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1000 results found for “endoplasmic reticulum protein”
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Name :
CXCL17 RatDescription:
VEGF Co-regulated Chemokine 1 Rat Recombinant
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
Product # :
CHM-281Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CXCL17 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.More Info
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Introduction
Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.
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Synonyms
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 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
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
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Background
What is the molecular weight/Mw of CXCL17 RAT Protein?
CXCL17 RAT Protein has a total Mw of 11.5kDa.
What is the source or expression system of CXCL17 RAT Protein?
Escherichia Coli.
What is the Purity of CXCL17 RAT Protein?
CXCL17 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL17 RAT Protein?
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.
What is the amino acid sequence of CXCL17 RAT Protein?
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
What applications can CXCL17 RAT Protein be used in?
CXCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL17 RAT Protein?
The endotoxin level is minimal, CXCL17 RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LILRA3 HumanDescription:
Leukocyte Immunoglobulin Like Receptor A3 Human Recombinant
LILRA3, ILT6, LIR4, LIR-4, LILRA3, CD85e, Leukocyte immunoglobulin-like receptor subfamily A member 3, leukocyte immunoglobulin-like receptor subfamily A member 3 isoform 1, CD85 antigen-like family member E, Immunoglobulin-like transcript 6, Leukocyte immunoglobulin-like receptor 4, Monocyte inhibitory receptor HM43/HM31.
Product # :
PRO-2831Price :
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Description
LILRA3 Human Recombinant is a single, glycosylated, polypeptide chain (24-439 a.a) containing a total of 658 amino acids and having a molecular mass of 72.2 kDa. LILRA3 is fused to a 239 a.a hIgG-his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The LILRA3 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
LILRA3, ILT6, LIR4, LIR-4, LILRA3, CD85e, Leukocyte immunoglobulin-like receptor subfamily A member 3, leukocyte immunoglobulin-like receptor subfamily A member 3 isoform 1, CD85 antigen-like family member E, Immunoglobulin-like transcript 6, Leukocyte immunoglobulin-like receptor 4, Monocyte inhibitory receptor HM43/HM31.
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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
DGSGPLPKPT LWAEPGSVIT QGSPVTLRCQ GSLETQEYHL YREKKTALWI TRIPQELVKK GQFPILSITW EHAGRYCCIY GSHTAGLSES SDPLELVVTG AYSKPTLSAL PSPVVTSGGN VTIQCDSQVA FDGFILCKEG EDEHPQCLNS HSHARGSSRA IFSVGPVSPS RRWSYRCYGY DSRAPYVWSL PSDLLGLLVP GVSKKPSLSV QPGPVVAPGE KLTFQCGSDA GYDRFVLYKE WGRDFLQRPG RQPQAGLSQA NFTLGPVSRS YGGQYTCSGA YNLSSEWSAP SDPLDILITG QIRARPFLSV RPGPTVASGE NVTLLCQSQG GMHTFLLTKE GAADSPLRLK SKRQSHKYQA EFPMSPVTSA HAGTYRCYGS LSSNPYLLTH PSDPLELVVS GAAETLSPPQ NKSDSKAGEL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH.
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Background
Leukocyte Immunoglobulin Like Receptor A3 (LILRA3) acts as a soluble receptor for class I MHC antigens. LILRA3 binds classical and non-classical HLA class I molecules and exhibits high affinity for monocyte surfaces, effectively suppressing LPS-induced TNF-alpha production. Unlike many of its family, LILRA3 has no transmembrane domain.
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 :
MINA HumanDescription:
MYC Induced Nuclear Antigen Human Recombinant
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
Product # :
PRO-2078Price :
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Shipped with Ice Packs
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Description
MINA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.9kDa. MINA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MINA protein solution (0.25mg/ml) containing 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
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Introduction
MYC Induced Nuclear Antigen, also known as MINA is an oxygenase which can function both as a histone lysine demethylase and a ribosomal histidine hydroxylase. MINA is involved in the demethylation of trimethylated Lys-9 on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. MINA also catalyzes the hydroxylation of 60S ribosomal protein L27a on His-39. In addition, MINA plays a significant role in cell growth and survival. MINA is implicated in ribosome biogenesis, probably in the duration of the assembly process of pre-ribosomal particles.
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Synonyms
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
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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 MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV.
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 :
RPS5 HumanDescription:
Ribosomal Protein S5 Human Recombinant
40S ribosomal protein S5, S5, RPS5.
Product # :
PRO-1300Price :
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Description
RPS5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-204 a.a.) and having a molecular mass of 25.3kDa.RPS5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RPS5 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
40S ribosomal protein S5 (RPS5) is a ribosomal protein, which is a member of the ribosomal protein S7P family.Ribosomes, which are the organelles that catalyze protein synthesis, composed of a small subunit and a large subunit that comprise of over 80 distinct ribosomal proteins. RPS5 is a 204 amino acid component of the 40S complex. RPS5 proteins exist as multiple processed pseudogenes which are scattered throughout the genome. RPS5 is expressed at varying amounts in colorectal cancer cells, proposing a possible role in carconigenesis.
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Synonyms
40S ribosomal protein S5, S5, RPS5.
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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 MGSMTEWETA APAVAETPDI KLFGKWSTDD VQINDISLQD YIAVKEKYAK YLPHSAGRYA AKRFRKAQCP IVERLTNSMM MHGRNNGKKL MTVRIVKHAF EIIHLLTGEN PLQVLVNAII NSGPREDSTR IGRAGTVRRQ AVDVSPLRRV NQAIWLLCTG AREAAFRNIK TIAECLADEL INAAKGSSNS YAIKKKDELE RVAKSNR.
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 :
OmpADescription:
Outer Membrane Protein-A Bacterial Recombinant
Outer Membrane Protein-A, OmpA.
Product # :
PRO-571Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 50.5 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing polyclonal and monoclonal antibodies in ELISA and Western Blot techniques. All forms of A-protein were found to activate the secretion of tumour necrosis factor alpha from murine macrophage. For ref see Maurice et al. (1999) Protein Expression and Purification 16, 396-404.The OmpA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel filtration.
(b) Analysis by SDS-PAGE.Biological Activity
The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.More Info
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Introduction
The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.
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Synonyms
Outer Membrane Protein-A, OmpA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bacterial Outer Membrane Protein-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted OmpA should be stored at 4 below -18°C. 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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Solubility
It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa itnvttnqti qrdkvnltlt gdvsafkkda ngnlvnkaga sigwkaaadg qsatavlgag nmaggvqnal aafgtlyvaa dntvpvpavn fnvkaeiqgd sqatynyfkd eladlfiltr dgmkfdtitt gttsanlihi rdvsnilpte ggkifvtite yadhaangrg egtvlvtrka lsvtlpsgga vtlkpadvaa dvgasitagr qarlvfevet nqgevavkks naegvdiqng trgtaplvdf tl.
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 :
MAP1LC3A HumanDescription:
Microtubule-Associated Protein 1 Light Chain 3 Alpha Human Recombinant
ATG8E, LC3, LC3A, MAP1ALC3, MAP1BLC3, MLP3A.
Product # :
PRO-495Price :
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Shipped with Ice Packs
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Description
MAP1LC3A Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-120 a.a.) and having a molecular mass of 15.1 kDa. The MAP1LC3A is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAP1LC3A solution (1mg/ml) contains 20mM Tris-HCl pH-8.0, 1mM DTT, 0.1M NaCl & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MAP1LC3A takes part in formation of autophagosomal vacuoles and is one of the light chain subunits that functions together with both MAP1A and/or MAP1B. MAP1LC3A has an important part in neuronal development and in maintaining the balance between neuronal plasticity and rigidity. MAP1LC3A is expressed as two alternatively spliced isoforms that are expressed in testis, brain, heart, liver and skeletal muscle, but are absent in thymus and peripheral blood leukocytes.
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Synonyms
ATG8E, LC3, LC3A, MAP1ALC3, MAP1BLC3, MLP3A.
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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
MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE QEKDEDGFLY MVYASQETFG 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.
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Name :
ARHGEF39 HumanDescription:
Rho Guanine Nucleotide Exchange Factor 39 Human Recombinant
Rho guanine nucleotide exchange factor 39, ARHGEF39, C9orf100, RP11-331F9.7.
Product # :
PRO-2101Price :
Quantity :
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Shipped with Ice Packs
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Description
ARHGEF39 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-335 a.a) and having a molecular mass of 40.7kDa.ARHGEF39 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARHGEF39 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Rho Guanine Nucleotide Exchange Factor 39, also known as ARHGEF39, is a protein coding gene which owns one DH (DBL-homology) domain and one PH domain. ARHGEF39 encourages cell proliferation.
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Synonyms
Rho guanine nucleotide exchange factor 39, ARHGEF39, C9orf100, RP11-331F9.7.
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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 MGSMELSCPG SRCPVQEQRA RWERKRACTA RELLETERRY QEQLGLVATY FLGILKAKGT LRPPERQALF GSWELIYGAS QELLPYLEGG CWGQGLEGFC RHLELYNQFA ANSERSQTTL QEQLKKNKGF RRFVRLQEGR PEFGGLQLQD LLPLPLQRLQ QYENLVVALA ENTGPNSPDH QQLTRAARLI SETAQRVHTI GQKQKNDQHL RRVQALLSGR QAKGLTSGRW FLRQGWLLVV PPHGEPRPRM FFLFTDVLLM AKPRPPLHLL RSGTFACKAL YPMAQCHLSR VFGHSGGPCG GLLSLSFPHE KLLLMSTDQE ELSRWYHSLT WAISSQKN.
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 :
RPL5 HumanDescription:
Ribosomal Protein L5 Human Recombinant
60S ribosomal protein L5, RPL5, MSTP030, Ribosomal protein L5, DBA6, L5, MSTP030.
Product # :
PRO-2058Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RPL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-297 a.a.) and having a molecular mass of 36.8kDa.RPL5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RPL5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Ribosomal Protein L5, also known as RPL5 is a part of the ribosomal protein L18P family. RPL5 which binds 5S RNA is necessary for rRNA maturation and structure of the 60S ribosomal subunits.
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Synonyms
60S ribosomal protein L5, RPL5, MSTP030, Ribosomal protein L5, DBA6, L5, MSTP030.
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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 MGSMGFVKVV KNKAYFKRYQ VKFRRRREGK TDYYARKRLV IQDKNKYNTP KYRMIVRVTN RDIICQIAYA RIEGDMIVCA AYAHELPKYG VKVGLTNYAA AYCTGLLLAR RLLNRFGMDK IYEGQVEVTG DEYNVESIDG QPGAFTCYLD AGLARTTTGN KVFGALKGAV DGGLSIPHST KRFPGYDSES KEFNAEVHRK HIMGQNVADY MRYLMEEDED AYKKQFSQYI KNSVTPDMME EMYKKAHAAI RENPVYEKKP KKEVKKKRWN RPKMSLAQKK DRVAQKKASF LRAQERAAES.
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 :
PLSCR1 HumanDescription:
Phospholipid Scramblase 1 Protein Human Recombinant
MMTRA1B, Phospholipid scramblase 1, PL scramblase 1, Ca(2+)-dependent phospholipid scramblase 1, Erythrocyte phospholipid scramblase,MmTRA1b.
Product # :
PRO-1271Price :
Quantity :
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Shipped with Ice Packs
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Description
PLSCR1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-288 a.a.) and having a molecular mass of 33.8kDa.PLSCR1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PLSCR1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl,30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Phospholipid scramblase (PLSCR1) is a member of the phospholipid scramblase family. PLSCR1 has a significant part in the antiviral reaction of IFN by intensifying and improving the IFN reaction via increasing expression of select subset of potent antiviral genes. PLSCR1 promotes cytokine-regulated cell proliferation and differentiation.
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Synonyms
MMTRA1B, Phospholipid scramblase 1, PL scramblase 1, Ca(2+)-dependent phospholipid scramblase 1, Erythrocyte phospholipid scramblase,MmTRA1b.
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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 MDKQNSQMNA SHPETNLPVG YPPQYPPTAF QGPPGYSGYP GPQVSYPPPP AGHSGPGPAG FPVPNQPVYN QPVYNQPVGA AGVPWMPAPQ PPLNCPPGLE YLSQIDQILI HQQIELLEVL TGFETNNKYE IKNSFGQRVY FAAEDTDCCT RNCCGPSRPF TLRIIDNMGQ EVITLERPLR CSSCCCPCCL QEIEIQAPPG VPIGYVIQTW HPCLPKFTIQ NEKREDVLKI SGPCVVCSCC GDVDFEIKSL DEQCVVGKIS KHWTGILREA FTDADNFGIQ FPLDLDVK
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 :
ARPC2 HumanDescription:
Actin Related Protein 2/3 Complex, Subunit 2 Human Recombinant
ARC34, p34-Arc, PNAS-139, PRO2446, Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subuni, ARPC2.
Product # :
PRO-1418Price :
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Description
ARPC2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-300a.a) and having a molecular mass of 36.7kDa. ARPC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
ARPC2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Actin-related protein 2/3 complex subunit 2 (ARPC2), is a part of the Rho family of small GTPases and one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. Nevertheless, the exact role of the protein (the p34 subunit) has yet to be determined.
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Synonyms
ARC34, p34-Arc, PNAS-139, PRO2446, Actin-related protein 2/3 complex subunit 2, Arp2/3 complex 34 kDa subuni, ARPC2.
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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 MGSMILLEVN NRIIEETLAL KFENAAAGNK PEAVEVTFAD FDGVLYHISN PNGDKTKVMV SISLKFYKEL QAHGADELLK RVYGSFLVNP ESGYNVSLLY DLENLPASKD SIVHQAGMLK RNCFASVFEK YFQFQEEGKE GENRAVIHYR DDETMYVESK KDRVTVVFST VFKDDDDVVI GKVFMQEFKE GRRASHTAPQ VLFSHREPPL ELKDTDAAVG DNIGYITFVL FPRHTNASAR DNTINLIHTF RDYLHYHIKC SKAYIHTRMR AKTSDFLKVL NRARPDAEKK EMKTITGKTF SSR.
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 :
HERC5 HumanDescription:
HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 Human Recombinant
HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.
Product # :
ENZ-797Price :
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Description
HERC5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (681-1024 a.a.) and having a molecular mass of 43kDa. HERC5 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
HERC5 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 (HERC5) is a member of the HERC family of ubiquitin ligases, found in a cluster of HERC family genes on chromosome 4. HERC5 is a protein with a HECT domain and 5 RCC1 repeats. The HERC5 protein localizes to the cytoplasm and perinuclear region and serves as an INF-induced E3 protein ligase that mediates ISGylation of protein targets. HERC5 exhibits antiviral activity towards HIV-1, influenza A virus and human papillomavirus. HERC5 is a major E3 ligase for ISG15 conjugation. HERC5 also serves as a positive regulator of innate antiviral response in cells induced by INF. Pro-inflammatory cytokines upregulate HERC5 in endothelial cells. HERC5 is physically connected with polyribosomes, broadly modifies recently synthesized proteins in a cotranslational fashion.
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Synonyms
HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.
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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 MGSFDLTVRR NHLIEDVLNQ LSQFENEDLR KELWVSFSGE IGYDLGGVKK EFFYCLFAEM IQPEYGMFMY PEGASCMWFP VKPKFEKKRY FFFGVLCGLS LFNCNVANLP FPLALFKKLL DQMPSLEDLK ELSPDLGKNL QTLLDDEGDN FEEVFYIHFN VHWDRNDTNL IPNGSSITVN QTNKRDYVSK YINYIFNDSV KAVYEEFRRG FYKMCDEDII KLFHPEELKD VIVGNTDYDW KTFEKNARYE PGYNSSHPTI VMFWKAFHKL TLEEKKKFLV FLTGTDRLQM KDLNNMKITF CCPESWNERD PIRALTCFSV LFLPKYSTME TVEEALQEAI NNNRGFG.
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 :
GRPEL1 HumanDescription:
GrpE-Like 1 Human Recombinant
HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.
Product # :
PRO-263Price :
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Description
GRPEL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (28-217a.a.) and having a molecular mass of 23.6kDa.GRPEL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GRPEL1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GRPEL1 is a vital component of the PAM complex, a complex necessary for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. GRPEL1 protein controls the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.
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Synonyms
HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.
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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 MCTATKQKNS GQNLEEDMGQ SEQKADPPAT EKTLLEEKVK LEEQLKETVE KYKRALADTE NLRQRSQKLV EEAKLYGIQA FCKDLLEVAD VLEKATQCVP KEEIKDDNPH LKNLYEGLVM TEVQIQKVFT KHGLLKLNPV GAKFDPYEHE ALFHTPVEGK EPGTVALVSK VGYKLHGRTL RPALVGVVKE A
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
G CSF Human, PEGDescription:
Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-018Price :
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Description
Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.
Purity
Greater than 95.0% as determined by SEC-HPLC.
Biological Activity
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.
More Info
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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
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Physical Appearance
Colorless, clear and transparent solution.
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Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
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Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.
What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.
What is the Purity of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.
What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.
What applications can G CSF HUMAN, PEG Protein be used in?
G CSF HUMAN, PEG Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
BMPR1A HumanDescription:
Bone Morphogenetic Protein Receptor Type IA Human Recombinant
BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.
Product # :
CYT-380Price :
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Shipped at Room temp
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Description
BMPR1A Human Recombinant extracellular domain produced in baculovirus is a monomeric, glycosylated, Polypeptide chain fused with 6xHis tag at C-terminus and having a molecular mass of 23 kDa. The BMR1A is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
CD292 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1X PBS.
Purity
Greater than 90.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to inhibit recombinant human BMP-2 induced alkaline phosphatase production by C2C12 myogenic cells. The ED50 for this effect is typically 1-3 µg/ml in the presence of 500 ng/ml of recombinant human BMP-2 corresponding to a Specific Activity of 2,000 units/mg.More Info
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Introduction
The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.
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Synonyms
BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bone Morphogenetic Protein Receptor 1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMPR1A 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 ALK-3 in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Bone Morphogenetic Protein Receptor Type IA Human Recombinant: Exploring the Potential of a Key Regulator in Bone Development
Abstract:
Bone Morphogenetic Protein Receptor Type IA (BMPR1A) human recombinant is a crucial regulator in bone development and homeostasis. This research paper provides a comprehensive analysis of BMPR1A, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMPR1A human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
Bone development and maintenance rely on intricate signaling pathways, with BMPR1A playing a pivotal role in bone morphogenesis. This paper explores the unique features of BMPR1A and presents novel approaches for its production and optimization, aiming to uncover its therapeutic potential in bone-related disorders.
Characteristics and Signaling Pathways:
BMPR1A belongs to the serine/threonine kinase receptor family and is expressed predominantly in skeletal tissues. It binds bone morphogenetic proteins (BMPs), initiating intracellular signaling cascades that regulate osteoblast differentiation and bone formation. BMPR1A activates the Smad-dependent and Smad-independent pathways, leading to the activation of transcription factors involved in bone-specific gene expression.
Production of BMPR1A Human Recombinant:
Efficient production methodologies are critical for harnessing the therapeutic potential of BMPR1A human recombinant. Mammalian cell-based expression systems, such as Chinese hamster ovary (CHO) cells, have been utilized to ensure proper folding and post-translational modifications. Optimization strategies, including codon optimization and vector engineering, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to obtain high-quality BMPR1A recombinant protein.
Potential Therapeutic Applications:
BMPR1A human recombinant holds significant promise in regenerative medicine. Disruption of BMP signaling has been implicated in skeletal disorders, including bone fractures, osteoporosis, and skeletal dysplasias. Modulating BMPR1A activity using BMPR1A human recombinant may provide a targeted therapeutic approach for promoting bone regeneration, fracture healing, and bone tissue engineering. Furthermore, BMPR1A signaling plays a role in other tissues, such as the cardiovascular system and nervous system, suggesting broader therapeutic applications.
Conclusion:
BMPR1A human recombinant represents a crucial regulator in bone development and holds immense potential in regenerative medicine. Optimizing production methodologies and further understanding its signaling pathways will enhance its clinical utility. With its implications in skeletal disorders and potential applications in other tissues, BMPR1A human recombinant stands as a promising tool for promoting bone regeneration and tissue engineering.
What is the molecular weight/Mw of BMPR1A Protein?
BMPR1A Protein has a total Mw of 23kDa.
What is the source or expression system of BMPR1A Protein?
Insect Cells.
What is the Purity of BMPR1A Protein?
BMPR1A Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of BMPR1A Protein?
Measured by its ability to inhibit recombinant human BMP-2 induced alkaline phosphatase production by C2C12 myogenic cells. The ED50 for this effect is typically 1-3 µg/ml in the presence of 500 ng/ml of recombinant human BMP-2 corresponding to a Specific Activity of 2,000 units/mg.
What applications can BMPR1A Protein be used in?
BMPR1A Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMPR1A Protein?
The endotoxin level is minimal, BMPR1A 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 :
SFRP5 HumanDescription:
Secreted Frizzled-Related Protein 5 Human Recombinant
Secreted Frizzled-Related Protein 5, SARP3, Secreted Apoptosis Related Protein 3, Secreted Apoptosis-Related Protein 3, Frizzled-Related Protein 1b, FRP-1b, SARP-3, SFRP-5, FRP1B, SFRP5.
Product # :
PRO-2171Price :
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Description
SFRP5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 311 amino acids (30-317 a.a) and having a molecular mass of 35kDa.SFRP5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SFRP5 protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Secreted Frizzled-Related Protein 5, also known as SFRP5, belongs to the SFRP family which includes a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRPs perform like soluble modulators of Wnt signaling. SFRP5 & SFRP1 are implicated in determining the polarity of photoreceptor cells in the retina. SFRP5 is highly expressed in the retinal pigment epithelium, as well as moderately expressed in the pancreas.
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Synonyms
Secreted Frizzled-Related Protein 5, SARP3, Secreted Apoptosis Related Protein 3, Secreted Apoptosis-Related Protein 3, Frizzled-Related Protein 1b, FRP-1b, SARP-3, SFRP-5, FRP1B, SFRP5.
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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 MGSEEYDYYG WQAEPLHGRS YSKPPQCLDI PADLPLCHTV GYKRMRLPNL LEHESLAEVK QQASSWLPLL AKRCHSDTQV FLCSLFAPVC LDRPIYPCRS LCEAVRAGCA PLMEAYGFPW PEMLHCHKFP LDNDLCIAVQ FGHLPATAPP VTKICAQCEM EHSADGLMEQ MCSSDFVVKM RIKEIKIENG DRKLIGAQKK KKLLKPGPLK RKDTKRLVLH MKNGAGCPCP QLDSLAGSFL VMGRKVDGQL LLMAVYRWDK KNKEMKFAVK FMFSYPCSLY YPFFYGAAEP H.
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 :
SERPING1 Human HEKDescription:
Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant HEK
C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.
Product # :
PRO-1639Price :
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Shipped at Room temp
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Description
SERPING1 Human Recombinant produced by transfected human cells is a single polypeptide chain containing 486 amino acids (23-500). SERPING1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
SERPING1 was lyophilized from a 0.2 µM filtered solution of 20mM Tris-HCl and 150mM NaCl, pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.
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Synonyms
C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SERPING1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPING1 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 SERPING1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTT
EPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKK
VETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAI
RDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTT
FDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQ
ALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQ
HQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFMLWDQQHKFPVFMGRVYDPRAVDHHHHHH
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 :
CEACAM21 HumanDescription:
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 21 Human Recombinant
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 21, CEACAM3, R29124_1.
Product # :
PRO-1637Price :
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Description
CEACAM21 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (35-240) and having a molecular mass of 25.0kDa.CEACAM21 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CEACAM21 solution 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
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Introduction
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 21 (CEACAM21) belongs to the family of carcinoembryonic antigen-related cell adhesion molecules (CEACAMs), which are used by a number of bacterial pathogens to bind and invade host cells. The transmembrane protein guides phagocytosis of several bacterial species which is dependent on the small GTPase Rac. CEACAM21 is assumed to have a central role in controlling human-specific pathogens by the innate immune system.
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Synonyms
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 21, CEACAM3, R29124_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 MGSWLFIASA PFEVAEGENV HLSVVYLPEN LYSYGWYKGK TVEPNQLIAA YVIDTHVRTP GPAYSGRETI SPSGDLHFQN VTLEDTGYYN LQVTYRNSQI EQASHHLRVY ESVAQPSIQA SSTTVTEKGS VVLTCHTNNT GTSFQWIFNN QRLQVTKRMK LSWFNHVLTI DPIRQEDAGE YQCEVSNPVS SNRSDPLKLT VKSDDNTLG.
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 :
MALD1Description:
Major Allergen Mal d 1 Recombinant (Mal d 1.0108)
Major allergen Mal d 1, Ypr10 protein, MALD1, ypr10, Mal d 1.0108
Product # :
ALR-013Price :
Quantity :
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Description
Recombinant MALD1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 17,492 Dalton. MALD1 purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
MALD1 is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
MALD1 is a ribonuclease and a heat-sensitive allergen which is a member of the pathogenesis-related protein class. MALD1 shares homologous IgE epitopes with major birch pollen allergen Bet v 1 and Cor a 1 from hazelnut pollen.
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Synonyms
Major allergen Mal d 1, Ypr10 protein, MALD1, ypr10, Mal d 1.0108
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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 :
NRBF2 HumanDescription:
Nuclear Receptor Binding Factor 2 Human Recombinant
Nuclear receptor binding factor 2, COPR1, COPR2, NRBF-2, Nuclear receptor-binding factor 2, Comodulator of PPAR and RXR, NRBF2, COPR.
Product # :
PRO-1692Price :
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Description
NRBF2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (45-287) and having a molecular mass of 29.9 kDa.NRBF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NRBF2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Nuclear receptor binding factor 2 (NRBF2) which works as transcriptional activator, modulates transcriptional activation by target nuclear receptors.
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Synonyms
Nuclear receptor binding factor 2, COPR1, COPR2, NRBF-2, Nuclear receptor-binding factor 2, Comodulator of PPAR and RXR, NRBF2, COPR.
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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 MGSMKLTQSE QAHLSLELQR DSHMKQLLLI QERWKRAQRE ERLKAQQNTD KDAAAHLQTS HKPSAEDAEG QSPLSQKYSP STEKCLPEIQ GIFDRDPDTL LYLLQQKSEP AEPCIGSKAP KDDKTIIEEQ ATKIADLKRH VEFLVAENER LRKENKQLKA EKARLLKGPI EKELDVDADF VETSELWSLP PHAETATASS TWQKFAANTG KAKDIPIPNL PPLDFPSPEL PLMELSEDIL KGFMNN.
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 :
NHEJ1 HumanDescription:
Nonhomologous End-Joining Factor 1 Human Recombinant
Nonhomologous end-joining factor 1, Protein cernunnos, XRCC4-like factor, Cernunnos, XLF, FLJ12610.
Product # :
PRO-1193Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
NHEJ1 Human Recombinant produced in E. coli is a single polypeptide chain containing 247 amino acids (1-224) and having a molecular mass of 27.8 kDa.NHEJ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NHEJ1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Non-homologous end-joining factor 1 (NHEJ1) is a member of the XLF family. NHEJ1 is a DNA repair factor vital for the nonhomologous end-joining pathway, which preferentially mediates repair of double-stranded breaks. NHEJ1 gene mutations cause different kinds of severe combined immunodeficiency disorders. NHEJ1 was initially detected as the protein mutated in five patients with growth retardation, microcephaly, and immunodeficiency. In addition, patients with NHEJ1 mutations have immunodeficiency caused by a defect in V(D)J recombination, which employs NHEJ to promote immune system diversity.
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Synonyms
Nonhomologous end-joining factor 1, Protein cernunnos, XRCC4-like factor, Cernunnos, XLF, FLJ12610.
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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 MGS MEELEQG LLMQPWAWLQ LAENSLLAKV FITKQGYALL VSDLQQVWHE QVDTSVVSQR AKELNKRLTA PPAAFLCHLD NLLRPLLKDA AHPSEATFSC DCVADALILR VRSELSGLPF YWNFHCMLAS PSLVSQHLIR PLMGMSLALQ CQVRELATLL HMKDLEIQDY QESGATLIRD RLKTEPFEEN SFLEQFMIEK LPEACSIGDG KPFVMNLQDL YMAVTTQ
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 :
TPRKB HumanDescription:
TP53RK Binding Protein Human Recombinant
TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.
Product # :
PRO-1185Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
TPRKB Human Recombinant produced E. coli is a single polypeptide chain containing 199 amino acids (1-175) and having a molecular mass of 22.2kDa.TPRKB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TPRKB solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
TPRKB is a member of the CGI121/TPRKB family. TPRKB is localized to nucleus and cytoplasm and is ubiquitously expressed. TPRKB is known to cooperate with TP53RK/PRPK.
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Synonyms
TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.
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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 MGSHMQLTHQ LDLFPECRVT LLLFKDVKNA GDLRRKAMEG TIDGSLINPT VIVDPFQILV AANKAVHLYK LGKMKTRTLS TEIIFNLSPN NNISEALKKF GISANDTSIL IVYIEEGEKQ INQEYLISQV EGHQVSLKNL PEIMNITEVK KIYKLSSQEE SIGTLLDAII CRMSTKDVL
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 :
CYTH3 HumanDescription:
Cytohesin 3 Human Recombinant
Cytohesin 3, PSCD3, ARNO3, GRP1, PH SEC7 and Coiled-Coil Domain-Containing Protein 3 , Pleckstrin Homology Sec7 and Coiled-Coil Domains 3, General Receptor of Phosphoinositides 1 , ARF Nucleotide-Binding Site Opener 3 , Protein ARNO3 , Cytohesin-3, CYTH3.
Product # :
PRO-1951Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CYTH3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (1-399) and having a molecular mass of 48.7 kDa.CYTH3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CYTH3 solution (0.25mg/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
Cytohesin 3 (CYTH3) belongs to the PSCD family, whose members have identical structural organization which consists of an N-terminal coiled-coil motif, a central Sec7 domain, and a C-terminal pleckstrin homology (PH) domain, and seem to mediate the regulation of protein sorting and membrane trafficking. CYTH3 is involved in the regulation of Golgi structure and function, and it might have a physiological role in regulating ADP-ribosylation factor protein 6 (ARF) functions, in addition to acting on ARF1.
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Synonyms
Cytohesin 3, PSCD3, ARNO3, GRP1, PH SEC7 and Coiled-Coil Domain-Containing Protein 3 , Pleckstrin Homology Sec7 and Coiled-Coil Domains 3, General Receptor of Phosphoinositides 1 , ARF Nucleotide-Binding Site Opener 3 , Protein ARNO3 , Cytohesin-3, CYTH3.
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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 MGSMDEDGGG EGGGVPEDLS LEEREELLDI RRRKKELIDD IERLKYEIAE VMTEIDNLTS VEESKTTQRN KQIAMGRKKF NMDPKKGIQF LIENDLLQSS PEDVAQFLYK GEGLNKTVIG DYLGERDEFN IKVLQAFVEL HEFADLNLVQ ALRQFLWSFR LPGEAQKIDR MMEAFASRYC LCNPGVFQST DTCYVLSFAI IMLNTSLHNH NVRDKPTAER FIAMNRGINE GGDLPEELLR NLYESIKNEP FKIPEDDGND LTHTFFNPDR EGWLLKLGGR VKTWKRRWFI LTDNCLYYFE YTTDKEPRGI IPLENLSIRE VEDPRKPNCF ELYNPSHKGQ VIKACKTEAD GRVVEGNHVV YRISAPSPEE KEEWMKSIKA SISRDPFYDM LATRKRRIAN KK.
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 :
EGLN3 HumanDescription:
Egl Nine Homolog 3 Human Recombinant
Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.
Product # :
PRO-1143Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
EGLN3 Human Recombinant produced in E. coli is a single polypeptide chain containing 263 amino acids (1-239) and having a molecular mass of 29.8 kDa.EGLN3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EGLN3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 300mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Egl Nine Homolog 3 (EGLN3) belongs to the EGLN family of prolyl hydroxylases. EGLN3 catalyzes hydroxylation of the ? subunit of hypoxia-inducible factor-?, which targets hypoxia-inducible factor-? for ubiquitination by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor. EGLN3 is the most significant isozyme in limiting physiological activation of HIFs (especially HIF2A) in hypoxia. EGLN3 is activated in cardiovascular cells and Hela cells after exposure to hypoxia. In addition, EGLN3 hydroxylates PKM2 in hypoxia, thus limiting glycolysis. Under normoxia, EGLN3 hydroxylates and regulates the stability of ADRB2. EGLN3 is inhibited by polynitrogen compounds possibly by chelation to Fe2+ ions.
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Synonyms
Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-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
MGSSHHHHHH SSGLVPRGSH MGSHMPLGHI MRLDLEKIAL EYIVPCLHEV GFCYLDNFLG EVVGDCVLER VKQLHCTGAL RDGQLAGPRA GVSKRHLRGD QITWIGGNEE GCEAISFLLS LIDRLVLYCG SRLGKYYVKE RSKAMVACYP GNGTGYVRHV DNPNGDGRCI TCIYYLNKNW DAKLHGGILR IFPEGKSFIA DVEPIFDRLL FFWSDRRNPH EVQPSYATRY AMTVWYFDAE ERAEAKKKFR NLTRKTESAL TED
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 :
AGO2 (1-200) HumanDescription:
Argonaute 2 (1-200 a.a.) Human Recombinant
Protein argonaute-2, Argonaute2, hAgo2, Argonaute RISC catalytic component 2, Eukaryotic translation initiation factor 2C 2, eIF-2C 2, eIF2C 2, PAZ Piwi domain protein, PPD, AGO2, EIF2C2, Protein slicer.
Product # :
PRO-2578Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
- formulation
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Description
AGO2 (1-200) Human Recombinant is a single, non-glycosylated, polypeptide chain containing 210 amino acids (1-200 a.a) and having a molecular mass of 23.7kDa (calculated). AGO2 (1-200) is fused to a 10 a.a His tag at N-terminal.
Source
Escherichia Coli.
Formulation
AGO2 (1-200) filtered (0.4 µm) and lyophilized from 0.5mg/ml in 50mM acetate buffer, pH 4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
The Argonaute protein is part of the RISC or RNA-induced silencing complex, as so, the protein has a key part in the slicing processes of RNA. The RNA interference (RNAi) is being held by RISC. Small non-coding RNA fragments bond to the Argonaute proteins, through base pairing, eventually leads to the cleavage of messenger RNA or translation suppression.
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Synonyms
Protein argonaute-2, Argonaute2, hAgo2, Argonaute RISC catalytic component 2, Eukaryotic translation initiation factor 2C 2, eIF-2C 2, eIF2C 2, PAZ Piwi domain protein, PPD, AGO2, EIF2C2, Protein slicer.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add 0.1M acetate buffer, pH 4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. AGO2 (1-200) is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS MYSGAGPALA PPAPPPPIQG YAFKPPPRPD FGTSGRTIKL QANFFEMDIP KIDIYHYELD IKPEKCPRRV NREIVEHMVQ HFKTQIFGDR KPVFDGRKNL YTAMPLPIGR DKVELEVTLP GEGKDRIFKV SIKWVSCVSL QALHDALSGR LPSVPFETIQ ALDVVMRHLP SMRYTPVGRS FFTASEGCSN PLGGGREVW.
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.