressed in the heart, brain, liver and pancreas. GCAT is also found in lung.
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Synonyms
2-amino-3-ketobutyrate coenzyme A ligase mitochondrial, AKB ligase, EC 2.3.1.29, Aminoacetone synthase, Glycine acetyltransferase, GCAT, KBL.
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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 MSALAQLRGI LEGELEGIRG AGTWKSERVI TSRQGPHIRV DGVSGGILNF CANNYLGLSS HPEVIQAGLQ ALEEFGAGLS SVRFICGTQS IHKNLEAKIA RFHQREDAIL YPSCYDANAG LFEALLTPED AVLSDELNHA SIIDGIRLCK AHKYRYRHLD MADLEAKLQE AQKHRLRLVA TDGAFSMDGD IAPLQEICCL ASRYGALVFM DECHATGFLG PTGRGTDELL GVMDQVTIIN STLGKALGGA SGGYTTGPGP LVSLLRQRAR PYLFSNSLPP AVVGCASKAL DLLMGSNTIV QSMAAKTQRF RSKMEAAGFT ISGASHPICP VMLGDARLAS RMADDMLKRG IFVIGFSYPV VPKGKARIRV QISAVHSEED IDRCVEAFVE VGRLHGALP.
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 :
CDC37 HumanDescription:
Cell Division Cycle 37 Human Recombinant
P50CDC37, CDC-37, CDC37, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, CDC37A, Cell Division Cycle 37.
Product # :
PRO-464Price :
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Description
CDC37 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids and having a molecular mass of 44.4 kDa.
Source
Escherichia Coli.
Formulation
The CDC37 protein solution contains 20mM Tris-HCl pH-8 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CDC37 is an essential protein in Saccharomyces cerevisiae and is a molecular chaperone with precise function in cell signal transduction. CDC37 forms a complex/associates with Hsp90 molecular chaperone as one of several auxiliary proteins that are collectively referred to as Hsp90 co-chaperones. CDC37 also forms complex with a number of protein kinases such as CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. CDC34 is involved in directing Hsp90 to its target kinases. CDC37 up-regulation is a common early event in some localized human cancers. CDC37 is necessary for maintaining prostate tumor cell growth and represents a novel target in the exploration for multitargeted therapies. CDC37 plays a role in regulating Hsp90 ATPase activity. CDC37 binds to Akt and HSP90 in the signal transduction pathway in human tumor cells. Tnf-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. CDC37 and heat shock protein 90 bind specifically to the kinase domain of LKB1.
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Synonyms
P50CDC37, CDC-37, CDC37, Hsp90 co-chaperone Cdc37, Hsp90 chaperone protein kinase-targeting subunit, CDC37A, Cell Division Cycle 37.
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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
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDVSV.
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 :
GSTM3 HumanDescription:
Glutathione S-Transferase MU 3 Human Recombinant
Glutathione S-transferase mu 3 (brain), GST5, GSTM3-3, GST class-mu 3, GSTB, GTM3, brain type mu-glutathione S-transferase, glutathione S-aralkyltransferase M3, glutathione S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18.
Product # :
ENZ-592Price :
Quantity :
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Shipped with Ice Packs
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Description
GSTM3 Recombinant produced in E. coli is a single polypeptide chain containing 249 amino acids (1-225) and having a molecular mass of 29.1kDa.GSTM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GSTM3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl,
1mM DTT and 10% glycerol.Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
GSTM3 belongs to the glutathione s-transferase (GST) family of proteins. There are eight GST proteins families, named alpha, kappa, mu, omega, pi, sigma, theta and zeta. Each one of the GST families has several proteins with different functions throughout the cell. The mu type of enzymes takes part in the detoxification of electrophilic compounds, including therapeutic drugs, carcinogens, environmental toxins and products of oxidative stress, by conjugation with glutathione.
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Synonyms
Glutathione S-transferase mu 3 (brain), GST5, GSTM3-3, GST class-mu 3, GSTB, GTM3, brain type mu-glutathione S-transferase, glutathione S-aralkyltransferase M3, glutathione
S-alkyltransferase M3, S-(hydroxyalkyl)glutathione lyase M3, EC 2.5.1.18. -
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSCESS MVLGYWDIRG LAHAIRLLLE FTDTSYEEKR YTCGEAPDYD RSQWLDVKFK LDLDFPNLPY LLDGKNKITQ SNAILRYIAR KHNMCGETEE EKIRVDIIEN QVMDFRTQLI RLCYSSDHEK LKPQYLEELP GQLKQFSMFL GKFSWFAGEK LTFVDFLTYD ILDQNRIFDP KCLDEFPNLK AFMCRFEALE KIAAYLQSDQ FCKMPINNKM AQWGNKPVC
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 :
RNF181 HumanDescription:
Ring Finger Protein 181 Human Recombinant
Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.
Product # :
PRO-1218Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RNF181 Human Recombinant produced in E. coli is a single polypeptide chain containing 176 amino acids (1-153) and having a molecular mass of 20.3 kDa.RNF181 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The RNF181 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
E3 ubiquitin-protein ligase RNF181 (RNF181) accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the thioester form and subsequently directly transfers the ubiquitin to targeted substrates. RNF181 is widely expressed, with the highest levels in the liver and heart and the lowest levels in the brain and skeletal muscle. RNF181 is also expressed in platelets (at protein level).
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Synonyms
Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASYFDE HDCEPSDPEQ ETRTNMLLEL ARSLFNRMDF EDLGLVVDWD HHLPPPAAKT VVENLPRTVI RGSQAELKCP VCLLEFEEEE TAIEMPCHHL FHSSCILPWL SKTNSCPLCR YELPTDDDTY EEHRRDKARK QQQQHRLENL HGAMYT.
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 :
RNF7 HumanDescription:
Ring Finger Protein 7 Human Recombinant
RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.
Product # :
PRO-1671Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RNF7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113 a.a) and having a molecular mass of 15.1kDa.RNF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNF7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Ring Finger Protein 7, also known as RNF7, is an extremely conserved ring finger protein. RNF7 is a vital subunit of SKP1-cullin/CDC53-F box protein ubiquitin ligases that are a part of the protein degradation machinery important for cell cycle progression and signal transduction. RNF7 is a substrate of casein kinase II (CSNK2A1/CKII) and also interacts with it. The phosphorylation of RNF7 by CSNK2A1 promotes the degradation of IkappaBalpha (CHUK/IKK-alpha/IKBKA) and p27Kip1(CDKN1B).
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Synonyms
RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADVEDG EETCALASHS GSSGSKSGGD KMFSLKKWNA VAMWSWDVEC DTCAICRVQV MDACLRCQAE NKQEDCVVVW GECNHSFHNC CMSLWVKQNN RCPLCQQDWV VQRIGK.
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 :
NTRK2 Human , HEKDescription:
Neurotrophic Receptor Tyrosine Kinase 2, HEK Human Recombinant
GP145-TrkB, trk-B, TRKB, NTRK2.
Product # :
CYT-1230Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NTRK2 Human Recombinant is a single, glycosylated, polypeptide chain (32-430 a.a) containing a total of 632 amino acids and having a molecular mass of 70.3 kDa. NTRK2 is fused to a 233 a.a hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The NTRK2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Synonyms
GP145-TrkB, trk-B, TRKB, NTRK2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
CPTSCKCSAS RIWCSDPSPG IVAFPRLEPN SVDPENITEI FIANQKRLEI INEDDVEAYV GLRNLTIVDS GLKFVAHKAF LKNSNLQHIN FTRNKLTSLS RKHFRHLDLS ELILVGNPFT CSCDIMWIKT LQEAKSSPDT QDLYCLNESS KNIPLANLQI PNCGLPSANL AAPNLTVEEG KSITLSCSVA GDPVPNMYWD VGNLVSKHMN ETSHTQGSLR ITNISSDDSG KQISCVAENL VGEDQDSVNL TVHFAPTITF LESPTSDHHW CIPFTVKGNP KPALQWFYNG AILNESKYIC TKIHVTNHTE YHGCLQLDNP THMNNGDYTL IAKNEYGKDE KQISAHFMGW PGIDDGANPN YPDVIYEDYG TAANDIGDTT NRSNEIPSTD VTDKTGREH LEPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.
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Background
NTRK2, also known as TrkB, is a high-affinity receptor for BDNF and other neurotrophins such as neurotrophin-4 (NT-4) and neurotrophin-3 (NT-3). It plays a crucial role in the development, function, and plasticity of the nervous system. Dysregulation of NTRK2 signaling is associated with various neurological disorders, including neurodegenerative diseases, psychiatric disorders, and cancers. NTRK2 has been developed to facilitate research into its biological functions and potential therapeutic applications. This paper provides a comprehensive overview of the scientific research on recombinant human NTRK2, focusing on its biological functionality, detailed description, and physical properties.
NTRK2 is critical for synaptic plasticity, which underlies learning and memory. Research with rhNTRK2 has demonstrated that BDNF-NTRK2 signaling enhances synaptic strength and facilitates long-term potentiation (LTP) in hippocampal neuron.
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 :
Prolactin MouseDescription:
Prolactin Mouse Recombinant
Mammotropin, Luterotropic hormone, Lutetropin, PRL.
Product # :
CYT-321Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
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Description
Prolactin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.5 kDa. The Prolactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 10mM sodium Phosphate buffer pH=8 and 50mM Nacl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Leu-Pro-Ile-Cys-Ser.
Citations
More Info
-
Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luterotropic hormone, Lutetropin, PRL.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prolactin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Prolactin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Pro-Ile-Cys.
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 :
GHRP4Description:
Growth Hormone Releasing Peptide-4
GHRP-4, GHRP4.
Product # :
HOR-022Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Growth Hormone Releasing Peptide-4 Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 607.73 Dalton and a Molecular formula of C34H37N7O4.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
-
Introduction
GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH effect on pituitary somatotrophs to stimulate GH release. The GHRP4 is one of several synthetic met-enkephalin analogs that owns unnatural D-amino acids. They were developed for their growth hormone (GH) releasing activity and called GH secretatogues. They lack opioid activity but are potent stimulators of GH release. These secretatogues are distinct from the growth hormone releasing hormone (GHRH or GHRF) as they share no sequence relation and derive their function through action at a completely different receptor, the ghrelin receptor.
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Synonyms
GHRP-4, GHRP4.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Growth Hormone Releasing Peptide-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRP4 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 GHRP4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
(D-Trp)-Ala-Trp-(D-Phe)-NH2.
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Background
What is the molecular weight/Mw of GHRP4 Protein?
GHRP4 Protein has a total Mw of 0.607kDa.
What is the Purity of GHRP4 Protein?
GHRP4 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of GHRP4 Protein?
The biological functionality of GHRP4 Protein will be determined in the future.
What is the amino acid sequence of GHRP4 Protein?
(D-Trp)-Ala-Trp-(D-Phe)-NH2.
What applications can GHRP4 Protein be used in?
GHRP4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GHRP4 Protein?
The endotoxin level is minimal, GHRP4 Protein was purified using conventional chromatography techniques.
Who supplies GHRP4 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of GHRP4?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GAGA-POZDescription:
GAGA-POZ Drosophila Melanogaster Recombinant
Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.
Product # :
PRO-435Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GAGA-POZ Drosophila Melanogaster Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids & having a molecular mass of 14 kDa.
Source
Escherichia Coli.
Formulation
The protein containing 10mM HEPES (pH-7.4) and 25mM NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
The GAGA factor is a sequence-specific DNA-binding protein, which participates in the regulation of the expression of a variety of different classes of genes in Drosophila such as many developmentally regulated genes, stress induced genes, and cell cycle regulated genes, as well as housekeeping genes. GAGA contains a C-terminal glutamine-rich domain and a highly conserved N-terminal POZ domain which reported to be involved in self-oligomerization in a number of other POZ domain containing proteins. In case of GAGA protein, the N-terminal POZ domain mediates the formation of oligomers both in vitro and in vivo.
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Synonyms
Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLLDLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQTVTKDDYTTH.
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 :
HCV Core 16.8kDaDescription:
Hepatitis C Virus Nucleocapsid (core) 16.8kDa Recombinant
Product # :
HCV-011Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant HCV Core produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 16.8 kDa and fused to a His tag at N-terminus.
Source
Escherichia Coli.
Formulation
HCV Core containing PBS, pH-7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
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). -
Physical Appearance
Sterile filtered colorless solution.
-
Stability
HCV Core although stable at room temperature for 4 weeks, 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.
- View Data Sheet
Name :
SNF8 HumanDescription:
SNF8, ESCRT-II Complex Subunit Human Recombinant
SNF8 ESCRT-II complex subunit homolog (S. cerevisiae), ESCRT-II complex subunit VPS22, ELL-associated protein of 30 kDa, EAP30 subunit of ELL complex, vacuolar-sorting protein SNF8, EAP30, VPS22, Dot3.
Product # :
PRO-1135Price :
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Description
SNF8 Human Recombinant produced in E. coli is a single polypeptide chain containing 282 amino acids (1-258) and having a molecular mass of 31.4 kDa.SNF8 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SNF8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SNF8 belongs to the SNF8 family of vacuolar sorting proteins and is restricts to both the nucleus and the cytoplasm. SNF8 is a subunit of the endosomal sorting complex essential for transport II (ESCRT-II), which is necessary for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway facilitates transfer of transmembrane proteins into the lumen of the lysosome for degradation. Additionally, the ESCRT-II complex takes part in transcription regulation by contributing to derepression of transcription by RNA polymerase II, probably by its interface with ELL.
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Synonyms
SNF8 ESCRT-II complex subunit homolog (S. cerevisiae), ESCRT-II complex subunit VPS22, ELL-associated protein of 30 kDa, EAP30 subunit of ELL complex, vacuolar-sorting protein SNF8, EAP30, VPS22, Dot3.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMHRRGV GAGAIAKKKL AEAKYKERGT VLAEDQLAQM SKQLDMFKTN LEEFASKHKQ EIRKNPEFRV QFQDMCATIG VDPLASGKGF WSEMLGVGDF YYELGVQIIE VCLALKHRNG GLITLEELHQ QVLKGRGKFA QDVSQDDLIR AIKKLKALGT GFGIIPVGGT YLIQSVPAEL NMDHTVVLQL AEKNGYVTVS EIKASLKWET ERARQVLEHL LKEGLAWLDL QAPGEAHYWL PALFTDLYSQ EITAEEAREA LP
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 :
BMP 7 HumanDescription:
Bone Morphogenetic Protein-7 Human Recombinant
Osteogenic Protein 1, BMP-7.
Product # :
CYT-333Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bone Morphogenetic Protein-7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 139 amino acids and having a molecular mass of 15679.97 Dalton. The BMP-7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-7 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM sodium citrate pH=3.5.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
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Synonyms
Osteogenic Protein 1, BMP-7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BMP-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP 7 Human 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 briefly centrifuge the vial prior to opening to bring the contents to the bottom. Reconstitute in 20mM-100mM acetic acid at a concentration of 0.1-0.5mg per ml. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Thr-Gly-Ser-Lys.
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Background
Bone Morphogenetic Protein-7 Human Recombinant: A Comprehensive Review
Abstract:
Bone Morphogenetic Protein-7 (BMP-7) is a crucial member of the transforming growth factor-beta (TGF-β) superfamily with diverse roles in development, tissue repair, and regeneration.
This research paper provides a comprehensive review of BMP-7 Human Recombinant, focusing on its structure, signaling pathways, and diverse functions. Additionally, the paper explores the therapeutic potential of BMP-7 modulation.
Introduction:
BMP-7 is a multifunctional growth factor that plays a significant role in skeletal development and tissue homeostasis. This paper aims to provide an extensive review of BMP-7 Human Recombinant, highlighting its importance in various biological processes and its potential therapeutic applications.
Structure and Function of BMP-7:
BMP-7 is a disulfide-linked homodimeric protein composed of two subunits. It binds to specific cell surface receptors, activating downstream signaling pathways, including the Smad pathway and non-Smad signaling cascades. These pathways regulate cellular processes such as proliferation, differentiation, and apoptosis.
Skeletal Development and Regeneration:
BMP-7 is a key regulator of bone formation and remodeling. It promotes osteoblast differentiation and bone mineralization, contributing to skeletal development and repair. BMP-7 also plays a role in cartilage formation and chondrogenesis.
Tissue Repair and Regeneration:
Beyond its skeletal functions, BMP-7 is involved in tissue repair and regeneration in various organs, including the kidney, liver, and heart. It promotes the regeneration of damaged tissues by stimulating cell proliferation, angiogenesis, and extracellular matrix remodeling.
Therapeutic Potential:
Due to its regenerative and reparative properties, BMP-7 has attracted significant attention as a potential therapeutic agent. It has been investigated for its applications in bone regeneration, cartilage repair, and the treatment of kidney and liver diseases. Clinical trials exploring the therapeutic efficacy of BMP-7 are ongoing.
Challenges and Future Perspectives:
Despite the promising therapeutic potential of BMP-7, challenges remain, including optimizing its delivery systems, understanding its dosage and duration of treatment, and managing potential side effects. Future research should focus on unraveling the intricate mechanisms of BMP-7 signaling, developing targeted therapies, and enhancing its clinical applications.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 15kDa.
What is the source or expression system of BMP7 Protein?
Escherichia Coli.
What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.
What is the amino acid sequence of BMP7 Protein?
BMP7 Protein is composed from 139 amino acids.
What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 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 tA MouseDescription:
Leptin Antagonist Triple Mutant Mouse Recombinant
Product # :
CYT-354Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- Citations
Description
Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, LEP was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting Leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM 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 Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.201 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 :
HCV NS5ADescription:
Hepatitis C Virus NS5A Recombinant
Product # :
HCV-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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- Citations
Description
Recombinant HCV NS5A produced in E. coli is a single polypeptide chain containing 118 amino acids (aa 2210-2306) and having a molecular mass of 13.4kDa.Recombinant HCV NS5A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HCV NS5A protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NS5A is a component of the replication complex which takes part in RNA-binding. NS5A protein’s hyperphosphorylated form is an inhibitor of viral replication. NS5A interacts with Human VAPB and through it targets the viral replication complex to vesicles. NS5A down-regulates viral IRES translation initiation and mediates interferon resistance by interacting and inhibiting human EIF2AK2/PKR. NS5a is also inhibits apoptosis by interacting with BIN1 and FKBP8.
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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 MSLKATCTAN HDSPDAELIE ANLLWRQEMG GNITRVESEN KVVILDSFDP LVAEEDEREV SVPAEILRKS RRFARALPVW ARPDYNPPLV ETWKKPDY.
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 :
LGALS13 HumanDescription:
Galectin-13 Human Recombinant
Galactoside-binding soluble lectin 13, Galectin-13, Gal-13, Placental tissue protein 13, PP13, Placental protein 13, LGALS13, PLAC8, GAL13.
Product # :
CYT-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human LGALS13 produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 16kDa. The LGALS13 also might appear as a homodimer, having a total Mw of 32kDa. LGALS13 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.
Source
Escherichia Coli.
Formulation
LGALS13 protein solution (0.5mg/ml) is formulated in 1xPBS buffer pH 7.4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Recombinant Galectin-13 is an E. coli expressed peptide, this protein is one of human placenta specific galectins, like all galectin family, it contains a carbohydrate recognition domain (CRD) as well. Increased blood concentration was found highly asscoaited with preeclampsia and HELLP syndrome in pregnant women. The molecular weight of galectin-13 is 16kDa.
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Synonyms
Galactoside-binding soluble lectin 13, Galectin-13, Gal-13, Placental tissue protein 13, PP13, Placental protein 13, LGALS13, PLAC8, GAL13.
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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
MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDM DEDSDIAFRFRVHFGNHVVMNRREFGIWMLEETTDYVPFEDGK
QFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSFVKMVQVSRDISLTSVCVCN
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Background
What is the molecular weight/Mw of LGALS13 HUMAN Protein?
LGALS13 HUMAN Protein has a total Mw of 32kDa.
What is the source or expression system of LGALS13 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS13 HUMAN Protein?
LGALS13 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS13 HUMAN Protein?
The biological functionality of LGALS13 HUMAN Protein will be determined in the future.
What is the amino acid sequence of LGALS13 HUMAN Protein?
MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDM DEDSDIAFRFRVHFGNHVVMNRREFGIWMLEETTDYVPFEDGK
QFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSFVKMVQVSRDISLTSVCVCN
What applications can LGALS13 HUMAN Protein be used in?
LGALS13 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS13 HUMAN Protein?
The endotoxin level is minimal, LGALS13 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 :
IFNW1 Human, HEKDescription:
Interferon-Omega 1 Human Recombinant, HEK
IFN omega-1, IFN alpha-II-1, IFNW1.
Product # :
CYT-1225Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
IFNW1 Human Recombinant is a single, glycosylated, polypeptide chain (22-195 a.a) containing a total of 180 amino acids and having a molecular mass of 20.9 kDa. IFNW1 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IFNW1 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .
Citations
More Info
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Synonyms
IFN omega-1, IFN alpha-II-1, IFNW1.
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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
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.
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Background
Interferons, a family of signaling proteins, play a pivotal role in the immune system’s defense against viral infections and other threats. Among these, Interferon W1 (IFNW1), a member of the Type I interferon family, has emerged as a key player in orchestrating antiviral responses and modulating immune reactions. This research embarks on a detailed exploration of the IFNW1 protein, unveiling its structural intricacies, signaling pathways, and its broader implications in immune regulation and disease. By delving into IFNW1, scientists aim to comprehend the nuances of its functions, decipher its interactions within the complex interferon network, and explore its potential applications in therapeutic interventions and beyond.
Structural Insights into IFNW1:
IFNW1, like other Type I interferons, exhibits a unique tertiary structure that enables it to interact with specific cell surface receptors. This interaction triggers a cascade of events, leading to the activation of various antiviral genes and immune modulatory pathways. Understanding the structural basis of IFNW1 is crucial for elucidating its binding affinities, biological activities, and its significance in immune responses.
Signaling Pathways and Antiviral Defense:
IFNW1 engages with its cognate receptors, initiating Janus kinase (JAK)-Signal Transducer and Activator of Transcription (STAT) signaling pathways. This activation leads to the transcription of interferon-stimulated genes (ISGs) with potent antiviral properties. IFNW1’s ability to induce an antiviral state in infected and neighboring cells is fundamental for restricting viral replication and curtailing the spread of infections. Additionally, IFNW1 plays a role in modulating adaptive immune responses, contributing to the broader immune defense mechanisms.
IFNW1 in Immunomodulation and Disease:
Beyond its antiviral functions, IFNW1 is implicated in immunomodulation and disease pathogenesis. Dysregulation of IFNW1 signaling is associated with autoimmune disorders, including lupus and rheumatoid arthritis, highlighting its involvement in immune-related diseases. Moreover, IFNW1 is being explored in cancer immunotherapy, where its ability to modulate the tumor microenvironment and enhance immune surveillance presents opportunities for novel treatment strategies.
Therapeutic Potential and Future Prospects:
The unique properties of IFNW1, particularly its role in immune regulation and antiviral defense, position it as a potential therapeutic target. Research efforts are directed towards harnessing its immunomodulatory functions for developing therapies against infectious diseases, autoimmune disorders, and certain cancers. Additionally, understanding IFNW1’s interactions with other components of the immune system opens avenues for innovative approaches in personalized medicine and targeted immunotherapies.
IFNW1 Protein, as an integral component of the interferon network, stands as a sentinel in the body’s defense against viral invasions and immune dysregulations. Its multifaceted roles in antiviral defense, immune modulation, and disease pathogenesis underscore its significance in biology and medicine. As researchers delve deeper into the intricacies of IFNW1, they pave the way for innovative therapies, immunomodulatory interventions, and a deeper understanding of immune responses. This research not only illuminates the pivotal role of IFNW1 but also holds the promise of transformative advancements in medicine, shaping the future of immunology and disease therapeutics.
What is the molecular weight/Mw of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein has a total Mw of 20.9kDa.
What is the source or expression system of IFNW1 HUMAN, HEK Protein?
HEK293 Cells.
What is the Purity of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNW1 HUMAN, HEK Protein?
The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .
What is the amino acid sequence of IFNW1 HUMAN, HEK Protein?
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.
What applications can IFNW1 HUMAN, HEK Protein be used in?
IFNW1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNW1 HUMAN, HEK Protein?
The endotoxin level is minimal, IFNW1 HUMAN, HEK 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.