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1000 results found for “Neuritin”
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Name :
CHGA Human, Sf9Description:
Chromogranin A Human Recombinant, Sf9
CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.
Product # :
PRO-2513Price :
Quantity :
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Shipped with Ice Packs
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Description
CHGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-457 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 448 amino acids and having a molecular mass of 50kDa.CHGA shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CHGA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol & 0.1mM PMSF.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromogranin-A Isoform 1 Preproprotein or CHGA is part of the neuroendocrine secretory proteins of the chromogranin/secretogranin family. CHGA is a precursor of numerus enzymes such as pancreastatin, catestatin, vasostatin-1,vasostatin-2, and parastatin. The protein acts as a negative regulator the neuroendocrine activity of autocrine or nearby cells (paracrine). CHGA causes further production of secretory granules that contains insulin in pancreatic islet beta cells.
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Synonyms
CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.
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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
ADLLPVNSPM NKGDTEVMKC IVEVISDTLS KPSPMPVSQE CFETLRGDER ILSILRHQNL LKELQDLALQ GAKERAHQQK KHSGFEDELS EVLENQSSQA ELKEAVEEPS SKDVMEKRED SKEAEKSGEA TDGARPQALP EPMQESKAEG NNQAPGEEEE EEEEATNTHP PASLPSQKYP GPQAEGDSEG LSQGLVDREK GLSAEPGWQA KREEEEEEEE EAEAGEEAVP EEEGPTVVLN PHPSLGYKEI RKGESRSEAL AVDGAGKPGA EEAQDPEGKG EQEHSQQKEE EEEMAVVPQG LFRGGKSGEL EQEEERLSKE WEDSKRWSKM DQLAKELTAE KRLEGQEEEE DNRDSSMKLS FRARAYGFRG PGPQLRRGWR PSSREDSLEA GLPLQVRGYP EEKKEEEGSA NRRPEDQELE SLSAIEAELE KVAHQLQALR RGHHHHHH.
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 :
Streptavidin-NCDescription:
Streptavidin-NC Recombinant
Product # :
PRO-338Price :
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Description
Recombinant Streptavidin-NC produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 24kDa. Streptavidin-NC is engineered to bind to nitrocellulose.
Source
Escherichia Coli.
Formulation
The sterile solution contains 10mM K2HPO4-KH2PO4, pH 7.3.
Purity
Greater than 93.0% as determined by SDS-PAGE.
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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Physical Appearance
Sterile Liquid formulation.
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Stability
Streptavidin-NC although stable at 4°C for 3 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Adiponectin Porcine, HEKDescription:
Adiponectin Porcine Recombinant, HEK derived
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-696Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Acrp30 Porcine Recombinant contains a total of 238 amino acids having a molecular Mass of 26kDa. The Porcine Adiponectin is fused to a 13 amino acid long N-terminal FLAG tag.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
Sterile filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 90% as determined by SDS PAGE.
More Info
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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Stability
For long term, store lyophilized AdipoQ 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.The lyophilized protein remains stable for 24 months when stored at -20°C.
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Solubility
Add deionized water and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
HVDYKDDDDK PAGETTEKPG ALLPMPKGAC AGWMAGIPGH PGHNGTPGRD GRDGVPGEKG EKGDTGLTGP KGDTGESGVT GVEGPRGFPG IPGRKGEPGE SAYVYRSAFS VGLETRVTVP NMPIRFTKIF YNQQNHYDVT TGKFHCNIPG LYYFSFHITV LKDVKVSLYK DKAVLFTYDQ QDKNVDQASG VLLYLEKGDQ WLQAYGDEEN GVYADNVNDS FTGFLLYHNIE.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
HVDYKDDDDK PAGETTEKPG ALLPMPKGAC AGWMAGIPGH PGHNGTPGRD GRDGVPGEKG EKGDTGLTGP KGDTGESGVT GVEGPRGFPG IPGRKGEPGE SAYVYRSAFS VGLETRVTVP NMPIRFTKIF YNQQNHYDVT TGKFHCNIPG LYYFSFHITV LKDVKVSLYK DKAVLFTYDQ QDKNVDQASG VLLYLEKGDQ WLQAYGDEEN GVYADNVNDS FTGFLLYHNIE.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
DCTN2 (1-401) HumanDescription:
Dynactin 2 (1-401 a.a.) Human Recombinant
DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.
Product # :
PRO-1776Price :
Quantity :
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Shipped with Ice Packs
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Description
Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (1-401 a.a) and having a molecular mass of 46.6kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.
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Synonyms
DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.
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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 MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAEE LTSTSVEHII VNPNAAYDKF KDKRVGTKGL DFSDRIGKTK RTGYESGEYE MLGEGLGVKE TPQQKYQRLL HEVQELTTEV EKIKTTVKES ATEEKLTPVL LAKQLAALKQ QLVASHLEKL LGPDAAINLT DPDGALAKRL LLQLEATKNS KGGSGGKTTG TPPDSSLVTY ELHSRPEQDK FSQAAKVAEL EKRLTELETA VRCDQDAQNP LSAGLQGACL METVELLQAK VSALDLAVLD QVEARLQSVL GKVNEIAKHK ASVEDADTQS KVHQLYETIQ RWSPIASTLP ELVQRLVTIK QLHEQAMQFG QLLTHLDTTQ QMIANSLKDN TTLLTQVQTT MRENLATVEG NFASIDERMK KLGK.
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 :
NAE1 HumanDescription:
NEDD8 Activating Enzyme E1 Subunit 1 Human Recombinant
NEDD8-activating enzyme E1 regulatory subunit, Amyloid beta precursor protein-binding protein 1 59 kDa, APP-BP1, Amyloid protein-binding protein 1, Proto-oncogene protein 1, NAE1, APPBP1, HPP1, ula-1, A-116A10.1.
Product # :
ENZ-227Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NAE1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 557 amino acids (1-534) and having a molecular mass of 62.7kDa.NAE1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NAE1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
NEDD8-activating enzyme E1 regulatory subunit (NAE1) is a member of the ubiquitin-activating E1 family. NAE1 binds to the beta-amyloid precursor protein. Beta-amyloid precursor protein is a cell surface protein with signal-transducing properties, and it is believed to have a role in the pathogenesis of Alzheimer's disease. NAE1 participates in a unique ubiquitinylation-related pathway involving the ubiquitin-like molecule NEDD8. Furthermore, the NAE1 protein is essential for cell cycle progression through the S/M checkpoint.
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Synonyms
NEDD8-activating enzyme E1 regulatory subunit, Amyloid beta precursor protein-binding protein 1 59 kDa, APP-BP1, Amyloid protein-binding protein 1, Proto-oncogene protein 1, NAE1, APPBP1, HPP1, ula-1, A-116A10.1.
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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).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAQLGKL LKEQKYDRQL RLWGDHGQEA LESAHVCLIN ATATGTEILK NLVLPGIGSF TIIDGNQVSG EDAGNNFFLQ RSSIGKNRAE AAMEFLQELN SDVSGSFVEE SPENLLDNDP SFFCRFTVVV ATQLPESTSL RLADVLWNSQ IPLLICRTYG LVGYMRIIIK EHPVIESHPD NALEDLRLDK PFPELREHFQ SYDLDHMEKK DHSHTPWIVI IAKYLAQWYS ETNGRIPKTY KEKEDFRDLI RQGILKNENG APEDEENFEE AIKNVNTALN TTQIPSSIED IFNDDRCINI TKQTPSFWIL ARALKEFVAK EGQGNLPVRG TIPDMIADSG KYIKLQNVYR EKAKKDAAAV GNHVAKLLQS IGQAPESISE KELKLLCSNS AFLRVVRCRS LAEEYGLDTI NKDEIISSMD NPDNEIVLYL MLRAVDRFHK QQGRYPGVSN YQVEEDIGKL KSCLTGFLQE YGLSVMVKDD YVHEFCRYGA AEPHTIAAFL GGAAAQEVIK IITKQFVIFN NTYIYSGMSQ TSATFQL.
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 :
NDRG3 HumanDescription:
N-Myc Downstream Regulated 3 Human Recombinant
Protein NDRG3, N-myc downstream-regulated gene 3 protein, NDRG3, N-Myc Downstream Regulated 3.
Product # :
PRO-2100Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NDRG3 Human Recombinant produced in E. coli is a single polypeptide chain containing 386 amino acids (1-363) and having a molecular mass of 42.4 kDa.NDRG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NDRG3 solution (0.25mg/1ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
N-Myc Downstream Regulated 3, also known as NDRG3, is a protein coding gene which is a part of the NDRG family and is expressed greatly in brain. NDRG2 is an important paralog of NDRG3.
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Synonyms
Protein NDRG3, N-myc downstream-regulated gene 3 protein, NDRG3, N-Myc Downstream Regulated 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 MGSMDELQDV QLTEIKPLLN DKEHDIETTH GVVHVTIRGL PKGNRPVILT YHDIGLNHKS CFNAFFNFED MQEITQHFAV CHVDAPGQQE GAPSFPTGYQ YPTMDELAEM LPPVLTHLSL KSIIGIGVGA GAYILSRFAL NHPELVEGLV LINVDPCAKG WIDWAASKLS GLTTNVVDII LAHHFGQEEL QANLDLIQTY RMHIAQDINQ DNLQLFLNSY NGRRDLEIER PILGQNDNKS KTLKCSTLLV VGDNSPAVEA VVECNSRLNP INTTLLKMAD CGGLPQVVQP GKLTEAFKYF LQGMGYIPSA SMTRLARSRT HSTSSSLGSG ESPFSRSVTS NQSDGTQESC ESPDVLDRHQ TMEVSC.
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 :
NHLH2 HumanDescription:
Nescient Helix Loop Helix 2 Human Recombinant
nescient helix loop helix 2, bHLHa34, HEN2, NSCL2, Class A basic helix-loop-helix protein 34, NHLH2, KIAA0490.
Product # :
PRO-1487Price :
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Shipping Method :
Shipped with Ice Packs
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Description
NHLH2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (1-135 a.a.) and having a molecular mass of 17.4kDa.NHLH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NHLH2 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 50% glycerol and 5mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Nescient Helix Loop Helix 2 (NHLH2) belongs to the basic helix-loop-helix (bHLH) transcription factor family. NHLH2 is expressed in developing and adult neuroendocrine tissues for example the pituitary and hypothalamus. NHLH2 can act as a DNA-binding protein and may be involved in the control of cell-type determination, probably in the developing nervous system.
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Synonyms
nescient helix loop helix 2, bHLHa34, HEN2, NSCL2, Class A basic helix-loop-helix protein 34, NHLH2, KIAA0490.
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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 MGSMMLSPDQ AADSDHPSSA HSDPESLGGT DTKVLGSVSD LEPVEEAEGD GKGGSRAALY PHPQQLSREE KRRRRRATAK YRSAHATRER IRVEAFNLAF AELRKLLPTL PPDKKLSKIE ILRLAICYIS YLNHVLDV.
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 :
NMNAT1 Human, ActiveDescription:
Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant , Active
NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.
Product # :
ENZ-1002Price :
Quantity :
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Shipped with Ice Packs
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Description
NMNAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-279 a.a.) and having a molecular mass of 36 kDa. The NMNAT1 is fused to a 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NMNAT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 7,000 pmol/min/ug, and was obtained by measuring the beta-NAD from nicotinamide mononucleotide and ATP per minute at pH 8.0 at 37C.More Info
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Introduction
NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.
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Synonyms
NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMENS EKTEVVLLAC GSFNPITNMH LRLFELAKDY MNGTGRYTVV KGIISPVGDA YKKKGLIPAY HRVIMAELAT KNSKWVEVDT WESLQKEWKE TLKVLRHHQE KLEASDCDHQ QNSPTLERPG RKRKWTETQD SSQKKSLEPK TKAVPKVKLL CGADLLESFA VPNLWKSEDI TQIVANYGLI CVTRAGNDAQ KFIYESDVLW KHRSNIHVVN EWIANDISST KIRRALRRGQSIRYLVPDLV QEYIEKHNLY SSESEDRNAG VILAPLQRNT AEAKT.
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 :
ECSIT HumanDescription:
ECSIT homolog Human Recombinant
ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.
Product # :
PRO-1241Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ECSIT Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (19-217) and having a molecular mass of 24.6 kDa.ECSIT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ECSIT solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ECSIT homolog (ECSIT) is a ubiquitously expressed protein which has a vital role as an adaptor protein in the cytosolic signal transduction cascade events triggered by Toll receptor activation. ECSIT promotes proteolytic activation of MAP3K1. ECSIT is also involved in the BMP signaling pathway. ECSIT is essential for normal embryonic development. ECSIT was originally classified as a cytoplasmic protein interacting specifically with TNF receptor associated factor (TRAF)-6 in the TLR pathway. ECSIT gene knockdown results in gravely impaired complex I assembly and disrupted mitochondrial function.
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Synonyms
ECSIT Homolog (Drosophila), Evolutionarily Conserved Signaling Intermediate In Toll Pathway Mitochondrial, Likely Ortholog Of Mouse Signaling Intermediate In Toll Pathway Evolutionarily Conserved, Protein SITPEC.
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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 MGSGTCGAAL TGTSISQVPL PKDSTGAADP PQPHIVGIQS PDQQAALARH NPARPVFVEG PFSLWLRNKC VYYHILRADL LPPEEREVEE TPEEWNLYYP MQLDLEYVRS GWDNYEFDIN EVEEGPVFAM CMAGAHDQAT MAKWIQGLQE TNPTLAQIPV VFRLAGSTRE LQTSSAGLEE PPLPEDHQEE DDNLQRQQQG QS
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 :
BCCIP HumanDescription:
BRCA2 And CDKN1A Interacting Protein Human Recombinant
BRCA2 and CDKN1A-interacting protein, P21- and CDK-associated protein 1, Protein TOK-1, BCCIP, TOK1, BRCA2 and CDKN1A-interacting protein.
Product # :
PRO-2014Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BCCIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-314 a.a.) and having a molecular mass of 38.6kDa.BCCIP is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BCCIP protein solution (0.5mg/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
BRCA2 And CDKN1A Interacting Protein (BCCIP) is a nuclear protein with multiple interacting domains which remained conserved throughout the evolution. BCCIP is an important cofactor for BRCA2 in tumor suppression, and a modulator of CDK2 kinase activity via p21. BCCIP takes also part in the regulation of BRCA2 and RAD51 nuclear focus formation, doublestrand break-induced homologous recombination, and cell cycle progression.
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Synonyms
BRCA2 and CDKN1A-interacting protein, P21- and CDK-associated protein 1, Protein TOK-1, BCCIP, TOK1, BRCA2 and CDKN1A-interacting protein.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMASRS KRRAVESGVP QPPDPPVQRD EEEEKEVENE DEDDDDSDKE KDEEDEVIDE EVNIEFEAYS LSDNDYDGIK KLLQQLFLKA PVNTAELTDL LIQQNHIGSV IKQTDVSEDS NDDMDEDEVF GFISLLNLTE RKGTQCVEQI QELVLRFCEK NCEKSMVEQL DKFLNDTTKP VGLLLSERFI NVPPQIALPM YQQLQKELAG AHRTNKPCGK CYFYLLISKT FVEAGKNNSK KKPSNKKKAA LMFANAEEEF FYEKAILKFN YSVQEESDTC LGGKWSFDDV PMTPLRTVML IPGDKMNEIM DKLKEYLSV.
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 :
C19ORF80 RatDescription:
Chromosome 19 Open Reading Frame 80 Rat Recombinant
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
Product # :
PRO-2024Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
C19ORF80 Rat Recombinant produced in E. coli is a polypeptide chain containing 193 amino acids and having a total molecular mass of 22.0 kDa. C19ORF80 has a N-Terminal His-tag (10 AA residue).
Source
Escherichia Coli.
Formulation
Filtered (0.4 µm) and lyophilized from a 0.5mg/ml solution containing 0.03M Acetate buffer pH 4.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.
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Synonyms
Betatrophin, Angiopoietin-like protein 8, Lipasin, C19orf80, Angptl8, RIFL, TD26, PRO1185, PVPA599.
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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. 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 antigen is limited. C19ORF80 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 VRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYKA TEARLTEAGR NLGLFDQALE FLGREVNQGR DATRELRTSL SEIQAEEDTL HLRAEATARS LREVARAQHA LRNSVRRLQV QLRGAWLGQA HQEFENLKDR ADKQNHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHMAA LPA
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 :
PI3 Human, Sf9Description:
Peptidase Inhibitor 3 Human Recombinant, Sf9
Elafin, ESI, SKALP, WAP3, WFDC14.
Product # :
PRO-2653Price :
Quantity :
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Description
PI3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 101 amino acids (23-117a.a) and having a molecular mass of 10.7kDa.PI3 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The PI3 solution (0.2mg/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
Peptidase Inhibitor 3, also referred to PI3, is neutrophil and pancreatic elastase-specific inhibitor of skin. The protein may prevent elastase mediated tissue proteolysis. PI3 has shown inhibition of alpha-4-beta-2/CHRNA2-CHRNB2 nicotinic acetylcholine receptor, a weak inhibition on Kv11.1/KCNH2/ERG1 and on the transient receptor potential cation channel subfamily V member 1.
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Synonyms
Elafin, ESI, SKALP, WAP3, WFDC14.
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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
AVTGVPVKGQ DTVKGRVPFN GQDPVKGQVS VKGQDKVKAQ EPVKGPVSTK PGSCPIILIR CAMLNPPNRC LKDTDCPGIK KCCEGSCGMA CFVPQHHHHH 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 :
Procalcitonin HumanDescription:
Procalcitonin Human Recombinant
Procalcitonin, PCT.
Product # :
HOR-304Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Procalcitonin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids and having a molecular mass of 12.8 kDa.The Procalcitonin is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 10mM sodium phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
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Synonyms
Procalcitonin, PCT.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized procalcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution procalcitonin 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 procalcitonin sterile 18MΩ-cm H2O at 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APFRSALESS PADPATLSED EARLLLAALV QDYVQMKASE LEQEQEREGS SLDSPRSKRC GNLSTCMLGT YTQDFNKFHT FPQTAIGVGA PGKKRDMSSD LERDHRPHVS MPQNAN.
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 :
UBLCP1 HumanDescription:
Ubiquitin-Like Domain Containing CTD Phosphatase 1 Human Recombinant
CPUB1, Ubiquitin-like domain-containing CTD phosphatase 1, Nuclear proteasome inhibitor UBLCP1.
Product # :
PRO-151Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UBLCP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-318 a.a) and having a molecular mass of 39.2kDa.UBLCP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UBLCP1 protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation averts assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.
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Synonyms
CPUB1, Ubiquitin-like domain-containing CTD phosphatase 1, Nuclear proteasome inhibitor UBLCP1.
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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 MGSMALPIIV KWGGQEYSVT TLSEDDTVLD LKQFLKTLTG VLPERQKLLG LKVKGKPAEN DVKLGALKLK PNTKIMMMGT REESLEDVLG PPPDNDDVVN DFDIEDEVVE VENREENLLK ISRRVKEYKV EILNPPREGK KLLVLDVDYT LFDHRSCAET GVELMRPYLH EFLTSAYEDY DIVIWSATNM KWIEAKMKEL GVSTNANYKI TFMLDSAAMI TVHTPRRGLI DVKPLGVIWG KFSEFYSKKN TIMFDDIGRN FLMNPQNGLK IRPFMKAHLN RDKDKELLKL TQYLKEIAKL DDFLDLNHKY WERYLSKKQG Q.
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 :
UFD1L HumanDescription:
Ubiquitin Fusion Degradation 1 Like Human Recombinant
Ubiquitin Fusion Degradation 1 Like (Yeast), UB Fusion Protein 1, Ubiquitin Fusion Degradation Protein 1 Homolog, UFD1.
Product # :
PRO-1625Price :
Quantity :
Shipping Method :
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Description
UFD1L Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (1-307) and having a molecular mass of 36.9kDa.UFD1L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UFD1L solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
UFD1L forms a complex with two other proteins, nuclear protein localization-4 and valosin-containing protein, and this complex is necessary for the degradation of ubiquitinated proteins. In addition, this complex controls the disassembly of the mitotic spindle and the formation of a closed nuclear envelope after mitosis. Mutations in this gene have been associated with Catch 22 syndrome as well as cardiac and craniofacial defects. Alternative splicing results in multiple transcript variants encoding different isoforms. A related pseudogene has been identified on chromosome 18.
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Synonyms
Ubiquitin Fusion Degradation 1 Like (Yeast), UB Fusion Protein 1, Ubiquitin Fusion Degradation Protein 1 Homolog, UFD1.
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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 MGSMFSFNMF DHPIPRVFQN RFSTQYRCFS VSMLAGPNDR SDVEKGGKII MPPSALDQLS RLNITYPMLF KLTNKNSDRM THCGVLEFVA DEGICYLPHW MMQNLLLEEG GLVQVESVNL QVATYSKFQP QSPDFLDITN PKAVLENALR NFACLTTGDV IAINYNEKIY ELRVMETKPD KAVSIIECDM NVDFDAPLGY KEPERQVQHE ESTEGEADHS GYAGELGFRA FSGSGNRLDG KKKGVEPSPS PIKPGDIKRG IPNYEFKLGK ITFIRNSRPL VKKVEEDEAG GRFVAFSGEG QSLRKKGRKP
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 :
ACTN1 HumanDescription:
Actinin Alpha 1 Human Recombinant
ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.
Product # :
PRO-2227Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-249 a.a) and having a molecular mass of 31.4kDa. ACTN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ACTN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.
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Synonyms
ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-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 MGSEFMDHYD SQQTNDYMQP EEDWDRDLLL DPAWEKQQRK TFTAWCNSHL RKAGTQIENI EEDFRDGLKL MLLLEVISGE RLAKPERGKM RVHKISNVNK ALDFIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ RKTAPYKNVN IQNFHISWKD GLGFCALIHR HRPELIDYGK LRKDDPLTNL NTAFDVAEKY LDIPKMLDAE DIVGTARPDE KAIMTYVSSF YHAF.
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 :
NFKBIA HumanDescription:
NF-kappa-B Inhibitor Alpha Human Recombinant
Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor alpha, nuclear factor of kappa light chain gene enhancer in B-cells, IKBA, I-kappa-B-alpha, IkappaBalpha, ikB-alpha, NFKBI, MAD-3, Major histocompatibility complex enhancer-binding protein MAD3, NF-kappa-B inhibitor alpha.
Product # :
PRO-960Price :
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Description
NFKBIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-317) and having a molecular mass of 37.7 kDa.NFKBIA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NFKBIA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
NFKBIA belongs to the I-kappa-B family of proteins which is separated into four groups (IkB-a, IkB-b, IkB-g, IkB-e). NFKBIA inhibits the NFkB complex by binding and impounding it in the cytoplasm. When stimulated, NFKBIA is phosphorylated on serine residues targeting it for degradation by the ubiquitin pathway.
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Synonyms
Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor alpha, nuclear factor of kappa light chain gene enhancer in B-cells, IKBA, I-kappa-B-alpha, IkappaBalpha, ikB-alpha, NFKBI, MAD-3, Major histocompatibility complex enhancer-binding protein MAD3, NF-kappa-B inhibitor alpha.
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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 MFQAAERPQE WAMEGPRDGL KKERLLDDRH DSGLDSMKDE EYEQMVKELQ EIRLEPQEVP RGSEPWKQQL TEDGDSFLHL AIIHEEKALT MEVIRQVKGD LAFLNFQNNL QQTPLHLAVI TNQPEIAEAL LGAGCDPELR DFRGNTPLHL ACEQGCLASV GVLTQSCTTP HLHSILKATN YNGHTCLHLA SIHGYLGIVE LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG ADVNRVTYQG YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEFTE DELPYDDCVF GGQRLTL
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 :
PFN2 HumanDescription:
Profilin-2 Human Recombinant
Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.
Product # :
PRO-809Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PFN2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.2 kDa. PFN2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
PFN2 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PFN2 is a ubiquitous actin monomer-binding protein which is part of the profilin family. PFN2 regulates actin polymerization in response to extra cellular signals. PFN2 binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, while it increases it at low concentrations. PFN2 binds to PIP2, it inhibits the formation of IP3 and DG.
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Synonyms
Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.
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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 MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF TNGLALGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF.
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 :
PI3 HumanDescription:
Peptidase Inhibitor 3 Human Recombinant
Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.
Product # :
PRO-1627Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PI3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (23-117) and having a molecular mass of 12.0kDa.PI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PI3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
PI3 is an elastase-specific protease inhibitor, which contains a WAP-type four-disulfide core (WFDC) domain, and is thus a member of the WFDC domain family. Most WFDC gene members are localized to chromosome 20q12-q13 in two clusters: centromeric and telomeric. PI3 belongs to the centromeric cluster.
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Synonyms
Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 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 MGSAVTGVPV KGQDTVKGRV PFNGQDPVKG QVSVKGQDKV KAQEPVKGPV STKPGSCPII LIRCAMLNPP NRCLKDTDCP GIKKCCEGSC GMACFVPQ
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 :
CETN1 HumanDescription:
Centrin-1 Human Recombinant
Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.
Product # :
PRO-1104Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CETN1 Human Recombinant produced E. coli is a single polypeptide chain containing 196 amino acids (1-172) and having a molecular mass of 22.1kDa.CETN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CETN1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CETN1 is an EF-hand type Ca2+-binding protein. CETN1 is localized to the centrosome of interphase cells, and reorganizes the region of the spindle poles during mitosis, reflecting the dynamic behavior of the centrosome during the cell cycle. CETN1 has a vital part in the determination of centrosome position and isolation, and in the course of microtubule separating.
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Synonyms
Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.
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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 MGSHMASGFK KPSAASTGQK RKVAPKPELT EDQKQEVREA FDLFDVDGSG TIDAKELKVA MRALGFEPRK EEMKKMISEV DREGTGKISF NDFLAVMTQK MSEKDTKEEI LKAFRLFDDD ETGKISFKNL KRVANELGEN LTDEELQEMI DEADRDGDGE VNEEEFLRIM KKTSLY
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 :
MGAT2 HumanDescription:
Mannoside Acetylglucosaminyltransferase 2 Human Recombinant
Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase, GlcNAc-T II, Mannoside Acetylglucosaminyltransferase 2, GNT-II, Beta-1,2-N-Acetylglucosaminyltransferase II, N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II, EC 2.4.1.143, CDG2A, CDGS2, GLCNACTI, NT2, Alpha-1,6-Mannosyl-Glycoprotein 2-Beta-N-Acetylglucosaminyltransferase, UDP-N-Acetylglucosamine:Alpha-6-D-Mannoside, Beta-1,2-N-Acetylglucosaminyltransferase II.
Product # :
ENZ-781Price :
Quantity :
Shipping Method :
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Description
MGAT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (30-447a.a) and having a molecular mass of 50kDa. MGAT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MGAT2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Mannoside Acetylglucosaminyltransferase 2 (MGAT2) is a golgi enzyme catalyzing an vital step in the conversion of oligomannose to complex N-glycans. MGAT2 enzyme has the characteristic glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. MGAT2 gene mutations may lead to carbohydrate-deficient glycoprotein syndrome, type II.
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Synonyms
Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase, GlcNAc-T II, Mannoside Acetylglucosaminyltransferase 2, GNT-II, Beta-1,2-N-Acetylglucosaminyltransferase II, N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II, EC 2.4.1.143, CDG2A, CDGS2, GLCNACTI, NT2, Alpha-1,6-Mannosyl-Glycoprotein 2-Beta-N-Acetylglucosaminyltransferase, UDP-N-Acetylglucosamine:Alpha-6-D-Mannoside, Beta-1,2-N-Acetylglucosaminyltransferase II.
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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 MRQRKNEALA PPLLDAEPAR GAGGRGGDHP SVAVGIRRVS NVSAASLVPA VPQPEADNLT LRYRSLVYQL NFDQTLRNVD KAGTWAPREL VLVVQVHNRP EYLRLLLDSL RKAQGIDNVL VIFSHDFWST EINQLIAGVN FCPVLQVFFP FSIQLYPNEF PGSDPRDCPR DLPKNAALKL GCINAEYPDS FGHYREAKFS QTKHHWWWKL HFVWERVKIL RDYAGLILFL EEDHYLAPDF YHVFKKMWKL KQQECPECDV LSLGTYSASR SFYGMADKVD VKTWKSTEHN MGLALTRNAY QKLIECTDTF CTYDDYNWDW TLQYLTVSCL PKFWKVLVPQ IPRIFHAGDC GMHHKKTCRP STQSAQIESL LNNNKQYMFP ETLTISEKFT VVAISPPRKN GGWGDIRDHE LCKSYRRLQ.
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 :
Hemopexin HumanDescription:
Hemopexin Human Recombinant
Hemopexin, Beta-1B-glycoprotein, HPX, Haemopexin.
Product # :
PRO-1869Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Hemopexin Human Recombinant produced in E. coli is. a single polypeptide chain containing 462 amino acids (24-462) and having a molecular mass of 51.7kDa. Hemopexin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Hemopexin solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Hemopexin (or haemopexin) is a plasma protein that binds heme with the highest affinity of any known protein. Hemopexin is generally expressed in liver, and belongs to acute phase reactants, the synthesis of which is induced after inflammation. Heme is potentially very toxic because of its ability to intercalate into lipid membrane and to generate hydroxyl radicals. Hemopexin’s function of scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin defends the body from the oxidative damage that free heme can cause. Additionally, hemopexin discharges its bound ligand for internalisation upon interacting with a specific receptor located on the surface of liver cells. This hemopexin function is in order to preserve the body's iron. Hemopexin’s levels in the serum are an indication of how much heme is present in the blood. Low Hemopexin levels show that there is a lot of it in the serum. For that reason, low hemopexin levels indicate that there has been consid
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Synonyms
Hemopexin, Beta-1B-glycoprotein, HPX, Haemopexin.
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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 MGSTPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN GTGHGNSTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ WPQGPSAVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKRLEKEVG TPHGIILDSV DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ATWTELPWPH EKVDGALCME KSLGPNSCSA NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC TH.
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 :
CUTA HumanDescription:
CutA Divalent Cation Tolerance Homolog Human Recombinant
ACHAP, C6orf82, MGC111154, cutA divalent cation tolerance homolog, CUTA.
Product # :
PRO-812Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CUTA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids (33-179 a.a.) and having a molecular mass of 17.1 kDa. CUTA protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CUTA Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CUTA is the 179 amino acid mammalian homolog of the cutA E. coli protein and is ubiquitously expressed, particularly in brain tissue. CUTA participates in cellular tolerance to a broad range of divalent cations other than copper. The CUTA protein is a cytoplasmic protein, encoded by the single-gene operon and has been related to divalent cation tolerance.
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Synonyms
ACHAP, C6orf82, MGC111154, cutA divalent cation tolerance homolog, CUTA.
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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). Please prevent freeze thaw cycles.
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Amino Acid Sequence
MRLLLLPRVL LTMASGSPPT QPSPASDSGS GYVPGSVSAA FVTCPNEKVA KEIARAVVEK RLAACVNLIP QITSIYEWKG KIEEDSEVLM MIKTQSSLVP ALTDFVRSVH PYEVAEVIAL PVEQGNFPYL QWVRQVTESV SDSITVLPLE 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.
- View Data Sheet
Name :
Cyclophilin A MouseDescription:
Cyclophilin A Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.
Product # :
ENZ-857Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Cyclophilin A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-164a.a.) and having a molecular mass of 20.4kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
Cyclophilin A protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.
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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 MGSMVNPTVF FDITADDEPL GRVSFELFAD KVPKTAENFR ALSTGEKGFG YKGSSFHRII PGFMCQGGDF TRHNGTGGRS IYGEKFEDEN FILKHTGPGI LSMANAGPNT NGSQFFICTA KTEWLDGKHV VFGKVKEGMN IVEAMERFGS RNGKTSKKIT ISDCGQL.
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.