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599 results found for “Mitochondrial Transcription Factor”
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Name :
STK16 HumanDescription:
Serine/Threonine Kinase 16 Human Recombinant
Serine/threonine-protein kinase 16, Myristoylated and palmitoylated serine/threonine-protein kinase, MPSK, Protein kinase PKL12, TGF-beta-stimulated factor 1, TSF-1, Tyrosine-protein kinase STK16, hPSK, STK16, MPSK1, PKL12, TSF1, KRCT.
Product # :
PKA-032Price :
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Shipped with Ice Packs
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Description
STK16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-305 a.a) and having a molecular mass of 37.2kDa.STK16 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STK16 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Serine/threonine-protein kinase 16 (STK16) is a membrane-associated protein kinase which phosphorylates on serine and threonine residues. STK16 is involved in secretory vesicle trafficking or intracellular signaling. Furthermore, the STK16 protein may have a role in regulating stromal-epithelial interactions which occur during ductal morphogenesis in the mammary gland. STK16 can autophosphorylate on Tyr residue; it is however unclear whether STK16 has tyrosine-protein kinase toward other proteins. STK16 may also be involved in TGF-beta signaling.
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Synonyms
Serine/threonine-protein kinase 16, Myristoylated and palmitoylated serine/threonine-protein kinase, MPSK, Protein kinase PKL12, TGF-beta-stimulated factor 1, TSF-1, Tyrosine-protein kinase STK16, hPSK, STK16, MPSK1, PKL12, TSF1, KRCT.
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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 MGSHMGHALC VCSRGTVIID NKRYLFIQKL GEGGFSYVDL VEGLHDGHFY ALKRILCHEQ QDREEAQREA DMHRLFNHPN ILRLVAYCLR ERGAKHEAWL LLPFFKRGTL WNEIERLKDK GNFLTEDQIL WLLLGICRGL EAIHAKGYAH RDLKPTNILL GDEGQPVLMD LGSMNQACIH VEGSRQALTL QDWAAQRCTI SYRAPELFSV QSHCVIDERT DVWSLGCVLY AMMFGEGPYD MVFQKGDSVA LAVQNQLSIP QSPRHSSALR QLLNSMMTVD PHQRPHIPLL LSQLEALQPP APGQHTTQI.
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 :
HDAC2 HumanDescription:
Histone Deacetylase 2 Human Recombinant
Histone deacetylase 2, YAF1, HD2, YY1-associated factor 1, transcriptional regulator homolog RPD3, RPD3, EC 3.5.1.98.
Product # :
ENZ-157Price :
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Description
HDAC2 Human Recombinant produced in Hi-5 Cell is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-488) and having a molecular mass of 56.4 kDa.The HDAC2 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Hi-5 Cell.
Formulation
The HDAC2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl, 0.1mM PMSF and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
HDAC2 is a member of the histone deacetylase family that performs through the construction of large multiprotein complexes and are in charge of the deacetylation of lysine residues on the N-terminal region of the core histones. HDAC2 forms transcriptional repressor complexes by relating to a diversity of proteins, like YY1- a mammalian zinc-finger transcription factor.
In addition, HDAC2 has a vital part in transcriptional regulation, cell cycle progression and developmental procedures. -
Synonyms
Histone deacetylase 2, YAF1, HD2, YY1-associated factor 1, transcriptional regulator homolog RPD3, RPD3, EC 3.5.1.98.
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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
MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA ILELLKYHQR VLYIDIDIHH
GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM
EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKTD VKEEDKSKDN SGEKTDTKGT KSEQLSNPSR HHHHHH
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 :
TNF a Human, HisDescription:
Tumor Necrosis Factor-Alpha Human Recombinant, His Tag
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Product # :
CYT-494Price :
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Shipped at Room temp
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Description
Tumor Necrosis Factor-α Human Recombinant His produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids fragment and having a molecular mass of 18.3kDa with an N-terminal hexahistidine tag. The TNF-alpha His is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.0.
Purity
Greater than 97.0% as determined by SDS-PAGE and HPLC analyses.
Biological Activity
The ED50 was determined in the presence of actinomycin D by a cytotoxicity assay using murine L929 cells is <0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107IU/mg.
More Info
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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer. -
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TNF-α although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-α 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 TNF-α 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
MHHHHHHVRS SSRTPSDKPV AHVVANPQAE GQLQWLNRRA NALLANGVEL RDNQLVVPSE GLYLIYSQVL FKGQGCPSTH VLLTHTISRI AVSYQTKVNL LSAIKSPCQR ETPEGAEAKP WYEPIYLGGV FQLEKGDRLS AEINRPDYLD FAESGQVYFG IIAL.
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 :
EIF1 HumanDescription:
Eukaryotic Translation Initiation Factor 1 Human Recombinant
A121, EIF-1, EIF1A, ISO1, SUI1, Eukaryotic translation initiation factor 1, eIF1, Protein translation factor SUI1 homolog, Sui1iso1, EIF1.
Product # :
PRO-773Price :
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Shipped with Ice Packs
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Description
EIF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-113 a.a.) and having a molecular weight of 16.9kDa.The EIF1 is fused to 37 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
EIF1 is important for scanning and plays a role in initiation site selection. EIF1 promotes the assembly of 48S ribosomal at the authentic initiation codon of a conventional capped mRNA.
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Synonyms
A121, EIF-1, EIF1A, ISO1, SUI1, Eukaryotic translation initiation factor 1, eIF1, Protein translation factor SUI1 homolog, Sui1iso1, EIF1.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWAGSMSA IQNLHSFDPF ADASKGDDLL PAGTEDYIHI RIQQRNGRKT LTTVQGIADD YDKKKLVKAF KKKFACNGTV IEHPEYGEVI QLQGDQRKNI CQFLVEIGLA KDDQLKVHGF.
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 :
C1QTNF7 HumanDescription:
Complement C1q Tumor Necrosis Factor-Related Protein 7 Human Recombinant
CTRP7, C1QTNF7, ZACRP7, Complement C1q tumor necrosis factor-related protein 7.
Product # :
PRO-514Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C1QTNF7 Human Recombinant produced in E.Coli is a signle, non-glycosylated, Polypeptide chain containing 283 amino acids and having a molecular mass of 30.22 kDa. The protein contains an extra 10 amino acid His tag at N-terminus. The C1QTNF7 amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q9BXJ2 amino acids 17–289.The C1QTNF7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Human C1QTNF7 was filtered (0.4µm) and lyophilized from a 0.5mg/ml solution containing 30mM Acetate Buffer, pH-4 and 5% (w/v) trehalose.
Purity
Greater than 95% as determined by SDS PAGE.
More Info
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Introduction
C1QTNF7 is a collagen type-IV specific for basement membranes.
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Synonyms
CTRP7, C1QTNF7, ZACRP7, Complement C1q tumor necrosis factor-related protein 7.
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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
Add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. 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 QPRGNQLKGE NYSPRYICSI PGLPGPPGPP GANGSPGPHG RIGLPGRDGR DGRKGEKGEK GTAGLRGKTG PLGLAGEKGD QGETGKKGPI GPEGEKGEVG PIGPPGPKGD RGEQGDPGLP GVCRCGSIVL KSAFSVGITT SYPEERLPII FNKVLFNEGE HYNPATGKFI CAFPGIYYFS YDITLANKHL AIGLVHNGQY RIKTFDANTG NHDVASGSTV IYLQPEDEVW LEIFFTDQNG LFSDPGWADS LFSGFLLYVD TDYLDSISEDDEL.
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 :
EIF3F HumanDescription:
Eukaryotic Translation Initiation Factor 3F Human Recombinant
Eukaryotic Translation Initiation Factor 3, Subunit F, EIF3S5 , Eukaryotic Translation Initiation Factor 3, Subunit 5 (Epsilon, 47kD), EC 3.4.19.12, Deubiquitinating Enzyme EIF3f, eIF3f, eIF-3-epsilon, EIF3 P47, Eukaryotic Translation Initiation Factor 3 Subunit 5, eIF3-p47, Eukaryotic Translation Initiation Factor 3, Subunit 5 Epsilon, 47kDa.
Product # :
PRO-1722Price :
Quantity :
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Shipped with Ice Packs
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Description
EIF3F Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-357 a.a) and having a molecular mass of 40kDa. EIF3F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EIF3F protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, and 0.4M urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Eukaryotic Translation Initiation Factor 3F, also known as EIF3F belongs to the eIF-3 subunit F family. EIF3F is a component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which isessential for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosomeand facilitates the recruitment of eIF-1, eIF-1A, eIF 2: GTP: methionyl-tRNAi and eIF-5 to form the 43S preinitiationcomplex (43S PIC). In addition, the eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA forAUG recognition. The eIF-3 complex is also necessary for disassembly and recycling of post termination ribosomalcomplexes and subsequently prevents premature union of the 40S and 60S ribosomal subunits prior to initiation. Among the diseases associated with EIF3F are intrahepatic cholangiocarcinoma, and cholangiocarcinoma.
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Synonyms
Eukaryotic Translation Initiation Factor 3, Subunit F, EIF3S5 , Eukaryotic Translation Initiation Factor 3, Subunit 5 (Epsilon, 47kD), EC 3.4.19.12, Deubiquitinating Enzyme EIF3f, eIF3f, eIF-3-epsilon, EIF3 P47, Eukaryotic Translation Initiation Factor 3 Subunit 5, eIF3-p47, Eukaryotic Translation Initiation Factor 3, Subunit 5 Epsilon, 47kDa.
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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 MGSMATPAVP VSAPPATPTP VPAAAPASVP APTPAPAAAP VPAAAPASSS DPAAAAAATA APGQTPASAQ APAQTPAPAL PGPALPGPFP GGRVVRLHPV ILASIVDSYE RRNEGAARVI GTLLGTVDKH SVEVTNCFSV PHNESEDEVA VDMEFAKNMY ELHKKVSPNE LILGWYATGH DITEHSVLIH EYYSREAPNP IHLTVDTSLQ NGRMSIKAYV STLMGVPGRT MGVMFTPLTV KYAYYDTERI GVDLIMKTCF SPNRVIGLSS DLQQVGGASA RIQDALSTVL QYAEDVLSGK VSADNTVGRF LMSLVNQVPK IVPDDFETML NSNINDLLMV TYLANLTQSQ IALNEKLVNL.
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 :
ATF BovineDescription:
Apo Transferrin Bovine
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-511Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bovine Apo Transferrin is a glycoprotein of approximately 77kDa.
Source
Bovine Serum.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Bovine Transferrin is a crucial component for the cultivation of mammalian cells in- vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin are Molecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
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Physical Appearance
Sterile Filtered off-white lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze.
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Solubility
It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 1gr/30ml in 20min. at 20-25C.
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Iron Content
The Iron content was estimated by ICP-OES and was found to be less than 40 ppm.
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 :
HSF1 AntibodyDescription:
Heat Shock Transcription Factor-1, Mouse Anti Human
HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.
Product # :
ANT-328Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 0.02% Sodium Azide and 10% Glycerol.
More Info
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Introduction
The transcription of heat-shock genes is rapidly induced after temperature stress in response to environmental changes, and it is also involved in oogenesis, spermatogenesis, and placental development. Hsp90, is a major repressor of HSF1 gene. HSF1 is known for its participation in heat shock response. HSF1 protein regulates the transcription of hundreds of targets, such as genes involved in protein folding, detoxification, energy generation, carbohydrate metabolism, and cell wall organization. HSF1 binds to MTA1 in vitro & in breast carcinoma. Suppression of estrogen-dependent transcription may contribute to role of HSF1 in cancer. Human cancer lines of diverse origins express higher dependence on HSF1 function to maintain proliferation and survival than their non-transformed counterparts. HSF1 induces anticoagulation and relaxation factors in vascular endothelial cells and could therefore be used to treat cardiovascular disease. HSF1 is directly involved in the regulation of HO1 havi
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Synonyms
HSF-1, HSF1, HSTF-1, HSTF1, Heat shock factor protein 1, Heat shock transcription factor 1.
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Immunogen
Anti-human HSF1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HSF1 amino acids 1-529 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
PJ7F9AT.
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Applications
HSF1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000~ 2,000. Recommended starting dilution is 1:1,000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
HSF1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
Visfatin HumanDescription:
Visfatin Human Recombinant
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
Product # :
CYT-318Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Visfatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 466 amino acids. The total molecular mass is 52.6kDa (calculated). The Visfatin is purified by Flag-affinity chromatography.
Source
Escherichia Coli.
Formulation
Visfatin was lyophilized with no additives.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The activity is determined by its ability to induce IL-6, IL-1 beta and TNF alpha production from human PBMCs at 100ng/ml.More Info
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Introduction
Excess adiposity is the most important risk in the development of type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-a, and IL-6, that modulate sensitivity and appear to play an important role in the pathogenesis, diabetes, dyslipidemia, inflammation, and atherosclerosis. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
Visfatin exerts mimetic effects that are dose-dependent and quantitatively similar to stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its mimetic effects, visfatin was as effective in reducing hyperglycemia in deficient diabetic mice. Visfatin was also found to be bound to and activate receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin did not compete for binding to the receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes. -
Synonyms
PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Visfatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Visfatin 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
Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. It is recommended to reconstitute the lyophilized product with 20 mM HCl at a concentration of 0.1 mg/mL, which can be further diluted into other aqueous solutions. Wait several minutes for full reconstitution and solubility.
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Amino Acid Sequence
MPPNTSKVYS YFECREKKTE NSKLRKVKYE ETVFYGLQYI LNKYLKGKVV TKEKIQEAKD VYKEHFQDDV FNEKGWNYIL EKYDGHLPIE IKAVPEGFVI PRGNVLFTVE NTDPECYWLT NWIETILVQS WYPITVATNS REQKKILAKY LLETSGNLDG LEYKLHDFGY RGVSSQETAG IGASAHLVNF KGTDTVAGLA LIKKYYGTKD PVPGYSVPAA EHSTITAWGK DHEKDAFEHI VTQFSSVPVS VVSDSYDIYN ACEKIWGEDL RHLIVSRSTQ APLIIRPDSG NPLDTVLKVL EILGKKFPVT ENSKGYKLLP PYLRVIQGDG VDINTLQEIV EGMKQKMWSI ENIAFGSGGG LLQKLTRDLL NCSFKCSYVV TNGLGINVFK DPVADPNKRS KKGRLSLHRT PAGNFVTLEE GKGDLEEYGQ DLLHTVFKNG KVTKSYSFDE IRKNAQLNIE LEAAHH.
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Background
About Visfatin Human
Visfatin is a cytokine expressed in visceral fat that was originally isolated as a secreted
element that synergized with stem cell factors and IL-7. One of its main functions is to
enhance the development of B cell precursors.The cytokine is also known as the “Pre-B Cell Colony-Enhancing Factor (PBEF).” It has been
identified in vertebrates, including mice and humans, and it’s being studied due to its link
to inflammatory conditions, beta cell function, and cardiovascular disease.
What’s the Function of Visfatin Human Recombinant?Visfatin human recombinant is produced in E. Coli. It’s a single, non-glycosylated,
polypeptide chain that contains 466 amino acids, it’s purified by FLAG-affinity
chromatography, and it contains a total molecular mass of 52.6 kDa.
What Are the Main Applications of Visfatin Human Recombinant?The cytokine is being researched because of its involvement in glucose homeostasis,
dysregulation in biosynthesis and signal transduction, and the pathogenesis of diabetes.
Visfatin human recombinant is tailored exclusively for laboratory research, ensuring
experts can get further answers regarding the cytokine’s involvement in different
processes, including pathogenesis, diabetes, inflammation, dyslipidemia, and
atherosclerosis.Findings can also help during the identification of high-risk people for cardiovascular
disease and diabetes.
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 :
CTGF Human (183-255)Description:
Connective Tissue Growth Factor (183-255 a.a.) Human Recombinant
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Product # :
CYT-1174Price :
Quantity :
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Description
CTGF Human Recombinant is a single, glycosylated polypeptide chain containing 80 amino acids (183-255a.a) and having a molecular mass of 9.1kDa (calculated). CTGF is fused to a 7 a.a His tag at N-terminal.
Source
HEK293 cells.
Formulation
CTGF 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 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Connective Tissue Growth Factor is a part of the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF, Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: tumorigenesis,fibrosis and vascular ailments. Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of 4 modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia. -
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
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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
MHHHHHHRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK.
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Background
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 9.1kDa.
What is the source or expression system of CTGF Protein?
HEK293 cells.
What is the Purity of CTGF Protein?
CTGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTGF Protein?
The biological functionality of CTGF Protein will be determined in the future.
What is the amino acid sequence of CTGF Protein?
MHHHHHHRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK.
What applications can CTGF Protein be used in?
CTGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTGF Protein?
The endotoxin level is minimal, CTGF 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 :
OTC HumanDescription:
Ornithine Carbamoyltransferase Human Recombinant
Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.
Product # :
ENZ-596Price :
Quantity :
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Description
OTC Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (33-354) and having a molecular mass of 38.9kDa.OTC is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The OTC solution (0.5mg/ml) contains 20mM MES buffer (pH 6.0), 100mM Nacl, 2mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
OTC is a member of the ATCase/OTCase family. OTC has a key part in the urea cycle, catalyzing the second step in this pathway: the transformation of L-orthinine and carbamoyl phosphate to L-citrulline. In humans, the urea cycle is a vital pathway to detoxification of ammonia. Alterations in the gene encoding OTC are linked to the X-linked disorder OTCD (ornithine carbamoyltransferase deficiency). OTCD disorder of the urea cycle is characterized by hyperammonemia.
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Synonyms
Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.
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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 MGSHMNKVQL KGRDLLTLKN FTGEEIKYML WLSADLKFRI KQKGEYLPLL QGKSLGMIFE KRSTRTRLST ETGFALLGGH PCFLTTQDIH LGVNESLTDT ARVLSSMADA VLARVYKQSD LDTLAKEASI PIINGLSDLY HPIQILADYL TLQEHYSSLK GLTLSWIGDG NNILHSIMMS AAKFGMHLQA ATPKGYEPDA SVTKLAEQYA KENGTKLLLT NDPLEAAHGG NVLITDTWIS MGQEEEKKKR LQAFQGYQVT MKTAKVAASD WTFLHCLPRK PEEVDDEVFY SPRSLVFPEA ENRKWTIMAV MVSLLTDYSP QLQKPKF.
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 :
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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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.
More Info
-
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.
-
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.
- View Data Sheet
Name :
KLF6 HumanDescription:
Kruppel-Like Factor 6 Human Recombinant
Krueppel-like factor 6, B-cell-derived protein 1, Core promoter element-binding protein, GC-rich sites-binding factor GBF, Proto-oncogene BCD1, Suppressor of tumorigenicity 12 protein, Transcription factor Zf9, KLF6, BCD1, COPEB, CPBP, ST12.
Product # :
PRO-1864Price :
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Description
KLF6 Human Recombinant produced in E. coli is. a single polypeptide chain containing 306 amino acids (1-283) and having a molecular mass of 34.3kDa. KLF6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KLF6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Kruppel-Like Factor 6 (KLF6) is a nuclear protein which has 3 zinc fingers. The zinc fingers of KLF6 are accountable for the specific DNA binding with the guanine-rich core promoter factors. The central region is involved in activation or posttranslational regulatory pathways, and the acidic N terminal domain takes part in the process of transcriptional activation.
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Synonyms
Krueppel-like factor 6, B-cell-derived protein 1, Core promoter element-binding protein, GC-rich sites-binding factor GBF, Proto-oncogene BCD1, Suppressor of tumorigenicity 12 protein, Transcription factor Zf9, KLF6, BCD1, COPEB, CPBP, ST12.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDVLPMC SIFQELQIVH ETGYFSALPS LEEYWQQTCL ELERYLQSEP CYVSASEIKF DSQEDLWTKI ILAREKKEES ELKISSSPPE DTLISPSFCY NLETNSLNSD VSSESSDSSE ELSPTAKFTS DPIGEVLVSS GKLSSSVTST PPSSPELSRE PSQLWGCVPG ELPSPGKVRS GTSGKPGDKG NGDASPDGRR RVHRCHFNGC RKVYTKSSHL KAHQRTHTGE KPYRCSWEGC EWRFARSDEL TRHFRKHTGA KPFKCSHCDR CFSRSDHLAL HMKRHL.
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 :
MIF Human His NDescription:
Macrophage Migration Inhibitory Factor Human, Recombinant His Tag N-Terminus
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Product # :
CYT-431Price :
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Description
MIF human Recombinant, fused to 40 a.a. His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques. Macrophage Inducing Factor Human Recombinant ( 1-115 a.a. ) is a single, non-glycosylated, polypeptide chain having a total amino acids of 155 and molecular mass of 17kDa.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing PBS pH-7.4.
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
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Liquid MIF although stable 4°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC LHSIGKIGGA QNRSYSKLLC GLLAERLRIS PDRVYINYYD MNAANVGWNN STFA.
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 :
CNTF RatDescription:
Ciliary Neurotrophic Factor Rat Recombinant
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-654Price :
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Description
CNTF Recombinant Rat produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids and having a molecular mass of 22834 Dalton. The CNTF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.025% NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by Gel Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.More Info
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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CNTF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CNTF in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
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Amino Acid Sequence
AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH
YGAKDKQM. -
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 22kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
Fully biologically active by its ability to phosphorylate STAT3 in several cells lines.
What is the amino acid sequence of CNTF Protein?
AFAEQTPLTL HRRDLSSRSIWLARKIRSDLTALMESYVKHQGLNKNI
NLDSVDGVPVASTDRWSEMTEAERLQENLQAYRTFQGMLTKLLEDQRV
HFTPTEGDFHQAIHTLMLQVSAFAYQLEELMVLLEQKIPENEADGMPA
TVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRVISSHQMGISALESH YGAKDKQM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF 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 :
BDH1 HumanDescription:
3-Hydroxybutyrate Dehydrogenase, Type 1 Human Recombinant
D-beta-hydroxybutyrate dehydrogenase, mitochondrial, BDH, 3-hydroxybutyrate dehydrogenase, BDH1, SDR9C1.
Product # :
ENZ-215Price :
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Shipped with Ice Packs
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Description
BDH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (47-343) and having a molecular mass of 35.3kDa.BDH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The BDH1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
BDH1 belongs to the short-chain dehydrogenase/reductase gene family. BDH1 forms a homotetrameric lipid-requiring enzyme of the mitochondrial membrane and has a specific necessity for phosphatidylcholine for optimal enzymatic activity. BDH1 catalyzes the interconversion of acetoacetate and (R)-3-hydroxybutyrate, the 2 main ketone bodies formed during fatty acid catabolism.
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Synonyms
D-beta-hydroxybutyrate dehydrogenase, mitochondrial, BDH, 3-hydroxybutyrate dehydrogenase, BDH1, SDR9C1.
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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 MASAAEPVGS KAVLVTGCDS GFGFSLAKHL HSKGFLVFAG CLMKDKGHDG VKELDSLNSD RLRTVQLNVC SSEEVEKVVE IVRSSLKDPE KGMWGLVNNA GISTFGEVEF TSLETYKQVA EVNLWGTVRM TKSFLPLIRR AKGRVVNISS MLGRMANPAR SPYCITKFGV EAFSDCLRYE MYPLGVKVSV VEPGNFIAAT SLYSPESIQA IAKKMWEELP EVVRKDYGKK YFDEKIAKME TYCSSGSTDT SPVIDAVTHA LTATTPYTRY HPMDYYWWLR MQIMTHLPGA ISDMIYIR.
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 :
TNFRSF4 HumanDescription:
TNF Receptor Superfamily Member 4 Human Recombinant
TNFRSF4, TNF Receptor Superfamily Member 4, TAX Transcriptionally-Activated Glycoprotein 1 Receptor, OX40L Receptor, ACT35 Antigen, CD134 Antigen, TXGP1L, Tax-Transcriptionally Activated Glycoprotein 1 Receptor, Tumor Necrosis Factor Receptor Superfamily, Member 4, Tumor Necrosis Factor Receptor Superfamily Member 4 , Lymphoid Activation Antigene ACT35, OX40 Cell Surface Antigen, OX40 Homologue , ATC35 Antigen, OX40 Antigen , ACT35, CD134, IMD16, OX40.
Product # :
CYT-1039Price :
Quantity :
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Description
TNFRSF4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 425 amino acids (29-214a.a.) and having a molecular mass of 46.9Da. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF4 is expressed with a 239 amino acid higG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFRSF4 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with mouse OX40 Ligand/TNFSF4 The ED50 range ≤ 0.15 ug/ml.
More Info
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Introduction
TNFRSF4, also known as TNF Receptor Superfamily Member 4, is a T cell co-stimulatory molecule which belongs to the TNF receptor superfamily. TNFRSF4 coordinates with other co-stimulatory substances such as CD28, CD40, CD30, CD27 and 4-1BB to control the activation of the immune response. TNFRSF4 takes a vital part in antigen-specific T cell expansion as well as survival. TNFRSF4 is up-regulated on CD4+ and CD8+ T cells upon engagement of the TCR by antigen presenting cells along with co-stimulation by CD40-CD40 Ligand and CD28-B7. In addition, TNFRSF4 regulates cytokine production from T cells, antigen presenting cells, natural killer cells and natural killer cells. TNFRSF4 regulates cytokine receptor signaling.
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Synonyms
TNFRSF4, TNF Receptor Superfamily Member 4, TAX Transcriptionally-Activated Glycoprotein 1 Receptor, OX40L Receptor, ACT35 Antigen, CD134 Antigen, TXGP1L, Tax-Transcriptionally Activated Glycoprotein 1 Receptor, Tumor Necrosis Factor Receptor Superfamily, Member 4, Tumor Necrosis Factor Receptor Superfamily Member 4 , Lymphoid Activation Antigene ACT35, OX40 Cell Surface Antigen, OX40 Homologue , ATC35 Antigen, OX40 Antigen , ACT35, CD134, IMD16, OX40.
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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
LHCVGDTYPS NDRCCHECRP GNGMVSRCSR SQNTVCRPCG PGFYNDVVSS KPCKPCTWCN LRSGSERKQL CTATQDTVCR CRAGTQPLDS YKPGVDCAPC PPGHFSPGDN QACKPWTNCT LAGKHTLQPA SNSSDAICED RDPPATQPQE TQGPPARPIT VQPTEAWPRT SQGPSTRPVE VPGGRALEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH
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 :
GTSF1 HumanDescription:
Gametocyte Specific Factor 1 Human Recombinant
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
Product # :
PRO-561Price :
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Shipping Method :
Shipped with Ice Packs
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Description
GTSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167) and having a molecular mass of 21.7 kDa.GTSF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GTSF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.
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Synonyms
Gametocyte Specific Factor 1, FAM112B, Family with Sequence Similarity 112 Member B, Gametocyte-Specific Factor 1, Protein FAM112B, GTSF1.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEETYTD SLDPEKLLQC PYDKNHQIRA CRFPYHLIKC RKNHPDVASK LATCPFNARH QVPRAEISHH ISSCDDRSCI EQDVVNQTRS LRQETLAEST WQCPPCDEDW DKDLWEQTST PFVWGTTHYS DNNSPASNIV TEHKNNLASG MRVPKSLPYV LPWKNNGNAQ.
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 :
NDUFS2 HumanDescription:
Histidine NADH Dehydrogenase Fe-S Protein 2 Human Recombinant
CI-49 , NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, Complex I-49kD, CI-49kD, NADH-ubiquinone oxidoreductase 49 kDa subunit, NDUFS2.
Product # :
ENZ-737Price :
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Description
NDUFS2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (77-463a.a) and having a molecular mass of 46.5kDa. NDUFS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFS2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
NDUFS2 is a core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysis. Complex I takes part in the transfer of electrons from NADH to the respiratory chain. Histidine NADH Dehydrogenase Fe-S Protein 2 (NDUFS2) is required for catalytic activity. Imperfections in NDUFS2 are the source of complex I mitochondrial respiratory chain deficiency, which is characterized by many symptoms including liver failure, cardiomyopathy and neurodegeneration.
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Synonyms
CI-49 , NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, Complex I-49kD, CI-49kD, NADH-ubiquinone oxidoreductase 49 kDa subunit, NDUFS2.
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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 MGSVKNITLN FGPQHPAAHG VLRLVMELSG EMVRKCDPHI GLLHRGTEKL IEYKTYLQAL PYFDRLDYVS MMCNEQAYSL AVEKLLNIRP PPRAQWIRVL FGEITRLLNH IMAVTTHALD LGAMTPFFWL FEEREKMFEF YERVSGARMH AAYIRPGGVH QDLPLGLMDD IYQFSKNFSL RLDELEELLT NNRIWRNRTI DIGVVTAEEA LNYGFSGVML RGSGIQWDLR KTQPYDVYDQ VEFDVPVGSR GDCYDRYLCR VEEMRQSLRI IAQCLNKMPP GEIKVDDAKV SPPKRAEMKT SMESLIHHFK LYTEGYQVPP GATYTAIEAP KGEFGVYLVS DGSSRPYRCK IKAPGFAHLA GLDKMSKGHM LADVVAIIGT QDIVFGEVDR.
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 :
CTF1 RatDescription:
Cardiotrophin-1 Rat Recombinant
Cardiotrophin-1, CT-1, Ctf1.
Product # :
CYT-199Price :
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Shipped at Room temp
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Description
Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.More Info
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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction. -
Synonyms
Cardiotrophin-1, CT-1, Ctf1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
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Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.4kDa.
What is the source or expression system of CTF1 Protein?
Escherichia Coli.
What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF1 Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.
What is the amino acid sequence of CTF1 Protein?
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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 :
Thymosin beta 4Description:
Thymosin β4
Thymosin beta-4. TB500, TB-500
Product # :
HOR-275Price :
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Description
Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by RP-HPLC.
More Info
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Introduction
Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.
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Synonyms
Thymosin beta-4. TB500, TB-500
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 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 Thymosin beta-4 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
Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.
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 :
NT 3 HumanDescription:
Neurotrophin-3 Human Recombinant
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
Product # :
CYT-257Price :
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Shipped at Room temp
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Description
Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 0.1% TFA.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.
More Info
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Introduction
NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.
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Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 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
MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of NT-3 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MGMT HumanDescription:
O-6-Methylguanine-DNA Methyltransferase Human Recombinant
Methylated-DNA--protein-cysteine methyltransferase, 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase, MGMT.
Product # :
ENZ-389Price :
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Description
MGMT Human Recombinant fused to a 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 227 amino acids (1-207) and having a molecular mass of 23.8 kDa. The MGMT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MGMT solution contains 20mM Tris-HCl pH-7.5, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MGMT is an enzyme that repairs O-6-methylguanine, a mutagenic DNA base damaged by endogenous and environmental alkylating agents and takes part in the cellular defense against the biological effects of O-6-methylguanine in DNA. MGMT repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. abnormal MGMT expression correlates with the prognosis in human solid cancers. MGMT decrease of expression is correlated with methylation. The human MGMT is a negative regulator of estrogen receptor-mediated transcription upon alkylation DNA damage. MGMT promoter hypermethylation plays an important role in the early steps of colorectal carcinogenesis. Abnormal promoter hypermethylation of MGMT gene is associated with oral squamous cell carcinomas.
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Synonyms
Methylated-DNA--protein-cysteine methyltransferase, 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase, MGMT.
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Physical Appearance
Sterile Filtered clear colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDKDCEMKRT TLDSPLGKLE LSGCEQGLHE IKLLGKGTSA ADAVEVPAPA AVLGGPEPLM QCTAWLNAYF HQPEAIEEFP VPAFHHPVFQ QESFTRQVLW KLLKVVKFGE VISYQQLAAL AGNPKAARAV GGAMRGNPVP ILIPCHRVVC SSGAVGNYSG GLAVKEWLLA HEGHRLGKPG LGGSSGLAGA WLKGAGATSG SPPAGRN.
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 :
MCM7 PAT1G8AT AntibodyDescription:
Minichromosome Maintenance Complex Component 7, Clone PAT1G8AT, Mouse Anti Human
Minichromosome Maintenance Complex Component 7, MCM7 Minichromosome Maintenance Deficient 7 (S. Cerevisiae), Minichromosome Maintenance Deficient (S. Cerevisiae) 7, DNA Replication Licensing Factor MCM7, Homolog of S. Cerevisiae Cdc47, CDC47 Homolog, P1CDC47, PNAS146, P85MCM, MCM2, CDC47, P1.1-MCM3, EC 3.6.4.12.
Product # :
ANT-719Price :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
MCM7 is a highly conserved mini-chromosome maintenance protein (MCM) vital for eukaryotic genome replication initiation. The MCM proteins form a hexameric protein complex which is a key component of the pre-replication complex (pre_RC) which takes part in replication forks formation and in DNA replication related proteins recruitment. The MCM complex is comprised of MCM2, 4, 6 and 7 proteins and possesses DNA helicase activity, such as DNA unwinding.
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Synonyms
Minichromosome Maintenance Complex Component 7, MCM7 Minichromosome Maintenance Deficient 7 (S. Cerevisiae), Minichromosome Maintenance Deficient (S. Cerevisiae) 7, DNA Replication Licensing Factor MCM7, Homolog of S. Cerevisiae Cdc47, CDC47 Homolog, P1CDC47, PNAS146, P85MCM, MCM2, CDC47, P1.1-MCM3, EC 3.6.4.12.
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Immunogen
Anti-human MCM7 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human MCM7 protein 1-414 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and k light chain.
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Clone
PAT1G8AT.
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Applications
MCM7 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
MCM7 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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.