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1000 results found for “eph receptor”
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Name :
DPH3P1 HumanDescription:
Diphthamide Biosynthesis 3 Pseudogene 1 Human Recombinant
Diphthamide Biosynthesis 3 Pseudogene 1, C20orf143, DPH3B, ZCSL1, CSL-Type Zinc Finger-Containing Protein 1, Chromosome 20 Open Reading Frame 143, DPH3, KTI11 Homolog (S. Cerevisiae) Pseudogene, DPH3B, KTI11 Homolog B (S. Cerevisiae), Zinc Finger, CSL-Type Containing 1, DPH3 Homolog B (KTI11, S. Cerevisiae), Putative DPH3 Homolog B, Zinc Finger, CSL Domain Containing 1.
Product # :
PRO-1914Price :
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Description
DPH3P1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a) and having a molecular mass of 11.1kDa.DPH3P1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DPH3P1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Diphthamide Biosynthesis 3 Pseudogene 1 also known as DPH3P1 may stand for a processed pseudogene of DPH3 since it lacks the exon/intron structurefound in the functional gene. Yet, DPH3P1 does contain an intact open reading frame, though its translation has not been established.
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Synonyms
Diphthamide Biosynthesis 3 Pseudogene 1, C20orf143, DPH3B, ZCSL1, CSL-Type Zinc Finger-Containing Protein 1, Chromosome 20 Open Reading Frame 143, DPH3, KTI11 Homolog (S. Cerevisiae) Pseudogene, DPH3B, KTI11 Homolog B (S. Cerevisiae), Zinc Finger, CSL-Type Containing 1, DPH3 Homolog B (KTI11, S. Cerevisiae), Putative DPH3 Homolog B, Zinc Finger, CSL Domain Containing 1.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAVFHDE VEIEDFQYDE DSETYFCPCP CGDNFSITKE ELENGEGVAM CPGCSLIIKV IYDKDQFACG ETVPVPSVNK E
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NECAP2 HumanDescription:
NECAP Endocytosis Associated 2 Human Recombinant
NECAP endocytosis-associated protein 2, NECAP-2, FLJ10420, Adaptin ear-binding coat-associated protein 2.
Product # :
PRO-180Price :
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Shipped with Ice Packs
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Description
NECAP2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 283 amino acids (1-263a.a.) and having a molecular mass of 30.5 kDa. NECAP2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NECAP2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
NECAP2 which is involved in endocytosis, is a vital protein paralogues for clathrin-mediated membrane trafficking which are enhanced in CCV layers. NECAP2 protein colocalizes with AP-2 at the plasma membrane by binding AP-2s ?-ear domain, and interacts with AP-1, AP-2 and several GAE domain proteins termed GGA1, GGA2 and GGA3.
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Synonyms
NECAP endocytosis-associated protein 2, NECAP-2, FLJ10420, Adaptin ear-binding coat-associated protein 2.
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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 MEESGYESVL CVKPDVHVYR IPPRATNRGY RAAEWQLDQP SWSGRLRITA KGQMAYIKLE DRTSGELFAQ APVDQFPGTA VESVTDSSRY FVIRIEDGNG RRAFIGIGFG DRGDAFDFNV ALQDHFKWVK QQCEFAKQAQ NPDQGPKLDL GFKEGQTIKL NIANMKKKEG AAGNPRVRPA STGGLSLLPP PPGGKTSTLI PPPGEQLAVG GSLVQPAVAP SSGGAPVPWP QPNPATADIW GDFTKSTGST SSQTQPGTGW VQF
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 :
DYNLRB2 HumanDescription:
Dynein Light Chain Roadblock-Type 2 Human Recombinant
Dynein light chain roadblock-type 2, Dynein light chain 2B cytoplasmic, Roadblock domain-containing protein 2, DYNLRB2, DNCL2B, DNLC2B, ROBLD2, MGC62033.
Product # :
PRO-174Price :
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Shipped with Ice Packs
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Description
DYNLRB2 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 116 amino acids (1-96 a.a.) and having a molecular mass of 13kDa. The DYNLRB2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DYNLRB2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Dynein light chain roadblock-type 2 (DYNLRB2) functions as one of several non-catalytic accessory components of the cytoplasmic dynein complex which are considered to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein functions as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
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Synonyms
Dynein light chain roadblock-type 2, Dynein light chain 2B cytoplasmic, Roadblock domain-containing protein 2, DYNLRB2, DNCL2B, DNLC2B, ROBLD2, MGC62033.
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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 MAEVEETLKR IQSHKGVIGT MVVNAEGIPI RTTLDNSTTV QYAGLLHHLT MKAKSTVRDI DPQNDLTFLR IRSKKHEIMV APDKEYLLIV IQNPCE.
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 :
IHH HumanDescription:
Indian Hedgehog Human Recombinant
Indian hedgehog protein, IHH, HHG-2, BDA1.
Product # :
CYT-195Price :
Quantity :
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Shipped at Room temp
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Description
IHH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
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.Biological Activity
Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.More Info
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Introduction
IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.
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Synonyms
Indian hedgehog protein, IHH, HHG-2, BDA1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IHH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IHH 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 IHH 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
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.
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Background
What is the molecular weight/Mw of IHH HUMAN Protein?
IHH HUMAN Protein has a total Mw of 19.8kDa.
What is the source or expression system of IHH HUMAN Protein?
Escherichia Coli.
What is the Purity of IHH HUMAN Protein?
IHH HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of IHH HUMAN Protein?
Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.
What is the amino acid sequence of IHH HUMAN Protein?
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.
What applications can IHH HUMAN Protein be used in?
IHH HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IHH HUMAN Protein?
The endotoxin level is minimal, IHH HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
EMG1 HumanDescription:
EMG1 Nucleolar Protein Human Recombinant
EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.
Product # :
PRO-1122Price :
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Shipped with Ice Packs
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Description
EMG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 267 amino acids (1-244) and having a molecular mass of 29.1kDa.EMG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EMG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
EMG1 is a 244 aa protein which has a role in ribosome biogenesis. EMG1 is a key protein in the small ribosomal subunit assembly, controls methylation during ribosome synthesis and takes part in pre-18S rRNA processing. EMG1 is localized to the nucleolus and a mutation in this gene is linked with Bowen-Conradi syndrome.
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Synonyms
EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.
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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 MGSMAAPSDG FKPRERSGGE QAQDWDALPP KRPRLGAGNK IGGRRLIVVL EGASLETVKV GKTYELLNCD KHKSILLKNG RDPGEARPDI THQSLLMLMD SPLNRAGLLQ VYIHTQKNVL IEVNPQTRIP RTFDRFCGLM VQLLHKLSVR AADGPQKLLK VIKNPVSDHF PVGCMKVGTS FSIPVVSDVR ELVPSSDPIV FVVGAFAHGK VSVEYTEKMV SISNYPLSAA LTCAKLTTAF EEVWGVI
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 :
OMP HumanDescription:
Olfactory Marker Protein Human Recombinant
Olfactory neuronal-specific protein, Olfactory marker protein, OMP.
Product # :
PRO-1412Price :
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Shipped with Ice Packs
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Description
OMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-163 a.a) and having a molecular mass of 21.3kDa. OMP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
OMP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Olfactory marker protein (OMP) which is expressed in the cytoplasm of olfactory chemosensory neurons in the nasal neuroepithelium, is associated in a unique way with the mature olfactory receptor neurons in numerous vertebrate species. OMP have a modulatory part in the odor detection/signal transduction cascade ant its expression is a sign of mature vertebrate olfactory receptor neurons (ORNs). OMP is also a potent enhancer of mitosis in fetal olfactory epithelial cells and it promotes an increase in uptake of tritiated thymidine in liver.
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Synonyms
Olfactory neuronal-specific protein, Olfactory marker protein, OMP.
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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 MGSMAEDRPQ QPQLDMPLVL DQGLTRQMRL RVESLKQRGE KRQDGEKLLQ PAESVYRLNF TQQQRLQFER WNVVLDKPGK VTITGTSQNW TPDLTNLMTR QLLDPTAIFW RKEDSDAIDW NEADALEFGE RLSDLAKIRK VMYFLVTFGE GVEPANLKAS VVFNQL.
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 :
TAC1 HumanDescription:
Tachykinin-1 Human Recombinant
Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 1.
Product # :
PRO-1338Price :
Quantity :
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Shipped with Ice Packs
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Description
TAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (20-129 a.a) and having a molecular mass of 15.6kDa.TAC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TAC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 2M Urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Tachykinin-1 (TAC1) belongs to the tachykinin peptide hormone family. TAC1 are a family of peptides which have similar biologic activities and share a common C-terminal sequence, phe-X-gly-leu-met-NH2, however they have distinct N-terminal sequences that convey receptor specificities. TAC1 is assumed to act as neurotransmitters which interact with nerve receptors and smooth muscle cells. TAC1 induces behavioral responses and serves as vasodilators and secretagogues.
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Synonyms
Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 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 MGSHMEEIGA NDDLNYWSDW YDSDQIKEEL PEPFEHLLQR IARRPKPQQF FGLMGKRDAD SSIEKQVALL KALYGHGQIS HKRHKTDSFV GLMGKRALNS VAYERSAMQN YERRR.
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 :
PEX26 HumanDescription:
Peroxisomal Biogenesis Factor 26 Human Recombinant
PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.
Product # :
PRO-1544Price :
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Shipped with Ice Packs
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Description
PEX26 Human Recombinant produced in E. coli is a single polypeptide chain containing 269 amino acids (1-246) and having a molecular mass of 29.3kDa. PEX26 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PEX26 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Peroxisomal Biogenesis Factor 26 (PEX26) which is a part of the peroxin-26 gene family is probably required for protein import into peroxisomes. PEX26 attaches PEX1 and PEX6 to peroxisome membranes to form heteromeric AAA ATPase complexes needed for the import of proteins into peroxisomes. Deficiencies in this gene are the cause of peroxisome biogenesis disorder complementation group 8. PBD is a group of peroxisomal disorders evolving from a failure of protein import into the peroxisomal membrane or matrix.
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Synonyms
PBD7A, PBD7B, PEX26M1T, Pex26pM1T, Peroxisome assembly protein 26, PEX26.
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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 MGSMKSDSST SAAPLRGLGG PLRSSEPVRA VPARAPAVDL LEEAADLLVV HLDFRAALET CERAWQSLAN HAVAEEPAGT SLEVKCSLCV VGIQALAEMD RWQEVLSWVL QYYQVPEKLP PKVLELCILL YSKMQEPGAV LDVVGAWLQD PANQNLPEYG ALAEFHVQRV LLPLGCLSEA EELVVGSAAF GEERRLDVLQ AIHTARQQQK QEHSGSEEAQ KPNLEGSVSH KFLSLPMLVR QLWDSAVSH.
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 :
PHF11 HumanDescription:
PHF11 Protein Human Recombinant
PHD finger protein 11, BRCA1 C-terminus-associated protein, Renal carcinoma antigen NY-REN-34, PHF11, BCAP, APY, IGEL, IGER, IGHER, NYREN34, NY-REN-34, RP11-185C18.3.
Product # :
PRO-1268Price :
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Description
PHF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 351 amino acids (1-331 a.a.) and having a molecular mass of 39.7kDa.PHF11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PHF11 protein solution (1mg/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
PHD finger protein 11 (PHF11) is a regulator of TH1-type cytokine gene expression. The decline in PHF11 expression observed with an AD-associated genotype may promote the intense TH2 reactions which characterize numerous allergic individuals. PHF11 is linked with raised total serum IgE levels, asthma and acute atopic dermatitis (AD) in children. Even though PHF11 includes a plant homeodomain, a motif frequently found in transcriptional regulators, PHF11 function of has yet been examined.
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Synonyms
PHD finger protein 11, BRCA1 C-terminus-associated protein, Renal carcinoma antigen NY-REN-34, PHF11, BCAP, APY, IGEL, IGER, IGHER, NYREN34, NY-REN-34, RP11-185C18.3.
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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 MAQASPPRPE RVLGASSPEA RPAQEALLLP TGVFQVAEKM EKRTCALCPK DVEYNVLYFA QSENIAAHEN CLLYSSGLVE CEDQDPLNPD RSFDVESVKK EIQRGRKLKC KFCHKRGATV GCDLKNCNKN YHFFCAKKDD AVPQSDGVRG IYKLLCQQHA QFPIIAQSAK FSGVKRKRGR KKPLSGNHVQ PPETMKCNTF IRQVKEEHGR HTDATVKVPF LKKCKEAGLL NYLLEEILDK VHSIPEKLMD ETTSESDYEE IGSALFDCRL FEDTFVNFQA AIEKKIHASQ QRWQQLKEEI ELLQDLKQTL CSFQENRDLM SSSTSISSLS Y.
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 :
CCL28 HumanDescription:
Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28)
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-353Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL28 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids and having a molecular mass of 12.3 kDa. The CCL28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM PBS and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 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
SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.
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Background
What is the molecular weight/Mw of CCL28 HUMAN Protein?
CCL28 HUMAN Protein has a total Mw of 12.3kDa.
What is the source or expression system of CCL28 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL28 HUMAN Protein?
CCL28 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 HUMAN Protein?
Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL28 HUMAN Protein?
SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.
What applications can CCL28 HUMAN Protein be used in?
CCL28 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 HUMAN Protein?
The endotoxin level is minimal, CCL28 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FOPNL HumanDescription:
FGFR1OP N-terminal like Human Recombinant
FGFR1OP N-terminal like-like protein, FOP-related protein of 20 kDa, pluripotent embryonic stem cell-related protein, lisH domain-containing protein C16orf63, chromosome 16 open reading frame 63, FGFR1OP N-terminal, PHSECRG2, C16orf63, DKFZp686N1651, FLJ31153, FOR20.
Product # :
PRO-1195Price :
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Description
FOPNL Human Recombinant produced in E. coli is a single polypeptide chain containing 194 amino acids (1-174) and having a molecular mass of 21.9 kDa.FOPNL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The VAMP7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
FGFR1OP N-terminal like (FOPNL) is a member of the FGFR1OP family and contains 1 LisH domain. FOPNL is participates in the biogenesis of cilia. FOPNL is extensively expressed and detected in the brain, heart, kidney, liver, lung, skeletal muscle, placenta and the intestine.
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Synonyms
FGFR1OP N-terminal like-like protein, FOP-related protein of 20 kDa, pluripotent embryonic stem cell-related protein, lisH domain-containing protein C16orf63, chromosome 16 open reading frame 63, FGFR1OP N-terminal, PHSECRG2, C16orf63, DKFZp686N1651, FLJ31153, FOR20.
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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 MATVAELKAV LKDTLEKKGV LGHLKARIRA EVFNALDDDR EPRPSLSHEN LLINELIREY LEFNKYKYTA SVLIAESGQP VVPLDRQFLI HELNAFEESK DNTIPLLYGI LAHFLRGTKD GIQNAFLKGP SLQPSDPSLG RQPSRRKPMD DHLRKEEQKS TNIEDLHVSQ AVNR
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 :
LECT1 HumanDescription:
Leukocyte Cell Derived Chemotaxin 1 Human Recombinant
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
Product # :
PRO-1846Price :
Quantity :
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Description
LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 144 amino acids (214-334) and having a molecular mass of 16.3kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LECT1 solution (1mg/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
Leukocyte Cell Derived Chemotaxin 1, also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.
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Synonyms
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
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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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV.
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 :
PTRHD1 HumanDescription:
Peptidyl-TRNA Hydrolase Domain Containing 1 Human Recombinant
C2orf79, Putative peptidyl-tRNA hydrolase PTRHD1, Peptidyl-tRNA hydrolase domain-containing protein 1, PTRHD1.
Product # :
ENZ-826Price :
Quantity :
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Description
PTRHD1 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 18.2kDa.PTRHD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTRHD1 protein solution (1mg/ml) containing Phosphate buffer saline (pH 7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Putative peptidyl-tRNA hydrolase PTRHD1 (PTRHD1) is a 140 amino acid protein, which is encoded by a gene located on human chromosome 2p23.3. Chromosome 2 is the second largest human chromosome; it consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome. Several genetic diseases are linked to genes on chromosome 2.
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Synonyms
C2orf79, Putative peptidyl-tRNA hydrolase PTRHD1, Peptidyl-tRNA hydrolase domain-containing protein 1, PTRHD1.
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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 MGSMHRGVGP AFRVVRKMAA SGAEPQVLVQ YLVLRKDLSQ APFSWPAGAL VAQACHAATA ALHTHRDHPH TAAYLQELGR MRKVVLEAPD ETTLKELAET LQQKNIDHML WLEQPENIAT CIALRPYPKE EVGQYLKKFR LFK.
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 :
MBP (27-396) E.ColiDescription:
Maltose Binding Protein (27-396) E.coli Recombinant
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
Product # :
PRO-2321Price :
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Description
Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (27-396 a.a) and having a molecular mass of 40.8kDa. MBP protein was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MBP protein solution (1mg/ml) containing 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
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused. -
Synonyms
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
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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
MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFGG YAQSGLLAEI TPDKAFQDKL YPFTWDAVRY NGKLIAYPIA VEALSLIYNK DLLPNPPKTW EEIPALDKEL KAKGKSALMF NLQEPYFTWP LIAADGGYAF KYENGKYDIK DVGVDNAGAK AGLTFLVDLI KNKHMNADTD YSIAEAAFNK GETAMTINGP WAWSNIDTSK VNYGVTVLPT FKGQPSKPFV GVLSAGINAA SPNKELAKEF LENYLLTDEG LEAVNKDKPL GAVALKSYEE ELAKDPRIAA TMENAQKGEI MPNIPQMSAF WYAVRTAVIN AASGRQTVDE ALKDAQTRIT K.
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 :
EOGT MouseDescription:
EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase Mouse Recombinant
EGF domain-specific O-linked N-acetylglucosamine transferase, Extracellular O-linked N-acetylglucosamine transferase.
Product # :
ENZ-946Price :
Quantity :
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Description
EOGT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 516 amino acids (20-527 a.a.) and having a molecular mass of 60.4kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). EOGT is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EOGT protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase (EOGT) takes part in the regulation of Notch receptor. EOGT catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine/ threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). EOGT mainly glycosylates the Thr residue positioned between the fifth and sixth conserved cysteines of folded EGF-like domains.
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Synonyms
EGF domain-specific O-linked N-acetylglucosamine transferase, Extracellular O-linked N-acetylglucosamine transferase.
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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
DKAHSEADDA PGKALYDYSS LRLPAEHIPF FLHNNRHVAS VCREDSHCPY KKHLENLNYC WGYEKSCAPE FRFGSPVCSY VDLGWTDTLE SAQDMFWRQA DFGYARERLG EIRTICQPER ASDSSLVCSR YLQYCRATGL YLDLRNIKRN HDRFKEDFLQ GGEIGGYCKL DSHALVSEGQ RKSPLQSWFA ELQGYTQLNF RPIEDAKCDI VVEKPTYFMK LDAGINMYHH FCDFLNLYLT QHVNNSFSTD VYIVMWDTST YGYGDLFSDT WKAFTDYDVI HLKTYDSKKV CFKEAVFSLL PRMRYGLFYN TPLISGCQNT GLFRAFSQHV LHRLNITQEG PKDGKVRVTI LARSTEYRKI LNQDELVNAL KTVSTFEVRV VDYKYRELGF LDQLRITHNT DIFIGMHGAG LTHLLFLPDW AAVFELYNCE DERCYLDLAR LRGIHYITWR KPSKVFPQDK GHHPTLGEHP KFTNYSFDVE EFMYLVLQAA EHVLQHPQWP FKKKHDELLE HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PIM2 HumanDescription:
PIM2 Human Recombinant
Pim-2 oncogene, Serine/threonine-protein kinase pim-2, Pim-2h, PIM2.
Product # :
PRO-1977Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PIM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-311 a.a) and having a molecular mass of 36.6kDa. PIM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PIM2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
PIM2 is a serine/threonine protein kinase which is a part of the CAMK family. PIM2 is expressed in various tissues mainly in spleen, thymus, testis and small intestine. PIM2 is implicated in tumor phenotypes and participates in the formation and preservation of Long-Term Potentiation (LTP). PIM2 is also involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate.
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Synonyms
Pim-2 oncogene, Serine/threonine-protein kinase pim-2, Pim-2h, PIM2.
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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 MGSMLTKPLQ GPPAPPGTPT PPPGGKDREA FEAEYRLGPL LGKGGFGTVF AGHRLTDRLQ VAIKVIPRNR VLGWSPLSDS VTCPLEVALL WKVGAGGGHP GVIRLLDWFE TQEGFMLVLE RPLPAQDLFD YITEKGPLGE GPSRCFFGQV VAAIQHCHSR GVVHRDIKDE NILIDLRRGC AKLIDFGSGA LLHDEPYTDF DGTRVYSPPE WISRHQYHAL PATVWSLGIL LYDMVCGDIP FERDQEILEA ELHFPAHVSP DCCALIRRCL APKPSSRPSL EEILLDPWMQ TPAEDVPLNP SKGGPAPLAW SLLP.
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 :
VEGF Human (121 a.a.), HisDescription:
Vascular Endothelial Growth Factor-121 Human Recombinant, His Tag
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-619Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a double, non-glycosylated, polypeptide chain (aa 207-327) containing a total of 142 amino acids and having a molecular mass of 16.3 kDa. The VEGF-121 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VEGF-121 His Tag in 20mM Tris pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is <4.2 ng/ml. Measured in a cell proliferation assay using NIH-3T3 cell, corresponding to a specific activity of less than 238,095.23units/mg.More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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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 MAPMAEGGGQ NHHEVVKFMD VYQRSYCHPI ETLVDIFQEY PDEIEYIFKP SCVPLMRCGG CCNDEGLECV PTEESNITMQ IMRIKPHQGQ HIGEMSFLQH NKCECRPKKD RARQEKCDKP RR.
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 :
TH MouseDescription:
Tyrosine Hydroxylase Mouse Recombinant
Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.
Product # :
ENZ-988Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TH Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 507 amino acids (1-498a.a.) and having a molecular mass of 57.0kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). TH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TH protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Tyrosine 3-monooxygenase (Th), is a rate-limiting enzyme in catecholamine synthesis. Th utilizes tetrahydrobiopterin as well as molecular oxygen to convert tyrosine to DOPA. Th regulates dopamine (DA) neurotransmission at the biosynthesis and reuptake steps. Th takes a vital part in the physiology of adrenergic neurons. Furthermore, Th effects overexpression in lymphocytes on the differentiation as well as function of T helper cells.
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Synonyms
Tyrosine 3-monooxygenase, Tyrosine 3-hydroxylase, TH.
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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
ADPMPTPSAS SPQPKGFRRA VSEQDTKQAE AVTSPRFIGR RQSLIEDARK EREAAAAAAA AAVASAEPGN PLEAVVFEER DGNAVLNLLF SLRGTKPSSL SRALKVFETF EAKIHHLETR PAQRPLAGSP HLEYFVRFEV PSGDLAALLS SVRRVSDDVR SAREDKVPWF PRKVSELDKC HHLVTKFDPD LDLDHPGFSD QAYRQRRKLI AEIAFQYKQG EPIPHVEYTK EEIATWKEVY ATLKGLYATH ACREHLEAFQ LLERYCGYRE DSIPQLEDVS HFLKERTGFQ LRPVAGLLSA RDFLASLAFR VFQCTQYIRH ASSPMHSPEP DCCHELLGHV PMLADRTFAQ FSQDIGLASL GASDEEIEKL STVYWFTVEF GLCKQNGELK AYGAGLLSSY GELLHSLSEE PEVRAFDPDT AAVQPYQDQT YQPVYFVSES FSDAKDKLRN YASRIQRPFS VKFDPYTLAI DVLDSPHTIR RSLEGVQDEL HTLTQALSAI SHHHHHH.
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 :
LCAT Human, HEKDescription:
Lecithin-Cholesterol Acyltransferase Human Recombinant, HEK
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
Product # :
ENZ-254Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
LCAT Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 429 amino acids (25-440) which includes a 13 amino acid Flag Tag fused at N-terminus and having a total molecular mass of 48.5 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.
Source
Human Embryonic Kidney 293 cells
Formulation
The LCAT protein was lyophilized from 0.4um filtered solution at a concentration of 0.5mg/ml containing 20mM Tris buffer, and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.
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Synonyms
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LCAT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCAT 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
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. LCAT HEK is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
HVDYKDDDDK PAGFWLLNVL FPPHTTPKAE LSNHTRPVIL VPGCLGNQLE AKLDKPDVVN WMCYRKTEDF FTIWLDLNMF LPLGVDCWID NTRVVYNRSS GLVSNAPGVQ IRVPGFGKTY SVEYLDSSKL AGYLHTLVQN LVNNGYVRDE TVRAAPYDWR LEPGQQEEYY RKLAGLVEEM HAAYGKPVFL IGHSLGCLHL LYFLLRQPQA WKDRFIDGFI SLGAPWGGSI KPMLVLASGD NQGIPIMSSI KLKEEQRITT TSPWMFPSRM AWPEDHVFIS TPSFNYTGRD FQRFFADLHF EEGWYMWLQS RDLLAGLPAP GVEVYCLYGV GLPTPRTYIY DHGFPYTDPV GVLYEDGDDT VATRSTELCG LWQGRQPQPV HLLPLHGIQH LNMVFSNLTL EHINAILLGA YRQGPPASPT ASPEPPPPE
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 :
LGALS8 MouseDescription:
Galectin-8 Mouse Recombinant
Galectin-8, Gal-8, LGALS-8, AI326142, D13Ertd524e, 1200015E08Rik.
Product # :
CYT-185Price :
Quantity :
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Shipped with Ice Packs
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- SDS-PAGE
Description
LGALS8 mouse Recombinant produced E. coli is a single polypeptide chain containing 339 amino acids (1-316) and having a molecular mass of 38kDa.LGALS8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LGALS8 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is ≤ 2ug/ml. Measured by its ability to agglutinate human red blood cells.
SDS-PAGE
More Info
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Introduction
LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.
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Synonyms
Galectin-8, Gal-8, LGALS-8, AI326142, D13Ertd524e, 1200015E08Rik.
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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 MGSMLSLNNL QNIIYNPIIP YVGTITEQLK PGSLIVIRGH VPKDSERFQV DFQLGNSLKP RADVAFHFNP RFKRSSCIVC NTLTQEKWGW EEITYDMPFR KEKSFEIVFM VLKNKFQVAV NGRHVLLYAH RISPEQIDTV GIYGKVNIHS IGFRFSSDLQ
SMETSALGLT QINRENIQKP GKLQLSLPFE ARLNASMGPG RTVVIKGEVN TNARSFNVDL VAGKTRDIAL HLNPRLNVKA FVRNSFLQDA WGEEERNITC FPFSSGMYFE MIIYCDVREF KVAINGVHSL EYKHRFKDLS SIDTLSVDGD IRLLDVRSW. -
Background
What is the molecular weight/Mw of LGALS8 MOUSE Protein?
LGALS8 MOUSE Protein has a total Mw of 38kDa.
What is the source or expression system of LGALS8 MOUSE Protein?
Escherichia Coli.
What is the Purity of LGALS8 MOUSE Protein?
LGALS8 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS8 MOUSE Protein?
The biological functionality of LGALS8 MOUSE Protein will be determined in the future.
What is the amino acid sequence of LGALS8 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMLSLNNL QNIIYNPIIP YVGTITEQLK PGSLIVIRGH VPKDSERFQV DFQLGNSLKP RADVAFHFNP RFKRSSCIVC NTLTQEKWGW EEITYDMPFR KEKSFEIVFM VLKNKFQVAV NGRHVLLYAH RISPEQIDTV GIYGKVNIHS IGFRFSSDLQ
SMETSALGLT QINRENIQKP GKLQLSLPFE ARLNASMGPG RTVVIKGEVN TNARSFNVDL VAGKTRDIAL HLNPRLNVKA FVRNSFLQDA WGEEERNITC FPFSSGMYFE MIIYCDVREF KVAINGVHSL EYKHRFKDLS SIDTLSVDGD IRLLDVRSW.
What applications can LGALS8 MOUSE Protein be used in?
LGALS8 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS8 MOUSE Protein?
The endotoxin level is minimal, LGALS8 MOUSE Protein was purified using conventional chromatography techniques.
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Assay Conditions
1. Mix equal volumes of human blood and Alsever’s solution (pH 7.0). (Alsever’s solution: NaCl 0.42g, Sodium citric acid 0.8g, Citric acid 0.055g, D-glucose 2.05g in DW100 ml).2. Centrifuge at 15000rpm for 10 minutes and wash 4 times with PBS.3. Dilute packed cells in a 0.5mg/ml trypsin-EDTA solution to give 4% red cell suspension.4. Incubate for 1 hour at 37°C and wash 4 times with PBS.5. Dilute packed cells in PBS to give a 4% red cell suspension.6. Load 50µl of 0.5%BSA-in-0.15M-NaCl solution and 25µl of 4%-Red-Cell-in-PBS in U shaped wells.7. Add 25µl of serial diluted galectin protein in PBS to each well plate (Round bottom 96 well plate).8. Incubate for 30 minutes at room temperature to observe visible agglutination.
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 :
LIF RatDescription:
Leukemia Inhibitory Factor Rat Recombinant
Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.
Product # :
CYT-731Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leukemia Inhibitory Factor (LIF) Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.8 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LIF Rat was lyophilized from 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity of rat LIF is determined by the ability to induce differentiation of M1 myeloid leukemic cells. The minimum detectable concentration of rat LIF in this assay is 0.5ng/mL.More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPLPITPVNA TCAIRHPCHG NLMNQIKSQL AQLNGSANAL FISYYTAQGE PFPNNVDKLC APNMTDFPPF HANGTEKTKL VELYRMVTYL GASLTNITWD QKNLNPTAVS LQIKLNATTD VMRGLLSSVL CRLCNKYHVG HVDVPCVPDN SSKEAFQRKK LGCQLLGTYK QVISVLAQAF .
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 :
GPHB5 HumanDescription:
Thyrostimulin Beta Human Recombinant
Glycoprotein hormone beta-5, ZLUT1, GPHB5, GPB5.
Product # :
HOR-257Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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Description
GPHB5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a total molecular mass of 13.34 kDa. The Thyrostimulin contains His tag which consists of 14 additional amino acids.The amino acid sequence of the recombinant human Thyrostimulin beta subunit is 100% homologous to the amino acid sequence of the human Thyrostimulin beta subunit without signal sequence. (N-terminal 24AA).Thyrostimulin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GPHB5 filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH 4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Human thyrostimulin ranks among the glycoprotein hormone family. These hormones consist of two subunits, the common alpha- and specific beta-subunits, which associate noncovalently to form a heterodimer. The alpha-subunit combines with four distinct beta-subunits giving rise to four biologically active hormones in human: FSH, LH, TSH, and CG. FSH, LH, and TSH, mainly expressed in the anterior pituitary, are essential for coordinated endocrine regulation in the hypothalamus- pituitary axis and show to activate specific G protein–coupled receptors in the thyroid (TSH receptor) and gonads (LH and FSH receptors), respectively.
The heterodimeric glycoprotein hormones have only been identified in vertebrates and are highly conserved in organisms from primitive rayfin fish (Chondrostei) to human in both primary sequences and functional characteristics.
Corticotroph-derived glycoprotein hormone (CGH), also referred to as thyrostimulin, is a noncovalent heterodimer of glycoprotein hormone alpha 2 (GPHA2) and glycoprotein hormone beta 5 (GPHB5).
Recombinant A2/B5 heterodimeric glycoproteins activates human TSH receptors, but not LH and FSH receptors, and shows high affinity to TSH receptors in a radioligand receptor assay. The heterodimer also stimulates cAMP production and thymidine incorporation by cultured thyroid cells and increases serum thyroxine levels in TSH-suppressed rats in vivo. This new heterodimeric glycoprotein hormone was named as thyrostimulin based on its thyroid-stimulating activity. The expression of thyrostimulin in the anterior pituitary known to express TSH receptors suggested a paracrine mechanism. -
Synonyms
Glycoprotein hormone beta-5, ZLUT1, GPHB5, GPB5.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thyrostimulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GPHB5 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 add 0.1M Acetate buffer pH4 to prepare a working stock solution of ~ 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this protein is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MRGSHHHHHH GMASASSGNL RTFVGCAVRE FTFLAKKPGC RGLRITTDAC WGRCETWEKP ILEPPYIEAH HRVCTYNETK QVTVKLPNCA PGVDPFYTYP VAIRCDCGAC STATTECETI.
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 :
Resistin RatDescription:
Resistin Rat Recombinant
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-1129Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- formulation
- purity
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Description
Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression. -
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin 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 Resistin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.
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 :
HLA-DOB HumanDescription:
Major Histocompatibility Complex Class II DO Beta Human Recombinant
HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.
Product # :
PRO-1967Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
HLA-DOB Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (27-224) and having a molecular mass of 25.2 kDa.HLA-DOB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The HLA-DOB solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Major Histocompatibility Complex Class II DO Beta (HLA-DOB) is a part of the HLA class II beta chain paralogues. This class II beta chain is a heterodimer which is located in intracellular vesicles and consists of an alpha (DOA) and a beta chain (DOB), both anchored in the membrane. HLA-DOB which interacts with the HLA-DM molecule in B-cells is a significant modulator in the HLA class II restricted antigen presentation pathway. Class II molecules are expressed in antigen presenting cells such as B lymphocytes, dendritic cells and macrophages.
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Synonyms
HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.
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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 MGSGTDSPED FVIQAKADCY FTNGTEKVQF VVRFIFNLEE YVRFDSDVGM FVALTKLGQP DAEQWNSRLD LLERSRQAVD GVCRHNYRLG APFTVGRKVQ PEVTVYPERT PLLHQHNLLH CSVTGFYPGD IKIKWFLNGQ EERAGVMSTG PIRNGDWTFQ TVVMLEMTPE LGHVYTCLVD HSSLLSPVSV EWRAQSEYSW RK.
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.