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1000 results found for “TSLP”
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Name :
PTP4A2 HumanDescription:
Protein Tyrosine Phosphatase Type IVA Member 2 Human Recombinant
HH13, HH7-2, HU-PP-1, OV-1, PRL-2, PRL2, ptp-IV1a, ptp-IV1b, PTP4A, PTPCAAX2.
Product # :
ENZ-558Price :
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Description
Recombinant Human PTP4A2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (1-167 a.a.) and having a molecular mass of 23.2 kDa. PTP4A2 is fused to a 36 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The PTP4A2 (0.5mg/ml) protein solution contains 20mM Tris-HCl, pH-8, 1mM EDTA and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PTP4A2 is part of a small class of the protein tyrosine phosphatase (PTP) family. PTP4A2 is localized to the early endosome that take part in a variety of cellular activities. PTP4A2 protein interacts with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), therefore has a role as a regulator of GGT II activity. Overexpression of PTP4A2 in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis.
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Synonyms
HH13, HH7-2, HU-PP-1, OV-1, PRL-2, PRL2, ptp-IV1a, ptp-IV1b, PTP4A, PTPCAAX2.
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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 KDRWGSMNRP APVEISYENM RFLITHNPTN ATLNKFTEEL KKYGVTTLVR VCDATYDKAP
VEKEGIHVLD WPFDDGAPPP NQIVDDWLNL LKTKFREEPG CCVAVHCVAG LGRAPVLVAL ALIECGMKYE DAVQFIRQKR RGAFNSKQLL
YLEKYRPKMR LRFRDTNGHC CVQ.
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 :
MCL1 HumanDescription:
Myeloid Cell Leukemia Sequence 1 Human Recombinant
Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.
Product # :
PRO-1202Price :
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Description
MCL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (1-327) and having a molecular mass of 37.2 kDa.MCL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MCL1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MCL1 is a member of the Bcl-2 family. MCL1 takes part in the control of apoptosis against cell existence, and in the preservation of viability but not of proliferation. Alternative splicing happens at this locus and two transcript variants encoding different isoforms are known. Isoform 1 is the longer gene product and it increases cell existence by inhibiting apoptosis. Isoform 2 is a shorter gene product which indorses apoptosis and is death-inducing.
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Synonyms
Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.
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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 MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG GEAGAVIGGS AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA PTRRAAPLEE MEAPAADAIM SPEEELDGYE PEPLGKRPAV LPLLELVGES GNNTSTDGSL PSTPPPAEEE EDELYRQSLE IISRYLREQA TGAKDTKPMG RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE DDVKSLSRVM IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR TKRDWLVKQR GWDGFVEFFH VEDLEGG.
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 :
DTNBP1 HumanDescription:
Dystrobrevin-Binding Protein 1 Isoform C Human Recombinant
Dysbindin, SDY, DBND, HPS7, My031, FLJ30031, MGC20210, DKFZp564K192, Dystrobrevin-binding protein 1, Hermansky-Pudlak syndrome 7 protein homolog, Hps7-like protein, DTNBP1.
Product # :
PRO-675Price :
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Description
DTNBP1 Human Recombinant fused to 37 a.a. N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (1-270a.a.) and having a molecular mass of 34.6 kDa.
Source
Escherichia Coli.
Formulation
The DTNBP1 solution contains 20mM Tris pH-8, 0.5mM DTT, 0.1M NaCl, and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
DTNBP1 is involved in organelle biogenesis connected with melanosomes, platelet dense granules, and lysosomes. An analogous protein in murine is a part of a protein complex called BLOC-1, and connects to alpha- and beta-dystrobrevins, which are factors of the dystrophin-associated protein complex (DPC). Mutations in DTNBP1 gene are associated with Hermansky-Pudlak syndrome type 7. DTNBP1 gene may also be associated with schizophrenia.
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Synonyms
Dysbindin, SDY, DBND, HPS7, My031, FLJ30031, MGC20210, DKFZp564K192, Dystrobrevin-binding protein 1, Hermansky-Pudlak syndrome 7 protein homolog, Hps7-like protein, DTNBP1.
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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 KDRWGSHMLS AHWEKKKTSL VELQEQLQQL PALIADLESM TANLTHLEAS FEEVENNLLHLEDLCGQCEL ERCKHMQSQQ LENYKKNKRK ELETFKAELD AEHAQKVLEM EHTQQMKLKE RQKFFEEAFQ QDMEQYLSTG YLQIAERREP IGSMSSMEVN VDMLEQMDLM DISDQEALDV FLNSGGEENT VLSPALGPES STCQNEITLQ VPNPSELRAK PPSSSSTCTD SATRDISEGG ESPVVQSDEE EVQVDTALAT SHTDREATPD GGEDSDS.
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 :
SSBP1 Human, HisDescription:
Single-Stranded DNA Binding Protein 1 Human Recombinant, His Tag
Mt-SSB, mtSSB, SOSS-B1, SSBP, PWP1-interacting protein 17, Single-stranded DNA-binding protein, mitochondrial.
Product # :
PRO-1408Price :
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Description
SSBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids (17-148 a.a.) and having a molecular mass of 17kDa.SSBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SSBP1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Single-Stranded DNA Binding Protein 1 (SSBP) participates in mitochondrial biogenesis. SSBP binds preferentially and cooperatively to ss-DNA. The SSBP protein is involved in mitochondrial DNA replication and associates with mitochondrial DNA.
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Synonyms
Mt-SSB, mtSSB, SOSS-B1, SSBP, PWP1-interacting protein 17, Single-stranded DNA-binding protein, mitochondrial.
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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 MGSESETTTS LVLERSLNRV HLLGRVGQDP VLRQVEGKNP VTIFSLATNE MWRSGDSEVY QLGDVSQKTT WHRISVFRPG LRDVAYQYVK KGSRIYLEGK IDYGEYMDKN NVRRQATTII ADNIIFLSDQ TKEKE.
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 :
ENSA HumanDescription:
Endosulfine Alpha Human Recombinant
ARPP-19e, Alpha endosulfine isoform 3, Alpha-endosulfine, ENSA, MGC4319, MGC8394, MGC78563.
Product # :
PRO-772Price :
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Description
ENSA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (1-121 a.a.) and having a molecular weight of 15.5kDa. The ENSA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Endosulfine Alpha protein solution contains 20mM Tris, pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ENSA is an endogenous ligand for sulfonylurea receptor. ENSA reduces K(ATP) channel currents by inhibiting sulfonylurea from binding to the receptor and thus stimulates insulin secretion. Endosulfine Alpha is part of a conserved cAMP-regulated phosphoprotein (ARPP) family. Endosulfine Alpha is an endogenous ligand for the sulfonylurea receptor, ABCC8/SUR1. Endosulfine Alpha is an endogenous regulator of KATP channels. ENSA modulates insulin secretion through the interaction with KATP channel. ENSA is a candidate gene for type 2 diabetes. ENSA is expressed in a wide range of tissues including muscle, brain, and endocrine tissues.
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Synonyms
ARPP-19e, Alpha endosulfine isoform 3, Alpha-endosulfine, ENSA, MGC4319, MGC8394, MGC78563.
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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 MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV E.
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 :
FABP9 HumanDescription:
Fatty Acid Binding Protein-9 Human Recombinant
Fatty acid-binding protein 9, Testis lipid-binding protein, TLBP, Testis-type fatty acid-binding protein, T-FABP, FABP9, PERF, PERF15.
Product # :
PRO-1088Price :
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Description
FABP9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-132 a.a) and having a molecular mass of 17.6kDa.FABP9 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FABP9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Fatty acid binding protein 9 (FABP9) belongs to the fatty acid-binding proteins (FABPs) which are a family of small, extremely conserved, cytoplasmic proteins to bind long-chain fatty acids and other hydrophobic ligands. FABP9 is found in midpachytene spermatocytes and round spermatids, and comprises part of the perinuclear theca. FABP9 probably links intracellular membranes and signals abnormal sperm formation during spermatogenesis.
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Synonyms
Fatty acid-binding protein 9, Testis lipid-binding protein, TLBP, Testis-type fatty acid-binding protein, T-FABP, FABP9, PERF, PERF15.
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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 MGSHMVEPFL GTWKLVSSEN FEDYMKELGV NFAARNMAGL VKPTVTISVD GKMMTIRTES SFQDTKISFK LGEEFDETTA DNRKVKSTIT LENGSMIHVQ KWLGKETTIK RKIVDEKMVV ECKMNNIVST RIYEKV.
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 :
TARBP2 HumanDescription:
TAR RNA Binding Protein 2 Human Recombinant
LOQS, TRBP, TRBP1, TRBP2, RISC-loading complex subunit TARBP2, TAR RNA-binding protein 2, Trans-activation-responsive RNA-binding protein, TARBP2.
Product # :
PRO-1980Price :
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Description
TARBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 345 amino acids (1-345 a.a) and having a molecular mass of 36.9kDa. TARBP2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TARBP2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TAR RNA Binding Protein 2 (TARBP2) is a component of the RISC loading complex which takes part in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. TARBP2, which is also known as the micro-RNA (miRNA) loading complex (miRLC), contains three DRBM (double-stranded RNA-binding) domains. TARBP2 binds to the HIV-1 TAR RNA and stimulates translation of TAR-containing RNAs.
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Synonyms
LOQS, TRBP, TRBP1, TRBP2, RISC-loading complex subunit TARBP2, TAR RNA-binding protein 2, Trans-activation-responsive RNA-binding protein, TARBP2.
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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
MLAANPGKTP ISLLQEYGTR IGKTPVYDLL KAEGQAHQPN FTFRVTVGDT SCTGQGPSKK AAKHKAAEVA LKHLKGGSML EPALEDSSSF SPLDSSLPED IPVFTAAAAA TPVPSVVLTR SPPMELQPPV SPQQSECNPV GALQELVVQK GWRLPEYTVT QESGPAHRKE FTMTCRVERF IEIGSGTSKK LAKRNAAAKM LLRVHTVPLD ARDGNEVEPD DDHFSIGVGS RLDGLRNRGP GCTWDSLRNS VGEKILSLRS CSLGSLGALG PACCRVLSEL SEEQAFHVSY LDIEELSLSG LCQCLVELST QPATVCHGSA TTREAARGEA ARRALQYLKI MAGSK.
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 b HumanDescription:
Tumor Necrosis Factor-Beta Human Recombinant
Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.
Product # :
CYT-224Price :
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Shipped at Room temp
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Description
Tumor Necrosis Factor-b Human Recombinant (Lymphotoxin) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids and having a molecular mass of 18645 Dalton. The TNF-b is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized protein with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAG.Biological Activity
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.05ng/ml, corresponding to a Specific Activity of 20,000,000IU/mg.Citations
More Info
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Introduction
Lymphotoxin alpha, a member of the tumor necrosis factor family, is a cytokine produced by lymphocytes. LTA is highly inducible, secreted, and exists as homotrimeric molecule. LTA forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. LTA is also involved in the formation of secondary lymphoid organs during development and plays a role in apoptosis.
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Synonyms
Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-b 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 Tumor Necrosis Factor-beta 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
MLPGVGLTPS AAQTARQHPK MHLAHSTLKP AAHLIGDPSK QNSLLWRANT DRAFLQDGFS LSNNSLLVPT SGIYFVYSQV VFSGKAYSPK ATSSPLYLAH EVQLFSSQYP FHVPLLSSQK MVYPGLQEPW LHSMYHGAAF QLTQGDQLST HTDGIPHLVL SPSTVFFGAF AL.
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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 1.082 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-b 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 :
TNNI1 HumanDescription:
Troponin I Type 1 Human Recombinant
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.
Product # :
PRO-1269Price :
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Description
TNNI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.8kDa.TNNI1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNNI1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Troponin I, (TNNI1) is a member of the troponin I family. Troponin complex has 3 subunits, TNNI1 known as the inhibitory Subunit which prevents the actin-myosin interactions and thus mediating striated muscle relaxation. TNNI1 combines with tropomyosin and regulates calcium sensitivity of striated muscles by structural modifications in actin-myosin complexes.
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Synonyms
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle ,Troponin I, slow-twitch isoform.
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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 MPEVERKPKI TASRKLLLKS LMLAKAKECW EQEHEEREAE KVRYLAERIP TLQTRGLSLS ALQDLCRELH AKVEVVDEER YDIEAKCLHN TREIKDLKLK VMDLRGKFKR PPLRRVRVSA DAMLRALLGS KHKVSMDLRA NLKSVKKEDT EKERPVEVGD WRKNVEAMSG MEGRKKMFDA AKSPTSQ
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 :
TPT1 HumanDescription:
Tumor Protein Translationally-Controlled 1 Human Recombinant
TCTP, Fortilin, Histamine-Releasing Factor, Translationally-controlled tumor protein, p23, HRF, Fortilin, p02, FLJ27337, TPT1.
Product # :
PRO-776Price :
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Description
TPT1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 210 amino acids (1-172 a.a.) and having a molecular mass of 23.9 kDa. TPT1 is fused to a 38 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TPT1 solution containing 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TPT1 takes part in calcium binding and microtubule stabilization. TPT1 is an immunoglobulin E dependent histamine-releasing factor produced by lymphocytes of atopic children and present in biologic fluids of allergic patients. TPT1 protein is similar to p23, a protein of Ehrlich ascites tumor cells, synthesized in the exponentially growing tumor. TPT1 is similar with IgE-dependent histamine releasing factor. TPT1 has a cell housekeeping function. TPT1 is involved in spermatogenesis and acts as a calcium binding protein of the human placenta that regulates calcium handling in trophoblast cells.
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Synonyms
TCTP, Fortilin, Histamine-Releasing Factor, Translationally-controlled tumor protein, p23, HRF, Fortilin, p02, FLJ27337, TPT1.
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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 KDRWGSHMMI IYRDLISHDE MFSDIYKIRE IADGLCLEVE GKMVSRTEGN IDDSLIGGNA SAEGPEGEGT ESTVITGVDI VMNHHLQETS FTKEAYKKYI KDYMKSIKGK LEEQRPERVK PFMTGAAEQI KHILANFKNY QFFIGENMNP DGMVALLDYR EDGVTPYMIF FKDGLEMEKC.
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 :
CFLAR HumanDescription:
CASP8 and FADD-Like Apoptosis Regulator Human Recombinant
CASP8 and FADD-like apoptosis regulator, CASH, CLARP, Casper, I-FLICE, Inhibitor of FLICE, MRIT, c-FLIP, FLAME, FLAME-1, FADD-like antiapoptotic molecule 1, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, CASP8AP1, MACH-related inducer of toxicity, usurpin beta, CASPER.
Product # :
PRO-920Price :
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Description
CFLAR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 480 amino acids (1-480) and having a molecular mass of 55.3 kDa.The CFLAR is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CFLAR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
The precise role of CFLAR is not yet revealed but it seems it is vital in apoptosis regulation downstream of all identified death receptors.
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Synonyms
CASP8 and FADD-like apoptosis regulator, CASH, CLARP, Casper, I-FLICE, Inhibitor of FLICE, MRIT, c-FLIP, FLAME, FLAME-1, FADD-like antiapoptotic molecule 1, Caspase homolog, Caspase-eight-related protein, Caspase-like apoptosis regulatory protein, Cellular FLICE-like inhibitory protein, CASP8AP1, MACH-related inducer of toxicity, usurpin beta, CASPER.
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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
MSAEVIHQVE EALDTDEKEM LLFLCRDVAI DVVPPNVRDL LDILRERGKL SVGDLAELLY RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI GEDLDKSDVS SLIFLMKDYM GRGKISKEKS FLDLVVELEK LNLVAPDQLD LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT SYRNVLQAAI QKSLKDPSNN FRLHNGRSKE QRLKEQLGAQ QEPVKKSIQE SEAFLPQSIP EERYKMKSKP LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG KPKMFFIQNY VVSEGQLENS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD FFWSLCTADM SLLEQSHSSP SLYLQCLSQK LRQERKRPLL DLHIELNGYM YDWNSRVSAK EKYYVWLQHT LRKKLILSYT.
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 :
CLPS HumanDescription:
Colipase Pancreatic Human Recombinant
Colipase Pancreatic, Pancreatic Colipase Preproprotein, Colipase, CLPS.
Product # :
PRO-1959Price :
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Description
CLPS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (18-112) and having a molecular mass of 12.5 kDa.CLPS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CLPS solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Colipase (CLPS) is a protein co-enzyme essential for optimal enzyme activity of pancreatic lipase. CLPS is secreted by the pancreas as an inactive form, procolipase, which is then activated in the intestinal lumen by trypsin. CLPS prevents the inhibitory effect of bile salts on the lipase-catalyzed intraduodenal hydrolysis of dietary long-chain triglycerides. CLPS allows lipase to anchor noncovalently to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts. CLPS binds to the C-terminal, non-catalytic domain of lipase, thus stabilizing an active conformation and significantly increasing the whole hydrophobic binding site.
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Synonyms
Colipase Pancreatic, Pancreatic Colipase Preproprotein, Colipase, CLPS.
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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 MGSAPGPRGI IINLENGELC MNSAQCKSNC CQHSSALGLA RCTSMASENS ECSVKTLYGI YYKCPCERGL TCEGDKTIVG SITNTNFGIC HDAGRSKQ.
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 :
ThrombinDescription:
Human Thrombin
Product # :
PRO-339Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thrombin was purified from human plasma.
Source
Human Plasma.
Formulation
Lyophilized protein containing mannitol, sodium chloride, calcium chloride.
Biological Activity
The specific activity was found to be 116 US Units/mg protein.
Citations
More Info
-
Introduction
Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.
-
Physical Appearance
lyophilized powder.
-
Stability
Lyophilized Human Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution human thrombin 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 human thrombin in sterile a 0.9% NaCl solution at 500U/ml.
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 :
TPD52L1 AntibodyDescription:
Tumor Protein D52 L1, Mouse Anti Human
Tumor protein D53, Tumor protein D52-like 1, TPD52L1, hD53, D53, MGC8556, TPD52L2.
Product # :
ANT-302Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
Citations
More Info
-
Introduction
TPD52L1 (hD53, hD53L1) is a member of D52 gene family and overexpressed in human breast carcinoma. TPD52L1 contains coiled-coil motif, which is responsible for homo- and heteromeric interaction, and may be a regulator of cell proliferation and calcium-mediated signal transduction. Moreover, TPD52L1 interacts with the mitogen-activated protein kinase kinase kinase 5 (MAP3K5/ASK1) and positively regulates MAP3K5-induced apoptosis.
-
Synonyms
Tumor protein D53, Tumor protein D52-like 1, TPD52L1, hD53, D53, MGC8556, TPD52L2.
-
Immunogen
Anti-human TPD52L1 mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human TPD52L1 amino acids 1-131 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
-
Clone
Pd1C5AT.
-
Applications
TPD52L1 antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:3,000. Recommended starting dilution is 1:1000.
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Type
Mouse Anti Human Monoclonal.
-
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.
-
Purification Method
TPD52L1 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.
- View Data Sheet
Name :
TNFRSF25 HumanDescription:
TNF Ligand Receptor Superfamily Member 25 Recombinant Human
Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.
Product # :
CYT-980Price :
Quantity :
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Description
TNFRSF25 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 417 amino acids (25-199) and having a molecular mass of 46.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). TNFRSF25 is fused to a 242 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFRSF25 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
Determined by the binding ability in a functional ELISA with Human VEGI (CAT# cyt-589). The ED50 range ≤ 5ug/ml.
Citations
More Info
-
Introduction
TNF Ligand Receptor Superfamily Member 25 (TNFRSF25) belongs to the TNF receptor superfamily that binds to the TNF-like protein TL1A. TNFRSF25 interacts directly with the adapter TRADD and regulates lymphocyte homeostasis. TNFRSF25 is also mediates activation of NF-kappa-B and induces apoptosis. TNFRSF25 signals are vital to exert T helper cell 2 effector activity in Th2-polarized CD4 cells and co-stimulate interleukin-13 production by glycosphingolipid-activated NKT cells.
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Synonyms
Tumor necrosis factor receptor superfamily member 25, TNFRSF25, TNF Ligand Receptor Superfamily Member 25, APO-3, DDR3, DR3, LARD, TNFRSF12, TR3, TRAMP, WSL-1, WSL-LR, Apo-3, Apoptosis-inducing receptor AIR, Protein WSL, Apoptosis-mediating receptor DR3, Apoptosis-mediating receptor TRAMP, Death receptor 3, Lymphocyte-associated receptor of death.
-
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.
-
Amino Acid Sequence
ADPQGGTRSP RCDCAGDFHK KIGLFCCRGC PAGHYLKAPC TEPCGNSTCL VCPQDTFLAW ENHHNSECAR CQACDEQASQ VALENCSAVA DTRCGCKPGW FVECQVSQCV SSSPFYCQPC LDCGALHRHT RLLCSRRDTD CGTCLPGFYE HGDGCVSCPT STLGSCPERC AAVCGWRQLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.
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 :
TUBB3 HumanDescription:
Tubulin, Beta 3 Class III Human Recombinant
Beta-4, CDCBM, CFEOM3A, TUBB4 , Tubulin beta-3 chain, Tubulin beta-4 chain, Tubulin beta-III, TUBB3.
Product # :
PRO-1388Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TUBB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-450 a.a.) and having a molecular mass of 52.8kDa. TUBB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
TUBB3 protein solution (0.25mg/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
-
Introduction
Tubulin, beta 3 class III (TUBB3), which is the major constituent of microtubules, is primarily Expressed in neurons and is involved in neurogenesis and in axon guidance and maintenance. TUBB3 binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain.
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Synonyms
Beta-4, CDCBM, CFEOM3A, TUBB4 , Tubulin beta-3 chain, Tubulin beta-4 chain, Tubulin beta-III, TUBB3.
-
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 MGSMREIVHI QAGQCGNQIG AKFWEVISDE HGIDPSGNYV GDSDLQLERI SVYYNEASSH KYVPRAILVD LEPGTMDSVR SGAFGHLFRP DNFIFGQSGA GNNWAKGHYT EGAELVDSVL DVVRKECENC DCLQGFQLTH SLGGGTGSGM GTLLISKVRE EYPDRIMNTF SVVPSPKVSD TVVEPYNATL SIHQLVENTD ETYCIDNEAL YDICFRTLKL ATPTYGDLNH LVSATMSGVT TSLRFPGQLN ADLRKLAVNM VPFPRLHFFM PGFAPLTARG SQQYRALTVP ELTQQMFDAK NMMAACDPRH GRYLTVATVF RGRMSMKEVD EQMLAIQSKN SSYFVEWIPN NVKVAVCDIP PRGLKMSSTF IGNSTAIQEL FKRISEQFTA MFRRKAFLHW YTGEGMDEME FTEAESNMND LVSEYQQYQD ATAEEEGEMY EDDEEESEAQ GPK.
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 :
Thyroglobulin Human, BiotinDescription:
Thyroglobulin Human, Biotinylated
Thyroglobulin, TGN, AITD3, TG.
Product # :
PRO-2563Price :
Quantity :
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Description
Human Thyroglobulin is a biotinylated, glycosylated, polypeptide chain having a total molecular mass of 662 kDa (331 kDa per subunit).
Source
Native, Isolated from human thyroid glands.
Formulation
Human Thyroglobulin biotinylated is supplied at a 20mM HEPES buffer pH-7.6, 150mM NaCl and 40% Sucrose (w/v).
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease. -
Synonyms
Thyroglobulin, TGN, AITD3, TG.
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Physical Appearance
Sterile Filtered 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. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)
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 :
TYRP1 HumanDescription:
Tyrosinase Related Protein 1 Human Recombinant
Tyrosinase Related Protein 1, Tyrosinase-Related Protein 1, Melanoma Antigen Gp75, Glycoprotein 75, DHICA Oxidase, Catalase B, CAS2, TRP1, TYRP, TRP, 5,6-Dihydroxyindole-2-Carboxylic Acid Oxidase, EC 1.14.18.1, EC 1.14.18.-, EC 1.14.18, B-PROTEIN, TRP-1, TYRRP, CATB, GP75, OCA3, 5,6-dihydroxyindole-2-carboxylic acid oxidase.
Product # :
PRO-2350Price :
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Description
TYRP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 462 amino acids (25-477a.a) and having a molecular mass of 52.5kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).TYRP1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TYRP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TYRP1, also known as 5, 6-dihydroxyindole-2-carboxylic acid oxidase, is a melanosomal enzyme which is a member of the tyrosinase family and takes a significant part in the melanin biosynthetic pathway. TYRP1 is a melanocyte-specific gene which is involved in eumelanin synthesis. Furthermore, TYRP1 is implicated in the oxidation of 5,6-dihydroxyindole-2-carboxylic acid-DHICA into indole-5,6-quinone-2-carboxylic acid. TYRP1 is regulated by the microphthalmia-associatedtranscription factor-MITF.
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Synonyms
Tyrosinase Related Protein 1, Tyrosinase-Related Protein 1, Melanoma Antigen Gp75, Glycoprotein 75, DHICA Oxidase, Catalase B, CAS2, TRP1, TYRP, TRP, 5,6-Dihydroxyindole-2-Carboxylic Acid Oxidase, EC 1.14.18.1, EC 1.14.18.-, EC 1.14.18, B-PROTEIN, TRP-1, TYRRP, CATB, GP75, OCA3, 5,6-dihydroxyindole-2-carboxylic acid oxidase.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADLQFPRQCA TVEALRSGMC CPDLSPVSGP GTDRCGSSSG RGRCEAVTAD SRPHSPQYPH DGRDDREVWP LRFFNRTCHC NGNFSGHNCG TCRPGWRGAA CDQRVLIVRR NLLDLSKEEK NHFVRALDMA KRTTHPLFVI ATRRSEEILG PDGNTPQFEN ISIYNYFVWT HYYSVKKTFL GVGQESFGEV DFSHEGPAFL TWHRYHLLRL EKDMQEMLQE PSFSLPYWNF ATGKNVCDIC TDDLMGSRSN FDSTLISPNS VFSQWRVVCD SLEDYDTLGT LCNSTEDGPI RRNPAGNVAR PMVQRLPEPQ DVAQCLEVGL FDTPPFYSNS TNSFRNTVEG YSDPTGKYDP AVRSLHNLAH LFLNGTGGQT HLSPNDPIFV LLHTFTDAVF DEWLRRYNAD ISTFPLENAP IGHNRQYNMV PFWPPVTNTE MFVTAPDNLG YTYEIQWPSR EFSVPEHHHH HH.
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 :
YARS2 HumanDescription:
Tyrosyl-tRNA Synthetase 2 Human Recombinant
Tyrosine--tRNA ligase mitochondrial, Tyrosyl-tRNA synthetase, TyrRS, YARS2, CGI-04, TYRRS, MLASA2, MT-TYRRS.
Product # :
ENZ-614Price :
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Shipped with Ice Packs
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Description
YARS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 482 amino acids (17-477 a.a.) and having a molecular mass of 53.7kDa.YARS2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
YARS2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Tyrosyl-tRNA synthetase (YARS2) is a mitochondrial protein which catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and afterward transferred to the acceptor end of tRNA(Tyr). YARS2 gene mutations are linked with myopathy with lactic acidosis and sideroblastic anemia type 2 (MLASA2).
-
Synonyms
Tyrosine--tRNA ligase mitochondrial, Tyrosyl-tRNA synthetase, TyrRS, YARS2, CGI-04, TYRRS, MLASA2, MT-TYRRS.
-
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 MTLNLSVLLP LGLRKAHSGA QGLLAAQKAR GLFKDFFPET GTKIELPELF DRGTASFPQT IYCGFDPTAD SLHVGHLLAL LGLFHLQRAG HNVIALVGGA TARLGDPSGR TKEREALETE RVRANARALR LGLEALAANH QQLFTDGRSW GSFTVLDNSA WYQKQHLVDF LAAVGGHFRM GTLLSRQSVQ LRLKSPEGMS LAEFFYQVLQ AYDFYYLFQR YGCRVQLGGS DQLGNIMSGY EFINKLTGED VFGITVPLIT STTGAKLGKS AGNAVWLNRD KTSPFELYQF FVRQPDDSVE RYLKLFTFLP LPEIDHIMQL HVKEPERRGP QKRLAAEVTK LVHGREGLDS AKRCTQALYH SSIDALEVMS DQELKELFKE APFSEFFLDP GTSVLDTCRK ANAIPDGPRG YRMITEGGVS INHQQVTNPE SVLIVGQHIL KNGLSLLKIG KRNFYIIKWL QL.
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 :
TLR2 HumanDescription:
Toll Like Receptor 2 Human Recombinant
Toll Like Receptor 2, Toll/Interleukin-1 Receptor-Like Protein 4, Toll-Like Receptor 2, TIL4, CD282 Antigen, CD282, TLR2.
Product # :
PRO-2337Price :
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Description
TLR2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 578 amino acids (21-588 aa) and having a molecular mass of 65.2kDa. TLR2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TLR2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TLR2 belongs to the Toll-like receptor (TLR) family that plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) which are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. TLR2 is expressed most abundantly in peripheral blood leukocytes, and mediates host response to Gram-positive bacteria and yeast via stimulation of NF-kappaB.
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Synonyms
Toll Like Receptor 2, Toll/Interleukin-1 Receptor-Like Protein 4, Toll-Like Receptor 2, TIL4, CD282 Antigen, CD282, TLR2.
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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
KEESSNQASL SCDRNGICKG SSGSLNSIPS GLTEAVKSLD LSNNRITYIS NSDLQRCVNL QALVLTSNGI NTIEEDSFSS LGSLEHLDLS YNYLSNLSSS WFKPLSSLTF LNLLGNPYKT LGETSLFSHL TKLQILRVGN MDTFTKIQRK DFAGLTFLEE LEIDASDLQS YEPKSLKSIQ NVSHLILHMK QHILLLEIFV DVTSSVECLE LRDTDLDTFH FSELSTGETN SLIKKFTFRN VKITDESLFQ VMKLLNQISG LLELEFDDCT LNGVGNFRAS DNDRVIDPGK VETLTIRRLH IPRFYLFYDL STLYSLTERV KRITVENSKV FLVPCLLSQH LKSLEYLDLS ENLMVEEYLK NSACEDAWPS LQTLILRQNH LASLEKTGET LLTLKNLTNI DISKNSFHSM PETCQWPEKM KYLNLSSTRI HSVTGCIPKT LEILDVSNNN LNLFSLNLPQ LKELYISRNK LMTLPDASLL PMLLVLKISR NAITTFSKEQ LDSFHTLKTL EAGGNNFICS CEFLSFTQEQ QALAKVLIDW PANYLCDSPS HVRGQQVQDV RLSVSECHRT LEHHHHHH
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 :
TNF a MouseDescription:
Tumor Necrosis Factor-Alpha Mouse Recombinant
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Product # :
CYT-252Price :
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Shipping Method :
Shipped at Room temp
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Description
Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(c) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.Citations
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 Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
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Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-a 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 :
TNFRSF14 Human, HisDescription:
HVEM Human Recombinant, His Tag
Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.
Product # :
CYT-800Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFRSF14 Human Recombinant produced in E. Coli is a single, glycosylated polypeptide chain containing 187 amino acids (39-202) and having a molecular mass of 19.7kDa.TNFRSF14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TNFRSF14 solution (0.5mg/ml) containing 20mM Tris-HCl (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.
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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 MGSLPSCKED EYPVGSECCP KCSPGYRVKE ACGELTGTVC EPCPPGTYIA HLNGLSKCLQ CQMCDPAMGL RASRNCSRTE NAVCGCSPGH FCIVQDGDHC AACRAYATSS PGQRVQKGGT ESQDTLCQNC PPGTFSPNGT LEECQHQTKC SWLVTKAGAG TSSSHWV.
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 :
PSPN MouseDescription:
Persephin Mouse Recombinant
Persephin, PSPN.
Product # :
CYT-802Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg.Citations
More Info
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Introduction
Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.
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Synonyms
Persephin, PSPN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN 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 PSPN 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
ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG
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 :
TGFA HumanDescription:
Transforming Growth Factor-Alpha Human Recombinant
Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.
Product # :
CYT-871Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TGFA Human Recombinant (40-89) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 50 amino acids and having a molecular mass of 5.6kDa. The TGFA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured in a proliferation assay using mouse BALB/c 3T3 cells, is 0.395ng/ml.
Citations
More Info
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Introduction
Transforming Growth Factor-Alpha (TGF-alpha) belongs to the EGF family of cytokines. TGFA soluble form is discharged from the membrane by proteolytic cleavage. Membrane-bound proTGF-alpha is biologically active and has a role in cell-cell adhesion or in the stimulation of adjacent cells. TGFA expression is common in transformed cells. Additionally, TGFA is expressed in normal tissues during embryogenesis and in adult cells/tissues, including the pituitary, keratinocytes, and macrophages.
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Synonyms
Transforming Growth Factor Alpha, Protransforming Growth Factor Alpha, TGF-Alpha, TGFA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TGFA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFA 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 TGFA in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VVSHFNDCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA.
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Background
Title: Transforming Growth Factor-Alpha Human Recombinant, Yeast: A Versatile Biopharmaceutical for Therapeutic Applications
Abstract:
Transforming Growth Factor-Alpha (TGF-α) is a potent growth factor involved in numerous physiological processes, including cell proliferation, differentiation, and tissue repair. The development of TGF-α human recombinant using yeast expression systems has provided a valuable biopharmaceutical tool for therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic applications of TGF-α human recombinant derived from yeast, highlighting its versatility and clinical significance.Introduction:
TGF-α is a crucial growth factor that regulates cellular functions and plays a vital role in tissue development and repair. Harnessing the therapeutic potential of TGF-α has been limited by challenges in its production and stability. However, the development of TGF-α human recombinant using yeast expression systems has overcome these limitations, making it an attractive biopharmaceutical for therapeutic interventions.Production Process and Characteristics:
TGF-α human recombinant derived from yeast is produced through recombinant DNA technology, utilizing yeast cells as expression hosts. Yeast expression systems offer several advantages, including high expression yields, cost-effectiveness, and the ability to produce correctly folded and biologically active TGF-α. The resulting TGF-α human recombinant closely resembles native TGF-α in terms of structure and function, allowing for effective therapeutic intervention.Therapeutic Applications:
TGF-α human recombinant derived from yeast has shown promise in various therapeutic applications. It has been investigated for its wound-healing properties, where it promotes tissue regeneration and accelerates the healing process. Additionally, TGF-α has been explored in tissue engineering and regenerative medicine, playing a crucial role in stimulating cell proliferation and tissue development. Furthermore, TGF-α has been studied in the context of cancer research, as it is involved in tumor growth and angiogenesis, making it a potential target for anticancer therapies.Advantages and Challenges:
The use of yeast expression systems for producing TGF-α human recombinant offers several advantages, including scalability, cost-effectiveness, and the ability to produce bioactive protein. However, challenges remain, such as optimizing production processes, purification methods, and ensuring product consistency and stability. Further research is needed to address these challenges and maximize the clinical potential of TGF-α human recombinant derived from yeast.Conclusion:
TGF-α human recombinant derived from yeast represents a versatile biopharmaceutical tool with significant therapeutic potential. Its production using yeast expression systems offers advantages in terms of scalability, cost-effectiveness, and bioactivity. The therapeutic applications of TGF-α human recombinant extend to wound healing, tissue engineering, and cancer research. Continued research and development efforts are crucial to optimizing production processes, overcoming challenges, and fully exploiting the clinical benefits of TGF-α human recombinant as a therapeutic agent.
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.