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343 results found for “Mediator Complex”
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Name :
IL7 Human, HEKDescription:
Interleukin-7 Human Recombinant, HEK
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Product # :
CYT-197Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL-7 Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 19-30kDa due to glycosylation.The IL-7 is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The IL7 was lyophilized from 1mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.Citations
More Info
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Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
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Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 IL-7 in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
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Background
What is the molecular weight/Mw of IL7 HUMAN, HEK Protein?
IL7 HUMAN, HEK Protein has a total Mw of 24.5kDa.
What is the source or expression system of IL7 HUMAN, HEK Protein?
HEK.
What is the Purity of IL7 HUMAN, HEK Protein?
IL7 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IL7 HUMAN, HEK Protein?
The activity was determined by the dose dependent stimulation of the proliferation of murine 2E8 cells and is typically 0.3ng/ml corresponding to a specific activity of 3,333,334units/mg.
What applications can IL7 HUMAN, HEK Protein be used in?
IL7 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL7 HUMAN, HEK Protein?
The endotoxin level is minimal, IL7 HUMAN, HEK Protein was purified using conventional chromatography techniques.
Who supplies recombinant IL7 HUMAN, HEK that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of IL7 HUMAN, HEK?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TNFSF7 Human, sf9Description:
CD70 Human Recombinant, sf9
CD70 Molecule, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7 , CD27 Ligand, CD27LG, TNFSF7, CD27-L, CD27L, Tumor Necrosis Factor Ligand 8A, Surface Antigen CD70, Ki-24 Antigen, CD70 Antigen, TNLG8A.
Product # :
CYT-953Price :
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Shipped with Ice Packs
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Description
TNFSF7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 164 amino acids (39-193 a.a.) and having a molecular mass of 18.2kDa. TNFSF7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFSF7 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CD70 also known as TNFSF7 is a cytokine which binds to CD27. TNFSF7 takes part in T-cell activation as well as induces the proliferation of costimulated T-cells. Moreover, TNFSF7 enhances the generation of cytolytic T-cells. Among the diseases which are associated with TNFSF7: Include acute myocarditis & Myocarditis.
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Synonyms
CD70 Molecule, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7 , CD27 Ligand, CD27LG, TNFSF7, CD27-L, CD27L, Tumor Necrosis Factor Ligand 8A, Surface Antigen CD70, Ki-24 Antigen, CD70 Antigen, TNLG8A.
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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
ADPQRFAQAQ QQLPLESLGW DVAELQLNHT GPQQDPRLYW QGGPALGRSF LHGPELDKGQ LRIHRDGIYM VHIQVTLAIC SSTTASRHHP TTLAVGICSP ASRSISLLRL SFHQGCTIAS QRLTPLARGD TLCTNLTGTL LPSRNTDETF FGVQWVRPHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2D3 HumanDescription:
Ubiquitin Conjugating Enzyme E2D3 Human Recombinant
Ubiquitin-conjugating enzyme E2 D3, EC 6.3.2.19, Ubiquitin-protein ligase D3, Ubiquitin carrier protein D3, Ubiquitin-conjugating enzyme E2-17 kDa 3, E2(17)KB 3, UBC4/5, UBCH5C, MGC5416, MGC43926, UBE2D3.
Product # :
ENZ-343Price :
Quantity :
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Shipped with Ice Packs
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Description
UBE2D3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-149a.a.) and having a molecular mass of 19.1kDa. UBE2D3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBE2D3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
UBE2D3 enzymes are human homologs of the yeast UBC4/5 family and play many important regulatory roles in inflammation and cancer. UbcH5a mediates the degradation of a myriad of short-lived regulatory proteins (such as p53 in the presence of E6/E6-AP or MDM2, c-Fos, I?B?, p105) and abnormal proteins. UBE2D3 has 88% and 89% sequence identity with UbcH5a and UbcH5b respectively.
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Synonyms
Ubiquitin-conjugating enzyme E2 D3, EC 6.3.2.19, Ubiquitin-protein ligase D3, Ubiquitin carrier protein D3, Ubiquitin-conjugating enzyme E2-17 kDa 3, E2(17)KB 3, UBC4/5, UBCH5C, MGC5416, MGC43926, UBE2D3.
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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 MLSNRKCLSK ELSDLARDPP AQCSAGPVGD DMFHWQATIM GPNDSPYQGG VFFLTIHFPT DYPFKPPKVA FTTRIYHPNI NSNGSICLDI LRSQWSPALT ISKVLLSICS LLCDPNPDDP LVPEIARIYK TDRDKYNRIS REWTQKYAM.
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 :
CNOT8 HumanDescription:
CCR4-NOT Transcription Complex, Subunit 8 Human Recombinant
CCR4-NOT transcription complex subunit 8, CAF1, CALIF, hCAF1, POP2, CAF1-like protein, CAF2, CCR4-associated factor 8, Caf1b, CNOT8.
Product # :
PRO-1517Price :
Quantity :
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Shipped with Ice Packs
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Description
CNOT8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 35.9 kDa.CNOT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CNOT8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CCR4-NOT Transcription Complex, Subunit 8 (CNOT8) is a part of the CAF1 family. CNOT8 is a ubiquitous transcription factor necessary for a varied set of processes and functions as part of the CCR-NOT complex. The CCR4-NOT complex which functions as general transcription regulation complex binds BTG2 and holds CHAF1A, CHAF1B, CNOT1, CNOT2, CNOT3, CNOT4, CNOT6 and CNOT8
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Synonyms
CCR4-NOT transcription complex subunit 8, CAF1, CALIF, hCAF1, POP2, CAF1-like protein, CAF2, CCR4-associated factor 8, Caf1b, CNOT8.
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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 MGSMPAALVE NSQVICEVWA SNLEEEMRKI REIVLSYSYI AMDTEFPGVV VRPIGEFRSS IDYQYQLLRC NVDLLKIIQL GLTFTNEKGE YPSGINTWQF NFKFNLTEDM YSQDSIDLLA NSGLQFQKHE EEGIDTLHFA ELLMTSGVVL CDNVKWLSFH SGYDFGYMVK LLTDSRLPEE EHEFFHILNL FFPSIYDVKY LMKSCKNLKG GLQEVADQLD LQRIGRQHQA GSDSLLTGMA FFRMKELFFE DSIDDAKYCG RLYGLGTGVA QKQNEDVDSA QEKMSILAII NNMQQ.
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 :
ELP5 HumanDescription:
Elongator Acetyltransferase Complex Subunit 5 Human Recombinant
C17orf81, DERP6, HSPC002, MST071, MSTP071, Dermal papilla-derived protein 6, S-phase 2 protein, ELP5.
Product # :
PRO-1660Price :
Quantity :
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Shipped with Ice Packs
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Description
ELP5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-316 a.a.) and having a molecular mass of 37.2kDa.ELP5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ELP5 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Elongator acetyltransferase complex subunit 5 (ELP5) is a member of the ELP5 family. ELP5 functions as subunit of the RNA polymerase II elongator complex, which is a histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is participated in transcriptional elongation. Elongator plays a role in chromatin remodeling and is involved in acetylation of histones H3 and probably H4. ELP5 takes part in cell migration and is widely expressed in in heart, brain, liver, skeletal muscle and testis.
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Synonyms
C17orf81, DERP6, HSPC002, MST071, MSTP071, Dermal papilla-derived protein 6, S-phase 2 protein, ELP5.
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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 MGSMTPSEGA RAGTGRELEM LDSLLALGGL VLLRDSVEWE GRSLLKALVK KSALCGEQVH ILGCEVSEEE FREGFDSDIN NRLVYHDFFR DPLNWSKTEE AFPGGPLGAL RAMCKRTDPV PVTIALDSLS WLLLRLPCTT LCQVLHAVSH QDSCPGDSSS VGKVSVLGLL HEELHGPGPV GALSSLAQTE VTLGGTMGQA SAHILCRRPR QRPTDQTQWF SILPDFSLDL QEGPSVESQP YSDPHIPPVD PTTHLTFNLH LSKKEREARD SLILPFQFSS EKQQALLRPR PGQATSHIFY EPDAYDDLDQ EDPDDDLDI.
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 :
GOSR2 HumanDescription:
Golgi SNAP Receptor Complex Member 2 Human Recombinant
Bos1, EPM6, GS27, Membrin, Golgi SNAP receptor complex member 2, 27 kDa Golgi SNARE protein, GOSR2.
Product # :
PRO-1399Price :
Quantity :
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Shipped with Ice Packs
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Description
GOSR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190a.a) and having a molecular mass of 24.6kDa. GOSR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
GOSR2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Golgi SNAP receptor complex member 2 isoform A (GOSR2) is a part of the SNARE Protein family which consists of important trafficking proteins between the endoplasmic reticulum and the Golgi and between Golgi subcompartments. GOSR2 is located near a locus implicated in familial essential hypertension, indicating that it is a potential candidate gene for this disease. GOSR2 exists as cytoplasmically oriented integral membrane proteins.
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Synonyms
Bos1, EPM6, GS27, Membrin, Golgi SNAP receptor complex member 2, 27 kDa Golgi SNARE protein, GOSR2.
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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 MGSMDPLFQQ THKQVHEIQS CMGRLETADK QSVHIVENEI QASIDQIFSR LERLEILSSK EPPNKRQNAR LRVDQLKYDV QHLQTALRNF QHRRHAREQQ ERQREELLSR TFTTNDSDTT IPMDESLQFN SSLQKVHNGM DDLILDGHNI LDGLRTQRLT LKGTQKKILD IANMLGLSNT VMRLIEKRAF QDK.
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 :
IFIH1 HumanDescription:
Interferon Induced With Helicase C Domain 1 Human Recombinant
Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.
Product # :
PRO-1505Price :
Quantity :
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Shipped with Ice Packs
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Description
IFIH1 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 152,000 Dalton. IFIH1 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
IFIH1 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.
Purity
Greater than 93.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.
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Synonyms
Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NDUFA4 HumanDescription:
NADH Dehydrogenase1 Alpha Subcomplex 4 Human Recombinant
NDUFA4, Mitochondrial Complex Associated, NADH-Ubiquinone Oxidoreductase MLRQ Subunit, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4, 9kDa, Complex I 9kDa Subunit, Complex I-MLRQ, CI-MLRQ, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4 (9kD, MLRQ), NADH Dehydrogenase [Ubiquinone] 1 Alpha Subcomplex Subunit 4, CI-9k, MLRQ, Cytochrome c oxidase subunit NDUFA4.
Product # :
ENZ-803Price :
Quantity :
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Shipped with Ice Packs
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Description
NDUFA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 104 amino acids (1-81 a.a) and having a molecular mass of 11.8kDa. NDUFA4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
NDUFA4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NADH Dehydrogenase1 Alpha Subcomplex 4 (NDUFA4) is a member of the complex I 9kDa subunit family. Mammalian complex I of mitochondrial respiratory chain is comprised of 45 different subunits. NDUFA4 protein has NADH dehydrogenase activity and oxidoreductase activity. NDUFA4 transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the NDUFA4 enzyme is assumed to be ubiquinone.
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Synonyms
NDUFA4, Mitochondrial Complex Associated, NADH-Ubiquinone Oxidoreductase MLRQ Subunit, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4, 9kDa, Complex I 9kDa Subunit, Complex I-MLRQ, CI-MLRQ, NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex, 4 (9kD, MLRQ), NADH Dehydrogenase [Ubiquinone] 1 Alpha Subcomplex Subunit 4, CI-9k, MLRQ, Cytochrome c oxidase subunit NDUFA4.
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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 MGSMLRQIIG QAKKHPSLIP LFVFIGTGAT GATLYLLRLA LFNPDVCWDR NNPEPWNKLG PNDQYKFYSV NVDYSKLKKE RPDF.
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 :
TRAPPC2 HumanDescription:
Trafficking Protein Particle Complex 2 Human Recombinant
Trafficking Protein Particle Complex 2, Sedlin, SEDL, Trafficking Protein Particle Complex Subunit 2, Spondyloepiphyseal Dysplasia Late, TRAPPC2P1, HYP38334, ZNF547L, MIP2A, TRS20, SEDT, TRAPPC2.
Product # :
PRO-1272Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TRAPPC2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (1-140 a.a.) and having a molecular mass of 18.8kDa.TRAPPC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TRAPPC2 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Trafficking Protein Particle Complex 2 (TRAPPC2) is assumed to be part of a large multi-subunit complex involved in the targeting and fusion of endoplasmic reticulum-to-Golgi transport vesicles with their acceptor compartment. Moreover, the TRAPPC2 protein can bind c-myc promoter-binding protein 1 and block its transcriptional repression capability. TRAPPC2 gene mutations are a cause of spondyloepiphyseal dysplasia tarda (SEDT).
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Synonyms
Trafficking Protein Particle Complex 2, Sedlin, SEDL, Trafficking Protein Particle Complex Subunit 2, Spondyloepiphyseal Dysplasia Late, TRAPPC2P1, HYP38334, ZNF547L, MIP2A, TRS20, SEDT, TRAPPC2.
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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 MGSMSGSFYF VIVGHHDNPV FEMEFLPAGK AESKDDHRHL NQFIAHAALD LVDENMWLSN NMYLKTVDKF NEWFVSAFVT AGHMRFIMLH DIRQEDGIKN FFTDVYDLYI KFSMNPFYEP NSPIRSSAFD RKVQFLGKKH LLS.
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 :
G CSF Human, PEGDescription:
Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-018Price :
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Shipped with Ice Packs
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Description
Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.
Purity
Greater than 95.0% as determined by SEC-HPLC.
Biological Activity
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.
Citations
More Info
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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
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Physical Appearance
Colorless, clear and transparent solution.
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Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
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Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.
What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.
What is the Purity of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.
What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.
What applications can G CSF HUMAN, PEG Protein be used in?
G CSF HUMAN, PEG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PDHX AntibodyDescription:
Pyruvate Dehydrogenase Complex, Component X, Mouse Anti Human
DLDBP, E3BP, OPDX, PDX1, proX, Component X.
Product # :
ANT-725Price :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
Citations
More Info
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Introduction
Pyruvate Dehydrogenase Complex, Component X, also known as PDHX, encodes the E3 binding protein subunit of the PDH complex which contains 3 catalytic subunits. PDHX tethers E3 dimers to the E2 core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is critical for a functional PDH complex.
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Synonyms
DLDBP, E3BP, OPDX, PDX1, proX, Component X.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human PDHX mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PDHX amino acids 54-501 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
PAT1E11AT
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Applications
PDHX 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
PDHX antibody was purified from mouse ascitic fluids by protein-A 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 :
TNFRSF8 MouseDescription:
CD30 Ligand Receptor Mouse Recombinant
Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1
Product # :
CYT-1165Price :
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Description
TNFRSF8 Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 479 amino acids (19-258 aa) and having a molecular mass of 52.2kDa.TNFRSF8 is fused to a 239 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFRSF8 protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1
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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
FPTDRPLKTT CAGDLSHYPG EAARNCCYQC PSGLSPTQPC PRGPAHCRKQ CAPDYYVNED GKCTACVTCL PGLVEKAPCS GNSPRICECQ PGMHCCTPAV NSCARCKLHC SGEEVVKSPG TAKKDTICEL PSSGSGPNCS NPGDRKTLTS HATPQAMPTL ESPANDSARS LLPMRVTNLV QEDATELVKV PESSSSKARE PSPDPGNAEK NMTLELPSPG TLPDISTSEN SKEPASTAST LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
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 :
TANK HumanDescription:
TRAF Family Member-Associated NFKB Activator Human Recombinant
TRAF, TRAF2, TRAF-interacting protein, ITRAF.
Product # :
PRO-1348Price :
Quantity :
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Description
TANK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 448 amino acids (1-425a.a) and having a molecular mass of 50.2kDa. TANK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TANK protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TRAF Family Member-Associated NFKB Activator (TANK) is located in the cytoplasm and binds Either TRAF1, TRAF2 or TRAF3. TANK is an inhibitor of TRAF function which regulates TRAF protein activity via sequestering TRAFs in a dormant position in the cytoplasm. Overexpression of TANK, inhibits TRAF2-mediated NF-Kappa-B activation signaled by CD40 and both TNF receptors and also inhibits LMP1-mediated NFkappa-B activation by blocking the connection of TRAF2 with LMP1.
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Synonyms
TRAF, TRAF2, TRAF-interacting protein, ITRAF.
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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 MGSMDKNIGE QLNKAYEAFR QACMDRDSAV KELQQKTENY EQRIREQQEQ LSLQQTIIDK LKSQLLLVNS TQDNNYGCVP LLEDSETRKN NLTLDQPQDK VISGIAREKL PKVRRQEVSS PRKETSARSL GSPLLHERGN IEKTFWDLKE EFHKICMLAK AQKDHLSKLN IPDTATETQC SVPIQCTDKT DKQEALFKPQ AKDDINRGAP SITSVTPRGL CRDEEDTSFE SLSKFNVKFP PMDNDSTFLH STPERPGILS PATSEAVCQE KFNMEFRDNP GNFVKTEETL FEIQGIDPIA SAIQNLKTTD KTKPSNLVNT CIRTTLDRAA CLPPGDHNAL YVNSFPLLDP SDAPFPSLDS PGKAIRGPQQ PIWKPFPNQD SDSVVLSGTD SELHIPRVCE FCQAVFPPSI TSRGDFLRHL NSHFNGET.
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 :
il 18 HumanDescription:
Interleukin-18 Human Recombinant
IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.
Product # :
CYT-269Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 18.2 kDa. The IL-18 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.
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Synonyms
IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin 18 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL18 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 Interleukin 18 in sterile PBS at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
YFGKLESKLS VIRNLNDQVL FIDQGNRPLF EDMTDSDCRD NAPRTIFIIS MYKDSQPRGM AVTISVKCEK ISTLSCENKI ISFKEMNPPD NIKDTKSDII FFQRSVPGHD NKMQFESSSY EGYFLACEKE RDLFKLILKK EDELGDRSIM FTVQNED
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Background
Also known as IFN-gamma inducing factor, Interleukin-18 or IL18 is a protein. In humans this protein is encoded by the IL18 gene. The protein is a proinflammatory cytokine.
Mechanism
The levels of IL-18 in the human body are increased at sites of inflammation. This includes cases of rheumatoid arthritis as well as other similar conditions. Osteoblastic cells express the protein and it is capable of inhibiting osteoclast formation. It is able to do this through a variety of mechanisms.
For instance, it is able to stimulate GM-CSF. This is created by T cells and is a response to treatment using IL-18. As well as this, the cytokine does stimulate INF-y production through vivo in bone. Furthermore, the impact on bone resorption and osteoclastogenesis is increased when used in conjunction with IL-12 treatment. Studies have shown that IL-18 provides an indirect stimulus on osteoclastogenesis due to the effect it has on T lymphocytes.
Furthermore, evidence has shown that IL-18 does increase the production of OPG. This was studied in research on transgenic mice that overexpressed IL-18. In these cases osteoclasts decreased as did bone mass. This suggested that IL-18 also has an impact on bone growth.
Interactions
Research has also explored the different interactions of IL-18 on other proteins. This includes the interaction between IL-18 and IL-18R. This has been shown to decrease the power of protective immunity and increase pathogenic responses during an infection involving intracellular bacteria. This interaction suggests that the presence or absence of IL-18R signal does impact the pathogenic compared to protective immunity.
Another interaction between interleukin 19 and Astrocyte has shown that it can improve neuropathic pain processing following nerve injury. It is proposed this is due to the fact that the nociceptive signals in the spinal cord are augmented due to this reaction.
Function
Belonging to the IL-1 superfamily, this cytokine is produced by macrophages as well as various other cells. It operates after binding with the interleukin-18 receptor. Working with IL-12, the protein is then able to induce-cell mediated immunity after an infection from lipopolysaccharide and other microbial products.
Once stimulated by IL-18 other cells including natural killer and T cells then release IFN-y. This type II IFN plays a crucial part in activating the macrophages of various other cells.
Together IL12 and IL-18 are able to successfully inhibit IgE and IG1 production that is dependent on IL-4. As well as this, the protein is also able to increase IgG2a production through B cells. IL-18 will interact specifically with this type of cytokine and has a negative impact on regulation of biological activity.
Structure
Many researchers have suggested that the structure of IL-18 is a key way to understand it’s receptor activation mechanism. The structure of IL-18 closely resembles of IL-1 and has various similarities. It is folded into a beta-trefoil structure and three sites have been shown to be important for receptor activation. These were revealed through extensive mutagenesis. Two of the sites provide binding sites for the IL-18 receptor and are located in positions similar to IL-1. The third structure seems to be used for IL-18 receptor beta binding.
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 :
IL1A RatDescription:
Interleukin-1 alpha Rat Recombinant
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Product # :
CYT-381Price :
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Shipped at Room temp
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Description
Interleukin-1A Rat Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17703 Dalton. The IL-1A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Tris-HCl, pH=8.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.Citations
More Info
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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
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Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 Interleukin 1a 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-His-Ser-Phe.
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Background
What is the molecular weight/Mw of IL1A RAT Protein?
IL1A RAT Protein has a total Mw of 17.7kDa.
What is the source or expression system of IL1A RAT Protein?
Escherichia Coli.
What is the Purity of IL1A RAT Protein?
IL1A RAT Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IL1A RAT Protein?
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.
What is the amino acid sequence of IL1A RAT Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-His-Ser-Phe.
What applications can IL1A RAT Protein be used in?
IL1A RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IL1A RAT Protein?
The endotoxin level is minimal, IL1A RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SAE1 HumanDescription:
SUMO1 Activating Enzyme Subunit 1 Human Recombinant
AOS1, HSPC140, SUA1, UBLE1A, SAE1, SUMO1 Activating Enzyme Subunit 1, FLJ3091.
Product # :
ENZ-534Price :
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Shipped with Ice Packs
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Description
SAE1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 378 amino acids (1-346 a.a.) and having a molecular mass of 42.2 kDa. The SAE1 is fused to 32 amino acid T7-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SAE1 Human solution containing 20mM Tris pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SAE1 is part of the ubiquitin-activating E1 family of proteins and participates in the significant first step of the UBL1 conjugation pathway. Proteins conjugated to Ub are marked for progressive degradation by the 26S Proteasome. SAE1 acts as a UBLI E1 ligase mediating the ATP-dependent activation of UBL1. SAE1 binds with UBLE1A and UBLE1B to form a heterodimer which can bind UBL1. SAE1 is a dimeric enzyme that takes part as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. SAE1 regulates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2.
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Synonyms
AOS1, HSPC140, SUA1, UBLE1A, SAE1, SUMO1 Activating Enzyme Subunit 1, FLJ3091.
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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
MHHHHHHMAS MTGGQQMGRD LYDDDDKDRW GSMVEKEEAG GGISEEEAAQ YDRQIRLWGL EAQKRLRASR VLLVGLKGLG AEIAKNLILA GVKGLTMLDH EQVTPEDPGA QFLIRTGSVG RNRAEASLER AQNLNPMVDV KVDTEDIEKK PESFFTQFDA VCLTCCSRDV IVKVDQICHK NSIKFFTGDV FGYHGYTFAN LGEHEFVEEK TKVAKVSQGV EDGPDTKRAK LDSSETTMVK KKVVFCPVKE ALEVDWSSEK AKAALKRTTS DYFLLQVLLK FRTDKGRDPS SDTYEEDSEL LLQIRNDVLD SLGISPDLLP EDFVRYCFSE MAPVCAVVGG ILAQEIVKAL SQRDPPHNNF FFFDGMKGNG IVECLGPK.
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 :
IL 22 RatDescription:
Interleukin-22 Rat Recombinant
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Product # :
CYT-173Price :
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Shipped at Room temp
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Description
IL-22 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.6kDa.The IL22 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity is measured by its ability to induce IL-10 secretion in COLO 205 (human colon carcinoma cells). The expected ED50 for this effect is 0.15-0.75ng/ml.Citations
More Info
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Introduction
IL-22 is a member of the IL-10 family of regulatory cytokines.Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10R-beta/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family.
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Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 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 Interleukin -22 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
LPINSQCKLE AANFQQPYIV NRTFMLAKEA SLADNNTDVR LIGEELFRGV KAKDQCYLMK QVLNFTLEDV LLPQSDRFQP YMQEVVPFLT KLSIHLSPCH ISGDDQNIQK NVRQLKETVQ KLGESGEIKA IGELDLLFMS LRNACV.
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 :
IL 29 Human, Sf9Description:
Interleukin-29 Human Recombinant, Sf9
Interleukin-29, IL-29, IFN-Lambda 1, Interferon-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.
Product # :
CYT-988Price :
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Description
Interleukin-29 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 187 amino acids (20-200a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL29 is fused with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL29 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
IL-29 is distantly related to type I interferons and the IL-10 family. Expression of IL-29 is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
IFN-Lambda 1 antiviral and antiproliferative activity requires Interferon-Lambda 2 receptor tyrosine residues. -
Synonyms
Interleukin-29, IL-29, IFN-Lambda 1, Interferon-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.
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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
GPVPTSKPTT TGKGCHIGRF KSLSPQELAS FKKARDALEE SLKLKNWSCS SPVFPGNWDL RLLQVRERPV ALEAELALTL KVLEAAAGPA LEDVLDQPLH TLHHILSQLQ ACIQPQPTAG PRPRGRLHHW LHRLQEAPKK ESAGCLEASV TFNLFRLLTR DLKYVADGNL CLRTSTHPES THHHHHH.
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 :
LIN28 HumanDescription:
LIN28 Human Recombinant
CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.
Product # :
PRO-743Price :
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Description
Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (42-209) and having a molecular mass of 21.1 kDa.LIN28 is expressed with a 23 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LIN28 protein solution (0.5mg/ml) contains 20mM Tris-HCl, pH-8, 10% glycerol, 0.1mM PMSF and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE
Citations
More Info
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Introduction
LIN28 plays an important role as a 'translational enhancer', leading specific mRNAs to polysomes and therefore increasing the competence of protein synthesis. LIN28 is a marker of undifferentiated human embryonic stem cells and it enhances the efficiency of the formation of induced pluripotent stem (iPS) cells from human fibroblasts. LIN28 binds to the let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells. Overexpression of LIN28 is associated with human germ-cell tumors.
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Synonyms
CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.
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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 SSGLVPRGSHRSMGICKWFN VRMGFGFLSM TARAGVALDP PVDVFVHQSK LHMEGFRSLK EGEAVEFTFK KSAKGLESIR VTGPGGVFCI GSERRPKGKS MQKRRSKGDR CYNCGGLDHH AKECKLPPQP KKCHFCQSIS HMVASCPLKA QQGPSAQGKP TYFREEEEEI HSPTLLPEAQ N.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UBE2K HumanDescription:
Ubiquitin-Conjugating Enzyme E2K Human Recombinant
HIP2, Huntingtin Interacting protein 2, HYPG, Ubiquitin-conjugating enzyme E2-25K kDa, Ubiquitin-protein ligase, Ubiquitin carrier protein, LIG, HIP-2, E2(25K), DKFZp686J24237, OTTHUMP00000218440, EC 6.3.2.19.
Product # :
ENZ-339Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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Description
UBE2K produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-200a.a.) and having a molecular mass of 26.5kDa.UBE2K is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UBE2K protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH7.5) 1mM DTT, 50mM NaCl, and 10% glycerol.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
UBE2K belongs to the ubiquitin-conjugating enzymes family which take part in many cellular processes such as selective protein degradation, DNA repair, cell cycle control, and sporulation. In this mechanism, the ATP-coupled activation and subsequent ligation of ubiquitin are catalyzed by separate enzymes functionally linked by ubiquitin carrier protein UBC1. In addition, UBE2K is involved in Alzheimer's disease, Huntington's disease and antigen processing through its interaction with amyloid-?, huntingtin, and MHC-heavy chain proteins.
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Synonyms
HIP2, Huntingtin Interacting protein 2, HYPG, Ubiquitin-conjugating enzyme E2-25K kDa, Ubiquitin-protein ligase, Ubiquitin carrier protein, LIG, HIP-2, E2(25K), DKFZp686J24237, OTTHUMP00000218440, EC 6.3.2.19.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMANI AVQRIKREFK EVLKSEETSK NQIKVDLVDE NFTELRGEIA GPPDTPYEGG RYQLEIKIPE TYPFNPPKVR FITKIWHPNI SSVTGAICLD ILKDQWAAAM TLRTVLLSLQ ALLAAAEPDD PQDAVVANQY KQNPEMFKQT ARLWAHVYAG APVSSPEYTK KIENLCAMGF DRNAVIVALS SKSWDVETAT ELLLSN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Clusterin HumanDescription:
Clusterin Human Recombinant
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
Product # :
CYT-278Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Clusterin Human Recombinant produced in HEK is a glycosylated, polypeptide chain containing 438 amino acids and having a molecular mass of 51.27 kDa. Clusterin (1-427 a.a.) is fused to 11 a.a. flag tag at c-terminal and purified by proprietary chromatographic techniques.
Source
293 cell line (Human embryonic kidney).
Formulation
Filtered (0.4 micron) and lyophilized PBS, pH 7.5.
Purity
Greater than 95% as determined by SDS PAGE.
Citations
More Info
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Introduction
Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others. -
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.
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Physical Appearance
Filtered, White, Lyophilized 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 deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.
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Amino Acid Sequence
DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.
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Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 51.27kDa.
What is the source or expression system of CLUSTERIN Protein?
293 cell line
What is the Purity of CLUSTERIN Protein?
CLUSTERIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CLUSTERIN Protein?
The biological functionality of CLUSTERIN Protein will be determined in the future.
What is the amino acid sequence of CLUSTERIN Protein?
DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.
What applications can CLUSTERIN Protein be used in?
CLUSTERIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 29 HumanDescription:
Interleukin-29 Human Recombinant
Interleukin-29, IL-29, IFN-Lambda 1, IFN-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.
Product # :
CYT-603Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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- purity
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Description
IL-29 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2 μm filtered solution containing no additives.
Purity
Greater than 90% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
IL-29 is distantly related to type I IFNs and the IL-10 family. Expression of IL-29 is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
IFN-Lambda 1 antiviral and antiproliferative activity requires IFN-Lambda 2 receptor tyrosine residues. -
Synonyms
Interleukin-29, IL-29, IFN-Lambda 1, IFN-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN-Lambda 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 1 Recombinant 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 IL-29 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
GPVPTSKPTTT GKGCHIGRFK SLSPQELASF KKARDALEES LKLKNWSCSS PVFPGNWDLR LLQVRERPVA LEAELALTLK VLEAAAGPAL EDVLDQPLHTLHHILSQLQA CIQPQPTAGP RPRGRLHHWL HRLQEAPKKE SAGCLEASVT FNLFRLLTRD LKYVADGNLC LRTSTHPEST.
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 :
IL18BP HumanDescription:
Interleukin-18 Binding Protein Human Recombinant
Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, IL18BPa, Interleukin-18-binding protein, Tadekinig-alfa.
Product # :
CYT-728Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL18BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (31-194 a.a) and having a molecular mass of 20kDa. IL18BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL18BP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Interleukin-18 Binding Protein (IL18BP) serves as an inhibitor of the proinflammatory cytokine, IL18. IL18BP binds IL18, inhibits the binding of IL18 to its receptor, and consequently inhibits IL18-induced IFN-gamma production, resulting in reduced T-helper type 1 immune responses. The IL18BP protein is constitutively expressed and secreted in mononuclear cells. Elevated levels of IL18BP protein are detected in the intestinal tissues of patients with Crohn's disease.
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Synonyms
Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, IL18BPa, Interleukin-18-binding protein, Tadekinig-alfa.
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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 MGSTPVSQTT TAATASVRST KDPCPSQPPV FPAAKQCPAL EVTWPEVEVP LNGTLSLSCV ACSRFPNFSI LYWLGNGSFI EHLPGRLWEG STSRERGSTG TQLCKALVLE QLTPALHSTN FSCVLVDPEQ VVQRHVVLAQ LWAGLRATLP PTQEALPSSH SSPQQQG.
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 :
Midkine RatDescription:
Midkine Rat Recombinant
Midkine, MK, Mdk.
Product # :
CYT-747Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
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- biological activity
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Description
Midkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a molecular mass of 13.2kDa.The Midkine Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-100 ng/ml.Citations
More Info
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Introduction
Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis. -
Synonyms
Midkine, MK, Mdk.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Midkine Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Midkine 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 Midkine Rat 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
VAKKKDKVKK GSECSEWTWG PCTPSSKDCG MGFREGTCGA QTQRIHCKVP CNWKKEFGAD CKYKFESWGA CDGSTGTKAR QGTLKKARYN AQCQETIRVT KPCTSKTKSK AKAKKGKGKD.
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.