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1000 results found for “karyopherin”
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Name :
CDH11 HumanDescription:
Cadherin 11 Human Recombinant
CAD11, CDHOB, OB, OSF-4, Cadherin 11, Osteoblast cadherin, OB-cadherin.
Product # :
PRO-1368Price :
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Shipped with Ice Packs
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Description
CDH11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 601 amino acids (54-617 a.a) and having a molecular mass of 66.2kDa. CDH11 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CDH11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cadherin 11 (CDH11) belongs to the cadherin superfamily (integral membrane proteins) which mediate calcium-dependent cell-cell adhesion. CDH11 is defined based on lacking a HAV cell adhesion recognition sequence specific to type I cadherins. CDH11 protein’s expression in osteoblastic cell lines, and its upregulation during differentiation, suggests a specific function in bone development and maintenance. CDH11 contributes to the sorting of heterogeneous cell types.
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Synonyms
CAD11, CDHOB, OB, OSF-4, Cadherin 11, Osteoblast cadherin, OB-cadherin.
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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 KDRWGSMGWV WNQFFVIEEY TGPDPVLVGR LHSDIDSGDG NIKYILSGEG AGTIFVIDDK SGNIHATKTL DREERAQYTL MAQAVDRDTN RPLEPPSEFI VKVQDINDNP PEFLHETYHA NVPERSNVGT SVIQVTASDA DDPTYGNSAK LVYSILEGQP YFSVEAQTGI IRTALPNMDR EAKEEYHVVI QAKDMGGHMG GLSGTTKVMI TLTDVNDNPP KFPQSVYQMS VSEAAVPGEE VGRVKAKDPD IGENGLVTYN IVDGDGMESF EITTDYETQE GVIKLKKPVD FETKRAYSLK VEAANVHIDP KFISNGPFKD TVTVKIAVED ADEPPMFLAP SYIHEVQENA AAGTVVGRVH AKDPDAANSP IRYSIDRHTD LDRFFTINPE DGFIKTTKPL DREETAWLNI TVFAAEIHNR HQEAKVPVAI RVLDVNDNAP KFAAPYEGFI CESDQTKPLS NQPIVTISAD DKDDTANGPR FIFSLPPEII HNPNFTVRDN RDNTAGVYAR RGGFSRQKQD LYLLPIVISD GGIPPMSSTN TLTIKVCGCD VNGALLSCNA EAYILNAGLS T.
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 :
CNTF Human, His ActiveDescription:
Ciliary Neurotrophic Factor Human Recombinant, His Tag Active
Ciliary neurotrophic factor, CNTF, HCNTF.
Product # :
CYT-909Price :
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Description
CNTF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200 a.a) and having a molecular mass of 25kDa. CNTF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNTF protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.5), 1 mM DTT,30% Glycerol and 0.2M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 1 ug/ml.More Info
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Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
Ciliary neurotrophic factor, CNTF, HCNTF.
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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 MAFTEHSPLT PHRRDLCSRS IWLARKIRSD LTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.
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Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 25kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 1 ug/ml.
What is the amino acid sequence of CNTF Protein?
MGSSHHHHHH SSGLVPRGSH MAFTEHSPLT PHRRDLCSRS IWLARKIRSD LTALTESYVK HQGLNKNINL DSADGMPVAS TDQWSELTEA ERLQENLQAY RTFHVLLARL LEDQQVHFTP TEGDFHQAIH TLLLQVAAFA YQIEELMILL EYKIPRNEAD GMPINVGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRFIS SHQTGIPARG SHYIANNKKM.
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
YEATS4 HumanDescription:
YEATS Domain Containing 4 Human Recombinant
YEATS domain-containing protein 4, Glioma-amplified sequence 41, Gas41, NuMA-binding protein 1, NuBI-1, NuBI1, YEATS4, GAS41, YAF9, 4930573H17Rik, B230215M10Rik.
Product # :
PRO-1019Price :
Quantity :
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Shipped with Ice Packs
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Description
YEATS4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-227 a.a.) and having a molecular mass of 28.9kDa. YEATS4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
YEATS4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 2mM DTT,0.2M NaCl and 0.1mM PMSF.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
YEATS Domain Containing 4 (YEATS4) has a high sequence homology to the human MLLT1, and yeast and human MLLT3 proteins. MLLT1 and MLLT3 proteins, both belong to a group of transcription factors, which indicates that YEATS might also represent a transcription factor. YEATS is believed to be necessary for RNA transcription. The YEATS gene has been shown to be amplified in tumors.
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Synonyms
YEATS domain-containing protein 4, Glioma-amplified sequence 41, Gas41, NuMA-binding protein 1, NuBI-1, NuBI1, YEATS4, GAS41, YAF9, 4930573H17Rik, B230215M10Rik.
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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 MGSMFKRMAE FGPDSGGRVK GVTIVKPIVY GNVARYFGKK REEDGHTHQW TVYVKPYRNE DMSAYVKKIQ FKLHESYGNP LRVVTKPPYE ITETGWGEFE IIIKIFFIDP NERPVTLYHL LKLFQSDTNA MLGKKTVVSE FYDEMIFQDP TAMMQQLLTT SRQLTLGAYK HETEFAELEV KTREKLEAAK KKTSFEIAEL KERLKASRET INCLKNEIRK LEEDDQAKDI.
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 :
NREP HumanDescription:
Neuronal Regeneration Related Protein Human Recombinant
Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related Protein.
Product # :
PRO-1780Price :
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Description
NREP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (1-68) and having a molecular mass of 10.3kDa.NREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NREP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Neuronal Regeneration Related Protein (NREP) has roles in neural function. NREP promotes axonal regeneration. In addition, NREP has functions in cellular differentiation. NREP protein induces differentiation of fibroblast into myofibroblast and increases retinoic-acid regulation of lipid-droplet biogenesis. NREP down-regulates the expression of TGFB1 and TGFB2 but not of TGFB3. NREP has a role in the regulation of alveolar generation.
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Synonyms
Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related Protein.
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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 MGSMVYYPEL FVWVSQEPFP NKDMEGRLPK GRLPVPKEVN RKKNDETNAA SLTPLGSSEL RSPRISYLHF F.
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 :
CAMP HumanDescription:
Cathelicidin Antimicrobial Peptide Human Recombinant
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
Product # :
PRO-1405Price :
Quantity :
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Shipped with Ice Packs
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Description
CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
CAMP protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.
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Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
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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 MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.
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 :
Troponin C-I HumanDescription:
Cardiac Troponin C-I Complex Human Recombinant
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
Product # :
PRO-345Price :
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Shipped with Ice Packs
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Description
Recombinant Human Cardiac Troponin C-I complex produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of approximately 50kDa. The Molar ratio on cTnC to cTnI is 1:1. The Cardiac Troponin C-I is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Human Cardiac Troponin C-I complex solution contains 500 mM Nacl, 20mM Tris-HCl and 60 mM B-mercaptoethanol, pH 7.5.
Purity
Greater than 90.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Troponin Complex is a heteromeric protein playing an important role in the regulation of skeletal and cardiac muscle contraction. It consists of three subunits, Troponin I, Troponin T and TroponinC. Each subunit is responsible for part of Troponin Complex function. E.g. Troponin I inhibits ATP-ase activity of acto-myosin.Troponin T and Troponin Iare presented in cardiac muscles in different forms than in skeletal muscles. Purified subunits of rcTnI, rcTnC and rcTnT are recomplexed in vitro under appropriate conditions.
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
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Physical Appearance
Sterile Filtered colourless liquid formualtion.
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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 :
TROVE2 HumanDescription:
TROVE Domain Family Member 2 Human Recombinant
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-329Price :
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Shipped with Ice Packs
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Description
RO-60 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 60kDa. RO60 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein solution contains 6M Urea, 500mM NaCl, 500mM imidazole and 10mM Tris pH-6.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
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Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
RO-60 although stable at 4°C for 3 weeks, should be stored below -18°C. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAGEA8 HumanDescription:
Melanoma Antigen Family A, 8 Human Recombinant
Melanoma Antigen Family A8, MAGE-8 Antigen, MAGE8, Cancer/Testis Antigen 1.8, CT1.8, Cancer/Testis Antigen Family 1, Member 8, Cancer/Testis Antigen Family 1, Melanoma-Associated Antigen 8, Melanoma Antigen Family A, 8, Member 8, MAGEA8.
Product # :
PRO-2206Price :
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Shipped with Ice Packs
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Description
MAGEA8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-318 a.a) and having a molecular mass of 37.6kDa.MAGEA8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAGEA8 protein solution (0.25mg/ml) containing Phosphate Buffered Saline, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Melanoma Antigen Family A 8, also known as MAGEA8 belongs to the MAGE gene family, which includes twelve known genes, of which six are expressed in tumors. Furthermore, the MAGE genes were at first isolated from different kinds of tumors, and according to their virtually exclusive tumor-specific expression in adult tissues, they have been used as targets for cancer immunotherapy.
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Synonyms
Melanoma Antigen Family A8, MAGE-8 Antigen, MAGE8, Cancer/Testis Antigen 1.8, CT1.8, Cancer/Testis Antigen Family 1, Member 8, Cancer/Testis Antigen Family 1, Melanoma-Associated Antigen 8, Melanoma Antigen Family A, 8, Member 8, MAGEA8.
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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 MGSMLLGQKS QRYKAEEGLQ AQGEAPGLMD VQIPTAEEQK AASSSSTLIM GTLEEVTDSG SPSPPQSPEG ASSSLTVTDS TLWSQSDEGS SSNEEEGPST SPDPAHLESL FREALDEKVA ELVRFLLRKY QIKEPVTKAE MLESVIKNYK NHFPDIFSKA SECMQVIFGI DVKEVDPAGH SYILVTCLGL SYDGLLGDDQ STPKTGLLII VLGMILMEGS RAPEEAIWEA LSVMGLYDGR EHSVYWKLRK LLTQEWVQEN YLEYRQAPGS DPVRYEFLWG PRALAETSYV KVLEHVVRVN ARVRISYPSL HEEALGEEKG V.
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 :
TNIP1 HumanDescription:
TNFAIP3 Interacting Protein 1 Human Recombinant
TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-1.
Product # :
PRO-005Price :
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Description
TNIP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 458 amino acids (94-530 a.a.) and having a molecular mass of 51.8kDa. The TNIP1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TNIP1 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol, 5mM DTT and 200mM NaCl.
Purity
Greater than 75.0% as determined by SDS-PAGE.
More Info
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Introduction
TNFAIP3-interacting protein 1 (TNIP1) interacts with zinc finger protein A20/TNFAIP3 and inhibits TNF-induced NF-kappa-B-dependent gene expression by interfering with a RIP- or TRAF2-mediated transactivation signal. Furthermore, TNIP1 interacts with HIV-1 matrix protein and is packaged into virions and its overexpression can inhibit viral replication. TNIP1 can regulate matrix nuclear localization, both nuclear import of Preintegration complex (PIC) and export of GAG polyprotein and viral genomic RNA during virion production.
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Synonyms
TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-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
MGSSHHHHHH SSGLVPRGSH MSNVTASPTA PACPSDKPAP VQKPPSSGTS SEFEVVTPEE QNSPESSSHA NAMALGPLPR EDGNLMLHLQ RLETTLSVCA EEPDHGQLFT HLGRMALEFN RLASKVHKNE QRTSILQTLC EQLRKENEAL KAKLDKGLEQ RDQAAERLRE ENLELKKLLM SNGNKEGASG RPGSPKMEGT GKKAVAGQQQ ASVTAGKVPE VVALGAAEKK VKMLEQQRSE LLEVNKQWDQ HFRSMKQQYE QKITELRQKL ADLQKQVTDL EAEREQKQRD FDRKLLLAKS KIEMEETDKE QLTAEAKELR QKVKYLQDQL SPLTRQREYQ EKEIQRLNKA LEEALSIQTP PSSPPTAFGS PEGAGALLRK QELVTQNELL KQQVKIFEED FQRERSDRER MNEEKEELKK QVEKLQAQVT LSNAQLKAFK DEEKAREALR QQKRKAKA.
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 :
KIR2DL5A AntibodyDescription:
Killer Cell Immunoglobulin-Like Receptor, 2 Domains Long Cytoplasmic Tail 5A, Mouse Anti Human
Killer Cell Immunoglobulin Like Receptor, Two Ig Domains And Long Cytoplasmic Tail 5A, Killer Cell Immunoglobulin-Like Receptor, Two Domains, Long Cytoplasmic Tail 5A, KIR2DL5, CD158F, Killer Cell Immunoglobulin-Like Receptor, Two Domains, Long Cytoplasmic Tail, 5, Killer Cell Immunoglobulin-Like Receptor KIR2DL5A, Killer Cell Immunoglobulin-Like Receptor 2DL5A, CD158f1 Antigen, KIR2DL5.1, KIR2DL5.3, CD158F1, KIR2DL5A.
Product # :
ANT-750Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Killer cell immunoglobulin-like receptor 2DL5A or KIR2DL5A is part of the killer cell Ig-like receptor (KIR) family. KIR2DL5A is atype I transmembrane glycoprotein. The protein is detected on the cell membrane as a monomer who, once tyrosine is phosphorylated, recruits the Src homology region 2-includes protein tyrosine phosphatase-2. Hence, KIR2DL5A is an inhibitory receptor gathering a combination of genetic, structural, and functional features unique among KIR, suggesting that KIR2DL5A plays a crucial role in innate immunity.
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Synonyms
Killer Cell Immunoglobulin Like Receptor, Two Ig Domains And Long Cytoplasmic Tail 5A, Killer Cell Immunoglobulin-Like Receptor, Two Domains, Long Cytoplasmic Tail 5A, KIR2DL5, CD158F, Killer Cell Immunoglobulin-Like Receptor, Two Domains, Long Cytoplasmic Tail, 5, Killer Cell Immunoglobulin-Like Receptor KIR2DL5A, Killer Cell Immunoglobulin-Like Receptor 2DL5A, CD158f1 Antigen, KIR2DL5.1, KIR2DL5.3, CD158F1, KIR2DL5A.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human KIR2DL5A mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human KIR2DL5A amino acids 22-238 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
PAT11C11AT.
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Applications
KIR2DL5A antibody has been tested by ELISA, Western blot analysis and ICC/IF 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
KIR2DL5A 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 :
NUCB2 HumanDescription:
Nucleobindin-2 Human Recombinant
Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.
Product # :
PRO-492Price :
Quantity :
Shipping Method :
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Description
The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 9.7kDa containing 82 amino acid residues of the human NUCB2.
Source
Escherichia Coli.
Formulation
The NUCB2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.
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Synonyms
Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized NUCB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NUCB2 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 NUCB2 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
VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.
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 :
AAGAB HumanDescription:
Alpha & Gamma-Adaptin Binding Protein Human Recombinant
P34, Alpha- and gamma-adaptin-binding protein p34.
Product # :
PRO-1479Price :
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Shipping Method :
Shipped with Ice Packs
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Description
AAGAB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-315 a.a.) and having a molecular mass of 36.7kDa.AAGAB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AAGAB protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.
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Synonyms
P34, Alpha- and gamma-adaptin-binding protein p34.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAGVPCALV TSCSSVFSGD QLVQHILGTE DLIVEVTSND AVRFYPWTID NKYYSADINL CVVPNKFLVT AEIAESVQAF VVYFDSTQKS GLDSVSSWLP LAKAWLPEVM ILVCDRVSED GINRQKAQEW CIKHGFELVE LSPEELPEED DDFPESTGVK RIVQALNANV WSNVVMKNDR NQGFSLLNSL TGTNHSIGSA DPCHPEQPHL PAADSTESLS DHRGGASNTT DAQVDSIVDP MLDLDIQELA SLTTGGGDVE NFERLFSKLK EMKDKAATLP HEQRKVHAEK VAKAFWMAIG GDRDEIEGLS SDEEH.
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 :
MMP10 HumanDescription:
Matrix Metallopeptidase 10 Human Recombinant
SL-2, STMY2, Stromelysin-2, Matrix metalloproteinase-10, MMP-10, Transin-2, MMP10.
Product # :
ENZ-764Price :
Quantity :
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Shipped with Ice Packs
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Description
MMP10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (99-476a.a) and having a molecular mass of 45.4kDa. MMP10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MMP10 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
MMP10 (Matrix Metallopeptidase 10) which is a part of the matrix metalloproteinase (MMP) is activating procollagenase. MMP10 is part of a cluster of MMP genes which localize to chromosome 11q22.3. MMP10 takes part in the breakdown of extracellular matrix in normal physiological processes, like embryonic development, reproduction, and tissue remodeling, as also in disease processes, such as arthritis and metastasis. The majority MMP's are secreted as inactive proproteins that are activated when cleaved by extracellular proteinases. MMP10 encodes an enzyme which degrades proteoglycans and fibronectin.
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Synonyms
SL-2, STMY2, Stromelysin-2, Matrix metalloproteinase-10, MMP-10, Transin-2, MMP10.
-
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 MGSFSSFPGM PKWRKTHLTY RIVNYTPDLP RDAVDSAIEK ALKVWEEVTP LTFSRLYEGE ADIMISFAVK EHGDFYSFDG PGHSLAHAYP PGPGLYGDIH FDDDEKWTED ASGTNLFLVA AHELGHSLGL FHSANTEALM YPLYNSFTEL AQFRLSQDDV NGIQSLYGPP PASTEEPLVP TKSVPSGSEM PAKCDPALSF DAISTLRGEY LFFKDRYFWR RSHWNPEPEF HLISAFWPSL PSYLDAAYEV NSRDTVFIFK GNEFWAIRGN EVQAGYPRGI HTLGFPPTIR KIDAAVSDKE KKKTYFFAAD KYWRFDENSQ SMEQGFPRLI ADDFPGVEPK VDAVLQAFGF FYFFSGSSQF EFDPNARMVT HILKSNSWLH C.
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 :
CYB5R3 HumanDescription:
Cytochrome B5 Reductase 3 Human Recombinant
Cytochrome b5 reductase 3, DIA1, B5R, Diaphorase (NADH) (cytochrome b-5 reductase), diaphorase-1, NADH-cytochrome b5 reductase 3 membrane-bound form, NADH-cytochrome b5 reductase 3 soluble form, Diaphorase-1, EC 1.6.2.2.
Product # :
PRO-1026Price :
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Description
CYB5R3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 300 amino acids (27-301) and having a molecular mass of 34.0kDa.CYB5R3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CYB5R3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CYB5R3 is a cytochrome b5 reductase, which includes a membrane-bound form in somatic cells (anchored in the endoplasmic reticulum, mitochondrial and other membranes) and a soluble form in erythrocytes. The membrane-bound form exists mainly on the cytoplasmic side of the endoplasmic reticulum and functions in desaturation and elongation of fatty acids, in cholesterol biosynthesis, and in drug metabolism. The erythrocyte form is located in a soluble fraction of circulating erythrocytes and is involved in methemoglobin reduction. The membrane-bound form has both membrane-binding and catalytic domains, while the soluble form has only the catalytic domain. Mutations in this gene cause methemoglobinemias.
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Synonyms
Cytochrome b5 reductase 3, DIA1, B5R, Diaphorase (NADH) (cytochrome b-5 reductase), diaphorase-1, NADH-cytochrome b5 reductase 3 membrane-bound form, NADH-cytochrome b5 reductase 3 soluble form, Diaphorase-1, EC 1.6.2.2.
-
Physical Appearance
Sterile filtered yellowish 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
MGSSHHHHHH SSGLVPRGSH MGSHMFQRST PAITLESPDI KYPLRLIDRE IISHDTRRFR FALPSPQHIL GLPVGQHIYL SARIDGNLVV RPYTPISSDD DKGFVDLVIK VYFKDTHPKF PAGGKMSQYL ESMQIGDTIE FRGPSGLLVY QGKGKFAIRP DKKSNPIIRT VKSVGMIAGG TGITPMLQVI RAIMKDPDDH TVCHLLFANQ TEKDILLRPE LEELRNKHSA RFKLWYTLDR APEAWDYGQG FVNEEMIRDH LPPPEEEPLV LMCGPPPMIQ YACLPNLDHV GHPTERCFVF.
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 :
ANGPT1 HumanDescription:
Angiopoietin-1 Human Recombinant
Angiopoietin 1, KIAA0003, ANG-1, AGP1, AGPT.
Product # :
CYT-074Price :
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Description
ANGPT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 480 amino acids (20-498) and having a molecular mass of 55.6 kDa.The ANGPT1 is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ANGPT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 5% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
ANGPT1 is an angiogenic factor which intervenes in blood vessel maturation and takes part in endothelial development. ANGPT1 is a secreted ligand for Tie-2, a cell surface receptor tyrosine kinase expressed in endothelial and hemopoietic cells. The glycosylated ANGPT1 protein has a coiled-coil region in the amino terminus and a fibrinogen-like domain at the carboxy terminus.
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Synonyms
Angiopoietin 1, KIAA0003, ANG-1, AGP1, AGPT.
-
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
MSNQRRSPEN SGRRYNRIQH GQCAYTFILP EHDGNCREST TDQYNTNALQ RDAPHVEPDF SSQKLQHLEH VMENYTQWLQ KLENYIVENM KSEMAQIQQN AVQNHTATML EIGTSLLSQT AEQTRKLTDV ETQVLNQTSR LEIQLLENSL STYKLEKQLL QQTNEILKIH EKNSLLEHKI LEMEGKHKEE LDTLKEEKEN LQGLVTRQTY IIQELEKQLN RATTNNSVLQ KQQLELMDTV HNLVNLCTKE GVLLKGGKRE EEKPFRDCAD VYQAGFNKSG IYTIYINNMP EPKKVFCNMD VNGGGWTVIQ HREDGSLDFQ RGWKEYKMGF GNPSGEYWLG NEFIFAITSQ RQYMLRIELM DWEGNRAYSQ YDRFHIGNEK QNYRLYLKGH TGTAGKQSSL ILHGADFSTK DADNDNCMCK CALMLTGGWW FDACGPSNLN GMFYTAGQNH GKLNGIKWHY FKGPSYSLRS TTMMIRPLDF
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Background
This factor was found in the conditioned medium of the human neuroepithelioma cell line SHEP1 and the mouse myoblast cell line C2C12ras. The cDNA encoding a protein of 498 amino acids was isolated by using a secretion-trap expression cloning procedure exploiting the presence of a signal sequence present in growth factors that are secreted by producer cells (Davis et al, 1996). Murine and human factors show 97 % identity at the amino acid level. For a related factor see: CDT6. The human gene has been mapped to chromosome 8q22.3-q23 (Cheung et al, 1998).
The expression of angiopoietin-1 mRNA is downregulated by PDGF, EGF, IL1-beta, and TGF-beta (Enholm et al, 1997).
Angiopoietin-1 is a ligand for the receptor-like tyrosine kinase designated TIE-2 (Davis et al, 1996). Binding of Angiopoietin-1 to its receptor induces tyrosine phosphorylation of the cytoplasmic receptor domain. A naturally occuring antagonist of Angiopoietin-1 binding to TIE-2 is Angiopoietin-2. Angiopoietin-1 also binds to the TIE-1 receptor and this interaction appears to be critical for the development of the right-hand side venous system. It is dispensable for the left-hand side venous system, suggesting that right-hand and left-hand side vascular networks are established early before asymmetrical features of the network become morphologically discernible Loughna and Sato, 2001).
Angiopoietin-1 does not directly promote the growth of cultured endothelial cells. Angiopoietin-1 is chemotactic for endothelial cells (Witzenbichler et al, 1998). Excess soluble TIE-2 receptors abolish the chemotactic response of endothelial cells toward angiopoietin-1. Angiopoietin-1 has been shown to counteract cell death by apoptosis in cultured endothelial cells (Holash et al, 1999). Angiopoietin-1 also acts as an apoptosis survival factor for endothelial cells and this effect is augmented by the presence of VEGF (Kwak et al, 1999).
Angiopoietin-2 dose-dependently blocks directed migration toward Angiopoietin-1. Carlson et al (2001) have shown that Ang-1 binds rather selectively to vitronectin and that Ang-1 can directly support adhesion of human umbilical vein endothelial cells and fibroblasts in a process mediated by integrins.
The physiologic roles of Angiopoietin-1 and its receptor are limited to angiogenic processes that occur subsequent to the earlier vasculogenic and angiogenic actions of the VEGF family and their receptors. However, it is unlike most of the known angiogenesis factors such as VEGF and other classical endothelial cell growth factors in that addition of the factor to cultures of endothelial cells does not directly promote cell growth even though the TIE-2 receptor becomes activated. Angiopoietin-1 also appears to be incapable of inducing the formation of tubules by endothelial cells.
Angiopoietins can potentiate the effects of other angiogenic cytokines. An investigation of the impact of angiopoietins on neovascularization in vivo in the cornea micropocket assay of neovascularization demonstrates that neither Angiopoietin-1 nor Angiopoietin-2 alone promote neovascularization. Holash et al (1999) have shown that a subset of tumors initially grows by coopting existing host vessels. Regression of these vessels via a process that involves disruption of interactions between endothelial cells and smooth muscle cells as well as cell death by apoptosis of endothelial cells first causes loss of tumour cells before angiogenesis begins at the tumor margin and the tumor is rescued under the influence of VEGF, Angiopoietin-1, and probably other angiogenic stimuli.
The embryonic expression pattern of Angiopoietin-1 suggests that it plays a particularly important role in the developing heart. Angiopoietin-1 is expressed highly in the myocardial wall surrounding the endocardium expressing TIE-2. Expression of Angiopoietin-1 becomes much more widespread later in development.
ANGPT1 Protein has a total Mw of 55.6kDa.
What is the source or expression system of ANGPT1 Protein?
Escherichia Coli.
What is the Purity of ANGPT1 Protein?
ANGPT1 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPT1 Protein?
The biological functionality of ANGPT1 Protein will be determined in the future.
What is the amino acid sequence of ANGPT1 Protein?
MSNQRRSPEN SGRRYNRIQH GQCAYTFILP EHDGNCREST TDQYNTNALQ RDAPHVEPDF SSQKLQHLEH VMENYTQWLQ KLENYIVENM KSEMAQIQQN AVQNHTATML EIGTSLLSQT AEQTRKLTDV ETQVLNQTSR LEIQLLENSL STYKLEKQLL QQTNEILKIH EKNSLLEHKI LEMEGKHKEE LDTLKEEKEN LQGLVTRQTY IIQELEKQLN RATTNNSVLQ KQQLELMDTV HNLVNLCTKE GVLLKGGKRE EEKPFRDCAD VYQAGFNKSG IYTIYINNMP EPKKVFCNMD VNGGGWTVIQ HREDGSLDFQ RGWKEYKMGF GNPSGEYWLG NEFIFAITSQ RQYMLRIELM DWEGNRAYSQ YDRFHIGNEK QNYRLYLKGH TGTAGKQSSL ILHGADFSTK DADNDNCMCK CALMLTGGWW FDACGPSNLN GMFYTAGQNH GKLNGIKWHY FKGPSYSLRS TTMMIRPLDF
What applications can ANGPT1 Protein be used in?
ANGPT1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPT1 Protein?
The endotoxin level is minimal, ANGPT1 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 :
NDFIP1 HumanDescription:
Nedd4 Family Interacting Protein 1 Human Recombinant
N4WBP5, NEDD4 family-interacting protein 1, Breast cancer-associated protein SGA-1M, NEDD4 WW domain-binding protein 5, Putative MAPK-activating protein PM13, Putative NF-kappa-B-activating protein 164, Putative NFKB and MAPK-activating protein,NDFIP1.
Product # :
PRO-1806Price :
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Description
NDFIP1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 139 amino acids (1-116) and having a molecular mass of 14.8kDa. NDFIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDFIP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Nedd4 Family Interacting Protein 1 (NDFIP1) is a part of a small group of evolutionarily conserved proteins having 3 ransmembrane domains. NDFIP1 is a possible target for ubiquitination by the Nedd4 family of proteins. NDFIP, which is a member of a family of integral Golgi membrane proteins, also modulates EGFR signaling through multiple pathways.
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Synonyms
N4WBP5, NEDD4 family-interacting protein 1, Breast cancer-associated protein SGA-1M, NEDD4 WW domain-binding protein 5, Putative MAPK-activating protein PM13, Putative NF-kappa-B-activating protein 164, Putative NFKB and MAPK-activating protein,NDFIP1.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMALALAA LAAVEPACGS RYQQLQNEEE SGEPEQAAGD APPPYSSISA ESAAYFDYKD ESGFPKPPSY NVATTLPSYD EAERTKAEAT IPLVPGRDED FVGRDDFDDA DQLRIGNDG.
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 :
APRIL HumanDescription:
APRIL Human Recombinant
Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.
Product # :
CYT-815Price :
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Description
APRIL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (105-247) and having a molecular mass of 17.6kDa.APRIL is fused to a 16 amino acid T7-tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
APRIL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
APRIL which is a part of the TNF ligand superfamily (TNFSF13) is a type II transmembrane protein. Normally, APRIL expression is low in tissues, but is elevated in numerous types of tumors and transformed cell lines.
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Synonyms
Tumor necrosis factor ligand superfamily member 13, A proliferation-inducing ligand, APRIL, TNF- and APOL-related leukocyte expressed ligand 2, TALL-2, TNF-related death ligand 1, TRDL-1, CD256, TNFSF13, TALL2, ZTNF2, UNQ383/PRO715.
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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
MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.
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Background
APRIL Human Recombinant: Expanding the Horizons of Immunotherapy
Abstract:
APRIL (A Proliferation-Inducing Ligand) is a promising molecule within the tumor necrosis factor (TNF) superfamily that plays a pivotal role in immune regulation. This research paper provides an overview of APRIL human recombinant, exploring its potential applications in immunotherapy. Understanding the mechanisms and therapeutic implications of APRIL holds promise in the field of immune-related disorders. This article presents a concise analysis of APRIL, highlighting its potential as a therapeutic target.Introduction:
Immunotherapy has revolutionized the treatment of various diseases by harnessing the power of the immune system. APRIL, a member of the TNF superfamily, has emerged as a potential candidate for immunotherapeutic interventions. This paper provides an overview of APRIL, shedding light on its structure, function, and potential applications in immunotherapy.APRIL Structure and Function:
APRIL is a transmembrane protein that can be proteolytically cleaved, leading to the generation of soluble forms. It interacts with its receptors, such as BCMA and TACI, to regulate immune responses. APRIL influences B-cell activation, proliferation, and antibody production, making it a compelling target for immunotherapeutic strategies.Immunotherapeutic Applications of APRIL Human Recombinant:
APRIL human recombinant holds great potential in immunotherapy. By modulating APRIL activity, it may be possible to enhance immune responses against cancer cells or dampen immune dysregulation in autoimmune disorders. Additionally, APRIL-based therapeutics could be developed to target specific immune cell populations or enhance the efficacy of existing immunotherapies.Challenges and Future Directions:
Although APRIL shows promise, there are challenges to overcome. Further research is needed to elucidate the precise mechanisms of APRIL-mediated immune regulation and identify optimal therapeutic approaches. Additionally, safety considerations and potential side effects must be thoroughly evaluated.Conclusion:
APRIL human recombinant represents a valuable tool for advancing immunotherapy. Understanding the structure, function, and therapeutic potential of APRIL opens up new avenues for treating immune-related disorders. Continued research and development in this field have the potential to revolutionize the landscape of immunotherapy, improving patient outcomes and expanding the possibilities for personalized medicine.What is the molecular weight/Mw of APRIL Protein?
APRIL Protein has a total Mw of 17.6kDa.
What is the source or expression system of APRIL Protein?
Escherichia Coli.
What is the Purity of APRIL Protein?
APRIL Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of APRIL Protein?
The biological functionality of APRIL Protein will be determined in the future.
What is the amino acid sequence of APRIL Protein?
MASMTGGQQM GRGSHMAVLT QKQKKQHSVL HLVPINATSK DDSDVTEVMW QPALRRGRGL QAQGYGVRIQ DAGVYLLYSQ VLFQDVTFTM GQVVSREGQG RQETLFRCIR SMPSHPDRAY NSCYSAGVFH LHQGDILSVI IPRARAKLNL SPHGTFLGL.
What applications can APRIL Protein be used in?
APRIL Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APRIL Protein?
The endotoxin level is minimal, APRIL 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 :
NIP7 HumanDescription:
Nuclear Import 7 Homolog Human Recombinant
Nuclear Import 7 Homolog, 60S ribosome subunit biogenesis protein NIP7 homolog KD93, CGI-37, HSPC031, FLJ10296, NIP7.
Product # :
PRO-780Price :
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Description
NIP7 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-180 a.a.) and having a molecular mass of 21.5kDa. NIP7 is fused to 8 amino acids His Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NIP7 protein solution contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
60S ribosome subunit biogenesis protein NIP7 homolog (NIP7) belongs to NIP7 family and contains 1 PUA domain. NIP7 interacts with pre-ribosome complex and may bind to RNA. NIP7 is vital for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.
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Synonyms
Nuclear Import 7 Homolog, 60S ribosome subunit biogenesis protein NIP7 homolog KD93, CGI-37, HSPC031, FLJ10296, NIP7.
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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.
-
Amino Acid Sequence
MRPLTEEETR VMFEKIAKYI GENLQLLVDR PDGTYCFRLH NDRVYYVSEK IMKLAANISG DKLVSLGTCFGKFTKTHKFR LHVTALDYLA PYAKYKVWIK PGAEQSFLYG NHVLKSGLGR ITENTSQYQG VVVYSMADIPLGFGVAAKST QDCRKVDPMA IVVFHQADIG EYVRHEETLT 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 :
EFNA3 Human, Sf9Description:
Ephrin A3 Human Recombinant, Sf9
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
Product # :
PRO-2614Price :
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Description
EFNA3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 434 amino acids (23-214aa) and having a molecular mass of 48.7kDaEFNA3 is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The Fractalkine solution (0.5 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
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Introduction
EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.
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Synonyms
Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPQGPGGAL GNRHAVYWNS SNQHLRREGY TVQVNVNDYL DIYCPHYNSS GVGPGAGPGP
GGGAEQYVLY MVSRNGYRTC NASQGFKRWE CNRPHAPHSP IKFSEKFQRY SAFSLGYEFH
AGHEYYYIST PTHNLHWKCL RMKVFVCCAS TSHSGEKPVP TLPQFTMGPN VKINVLEDFE
GENPQVPKLE KSISGLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV
TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY
KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV
EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH
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 :
EFNA5 HumanDescription:
Ephrin A5 Human Recombinant
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
Product # :
PRO-2327Price :
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Shipped with Ice Packs
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Description
EFNA5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 422 amino acids (21-203 a.a.) and having a molecular mass of 48.1kDa. EFNA5 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EFNA5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Ephrin A5 (EFNA5) is a part of the ephrin ligand family which binds the members of ephrin receptor subfamily of tyrosine kinases and stimulates contact-dependent bidirectional signaling into neighboring cells. EFNA5 is mainly expressed in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney.
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Synonyms
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
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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
QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH 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.
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Name :
EIF1AX HumanDescription:
Eukaryotic Translation Initiation Factor 1 X-linked Human Recombinant
eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.
Product # :
PRO-253Price :
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Shipped with Ice Packs
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Description
EIF1AX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 150 amino acids (1-144a.a.) and having a molecular wieght of 18.6kDa. EIF1AX is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF1AX protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 5mM DTT, 200mM NaCl and 40% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
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Introduction
EIF1AX is an important eukaryotic translation initiation factor. EIF1AX is essential for the binding of the 43S complex (a 40S subunit, eIF2/GTP/Met-tRNAi and eIF3) to the 5'' end of capped RNA. EIF1AP1 is needed for maximal rate of protein biosynthesis. EIF1AX increases ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA (I) to 40 S ribosomal subunits.
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Synonyms
eukaryotic translation initiation factor 1A, X-linked, eIF-4C, EIF1A, EIF4C, eIF-1A, EIF1AP1.
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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 MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM CFDGVKRLCH IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA RSLKAYGELP EHAKINETDT FGPGDDDEIQ FDDIGDDDED IDDI
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 :
STAMBP HumanDescription:
STAM Binding Protein Human Recombinant
STAM-binding protein, Associated molecule with the SH3 domain of STAM, Endosome-associated ubiquitin isopeptidase, AMSH, EC 3.1.2.15, EC 3.4.19, MICCAP.
Product # :
PRO-017Price :
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Shipping Method :
Shipped with Ice Packs
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Description
STAMBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424) and having a molecular mass of 50kDa. STAMBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STAMBP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE..
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Introduction
STAM Binding Protein (STAMBP) is a zinc metalloprotease which specifically cleaves Lys-63-linked polyubiquitin chains, however it doesn’t cleave Lys-48-linked polyubiquitin chains. STAMBP has a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. In addition, STAMBP potentiates BMP signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. STAMBP also has a major role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is essential for efficient EGFR degradation but not for its internalization. STAMBP is also involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.
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Synonyms
STAM-binding protein, Associated molecule with the SH3 domain of STAM, Endosome-associated ubiquitin isopeptidase, AMSH, EC 3.1.2.15, EC 3.4.19, MICCAP.
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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 MGSMSDHGDV SLPPEDRVRA LSQLGSAVEV NEDIPPRRYF RSGVEIIRMA SIYSEEGNIE HAFILYNKYI TLFIEKLPKH RDYKSAVIPE KKDTVKKLKE IAFPKAEELK AELLKRYTKE YTEYNEEKKK EAEELARNMA IQQELEKEKQ RVAQQKQQQL EQEQFHAFEE MIRNQELEKE RLKIVQEFGK VDPGLGGPLV PDLEKPSLDV FPTLTVSSIQ PSDCHTTVRP AKPPVVDRSL KPGALSNSES IPTIDGLRHV VVPGRLCPQF LQLASANTAR GVETCGILCG KLMRNEFTIT HVLIPKQSAG SDYCNTENEE ELFLIQDQQG LITLGWIHTH PTQTAFLSSV DLHTHCSYQM MLPESVAIVC SPKFQETGFF KLTDHGLEEI SSCRQKGFHP HSKDPPLFCS CSHVTVVDRA VTITDLR.
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 :
ERO1L HumanDescription:
ERO1-Like Human Recombinant
ERO1-Like (S. Cerevisiae), Endoplasmic Oxidoreductin-1-Like Protein, Oxidoreductin-1-L-Alpha, ERO1-L-Alpha, ERO1LA, ERO1-L, ERO1 (S. Cerevisiae)-Like, ERO1-Like Protein Alpha, ERO1-Alpha, EC 1.8.4.-, EC 1.8.4, ERO1A, ERO1L.
Product # :
PRO-1957Price :
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Shipping Method :
Shipped with Ice Packs
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Description
ERO1L Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 468 amino acids (24-468) and having a molecular mass of 54.4 kDa.ERO1L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ERO1L solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ERO1-like protein alpha (ERO1L) is an essential oxidoreductase, which oxidizes proteins and is necessary for the folding of immunoglobulins. ERO1L covalently binds with PDI (protein disulfide-isomerase) and jointly they generate disulfide bonds between proteins in the endoplasmic reticulum. ERO1L is stimulated by hypoxia, proposing that ERO1L is regulated through the HIF (hypoxia inducible transcrip-tion factor) pathway. At low levels ERO1L is ubiquitously expressed, however at high levels it is expressed in the upper digestive tract and esophagus. In addition, ERO1L is involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thus having a role in retrotranslocation of the toxin. Furthermore, ERO1L plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.
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Synonyms
ERO1-Like (S. Cerevisiae), Endoplasmic Oxidoreductin-1-Like Protein, Oxidoreductin-1-L-Alpha, ERO1-L-Alpha, ERO1LA, ERO1-L, ERO1 (S. Cerevisiae)-Like, ERO1-Like Protein Alpha, ERO1-Alpha, EC 1.8.4.-, EC 1.8.4, ERO1A, ERO1L.
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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 MGSEEQPPET AAQRCFCQVS GYLDDCTCDV ETIDRFNNYR LFPRLQKLLE SDYFRYYKVN LKRPCPFWND ISQCGRRDCA VKPCQSDEVP DGIKSASYKY SEEANNLIEE CEQAERLGAV DESLSEETQK AVLQWTKHDD SSDNFCEADD IQSPEAEYVD LLLNPERYTG YKGPDAWKIW NVIYEENCFK PQTIKRPLNP LASGQGTSEE NTFYSWLEGL CVEKRAFYRL ISGLHASINV HLSARYLLQE TWLEKKWGHN ITEFQQRFDG ILTEGEGPRR LKNLYFLYLI ELRALSKVLP FFERPDFQLF TGNKIQDEEN KMLLLEILHE IKSFPLHFDE NSFFAGDKKE AHKLKEDFRL HFRNISRIMD CVGCFKCRLW GKLQTQGLGT ALKILFSEKL IANMPESGPS YEFHLTRQEI VSLFNAFGRI STSVKELENF RNLLQNIH.
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 :
ETHE1 HumanDescription:
Ethylmalonic Encephalopathy 1 Human Recombinant
Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.
Product # :
PRO-1027Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ETHE1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (13-254) and having a molecular mass of 29.1kDa.ETHE1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ETHE1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ETHE1 is a mitochondrial sulfur dioxygenase involved in catabolism of sulfide that accumulates to toxic levels in ethylmalonic encephalopathy. Mutations of ETHE1 were detected in all the typical ethylmalonic encephalopathy patients analysed, but no ETHE1 mutations were identified in patients presenting with early onset progressive encephalopathy with ethylmalonic aciduria.
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Synonyms
Ethylmalonic encephalopathy protein 1, HSCO, Hepatoma subtracted clone one protein, YF13H12, protein ETHE1 mitochondrial, D83198, EC 3.1.2.6.
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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 MGSHMLSQRG GSGAPILLRQ MFEPVSCTFT YLLGDRESRE AVLIDPVLET APRDAQLIKE LGLRLLYAVN THCHADHITG SGLLRSLLPG CQSVISRLSG AQADLHIEDG DSIRFGRFAL ETRASPGHTP GCVTFVLNDH SMAFTGDALL IRGCGRTDFQ QGCAKTLYHS VHEKIFTLPG DCLIYPAHDY HGFTVSTVEE ERTLNPRLTL SCEEFVKIMG NLNLPKPQQI DFAVPANMRC GVQTPTA
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.