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1000 results found for “Cytochrome”
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Name :
LCN2 Human, PichiaDescription:
Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant, Pichia
Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.
Product # :
ENZ-064Price :
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Shipped at Room temp
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Description
Neutrophil Gelatinase Associated Lipocalin Human Recombinant is expressed in Pichia pastoris having a molecular weight of approximately 21kDa.The LCN2 is purified by proprietary chromatographic techniques.
Source
Pichia pastoris.
Formulation
LCN2 was lyophilized from 0.02M NH4HCO3.
Purity
Greater than 96% as determined by SDS-PAGE.
More Info
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Introduction
Recombinant Human Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke. -
Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LCN2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCN2 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 LCN2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
PRDX6 HumanDescription:
Peroxiredoxin-6 Human Recombinant
Peroxiredoxin-6, Antioxidant protein 2, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Non-selenium glutathione peroxidase, 24 kDa protein, Liver 2D page spot 40, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, NSGPx, PRDX6, AOP2, KIAA0106, PRX, p29, 1-Cys, MGC46173.
Product # :
ENZ-432Price :
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Description
Peroxiredoxin- 6 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 244 amino acids (1-224 a.a.) and having a molecular mass of 27.1kDa.The Peroxiredoxin-6 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Peroxiredoxin-6 solution contains 20mM Tris-HCl buffer (pH8.0) and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >2,000pmol/min/ug was defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25C for 1minute.
More Info
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Introduction
Peroxiredoxin 6 (PRDX6) belongs to the thiol-specific antioxidant protein family. PRDX6 is a bifunctional enzyme with 2 distinct active sites. PRDX6 is involved in redox regulation of the cell and can reduce Hydrogen peroxide and short chain organic, fatty acid, and phospholipid hydroperoxides. PRDX6 may have a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Furthermore, PRDX6 eases the oxidative stress and TGF-beta-induced abnormalities of human trabecular meshwork cells. In addition, PRDX6 is necessary for blood vessel integrity in injured skin.
At acidic pH, PRDX6 binds to reduced phospholipids, however at cytosolic pH PRDX6 binds only to phospholipids that are oxidized which is compatible with the role for PRDX6 in the repair of peroxidized cell membranes. Hydrogen peroxide-mediated hyperoxidation of PRDX6 induces cell cycle arrest at the G2/M transition via up-regulation of iPLA2 activity. Overexpression of PRDX6 is linked to oligodendroglioma. -
Synonyms
Peroxiredoxin-6, Antioxidant protein 2, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Non-selenium glutathione peroxidase, 24 kDa protein, Liver 2D page spot 40, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, NSGPx, PRDX6, AOP2, KIAA0106, PRX, p29, 1-Cys, MGC46173.
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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 MPGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF PIIDDRNREL AILLGMLDPA EKDEKGMPVT ARVVFVFGPD KKLKLSILYP ATTGRNFDEI LRVVISLQLT AEKRVATPVD WKDGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP.
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 :
CXCL3 HumanDescription:
GRO-Gamma Human Recombinant (CXCL3)
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma(1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
Product # :
CHM-310Price :
Quantity :
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Shipped at Room temp
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Description
GRO-Gamma Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7902 Dalton. The CXCL3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
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Synonyms
Macrophage inflammatory protein 2-beta, MIP2-beta, CXCL3, Growth-regulated protein gamma, GRO-gamma, GRO-gamma(1-73), GRO3, GROg, MIP2B, SCYB3, MIP-2b, CINC-2b, MGSA gamma.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 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 CXCL3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Val-Thr.
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Background
What is the molecular weight/Mw of CXCL3 HUMAN Protein?
CXCL3 HUMAN Protein has a total Mw of 7.9kDa.
What is the source or expression system of CXCL3 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL3 HUMAN Protein?
CXCL3 HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL3 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CXCL3 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Val-Thr.
What applications can CXCL3 HUMAN Protein be used in?
CXCL3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL3 HUMAN Protein?
The endotoxin level is minimal, CXCL3 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
URM1 HumanDescription:
Ubiquitin Related Modifier 1 Human Recombinant
Ubiquitin-related modifier 1 homolog, URM1, C9orf74, MGC2668, RP11-339B21.4.
Product # :
PRO-188Price :
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Description
URM1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101 a.a.) and having a molecular mass of 13.5kDa.URM1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The URM1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
URM1 is ubiquitin-related modifier 1 homolog protein which mainly functions in the post-translational modification of proteins via the urmylation pathway. Urm1 covalently binds to its E1 activating enzyme, Uba4p, to conjugate alkyl hydroperoxide reductase (Ahp1) as determined by studies with Saccharomyces cerevisiae. It has been theorized that this complex may then have a role in the oxidative-stress response in mammals.
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Synonyms
Ubiquitin-related modifier 1 homolog, URM1, C9orf74, MGC2668, RP11-339B21.4.
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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 MAAPLSVEVE FGGGAELLFD GIKKHRVTLP GQEEPWDIRN LLIWIKKNLL KERPELFIQG DSVRPGILVL INDADWELLG ELDYQLQDQD SVLFISTLHG G.
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 :
PYCR2 HumanDescription:
Pyrroline-5-Carboxylate Reductase 2 Human Recombinant
P5CR2, Pyrroline-5-carboxylate reductase 2 isoform 1, P5C reductase 2.
Product # :
ENZ-118Price :
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Description
PYCR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a) and having a molecular mass of 36kDa.PYCR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PYCR2 protein solution (0.25mg/ml) in phosphate buffered saline (pH7.4), 50% glycerol, 5mM DTT and 1mM EDTA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Pyrroline-5-carboxylate reductase 2 isoform 1 (PYCR2) is a member of the pyrroline-5-carboxylate reductase family. PYCR2 protein catalyzes the conversion of pyrroline-5-carboxylate to proline, which is the last step in proline biosynthesis. The three substrates of the PYCR2 enzyme are L-proline, NAD+, and NADP+, while its four products are 1-pyrroline-5-carboxylate, NADH, NADPH, and H+.
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Synonyms
P5CR2, Pyrroline-5-carboxylate reductase 2 isoform 1, P5C reductase 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 MGSMSVGFIG AGQLAYALAR GFTAAGILSA HKIIASSPEM NLPTVSALRK MGVNLTRSNK ETVKHSDVLF LAVKPHIIPF ILDEIGADVQ ARHIVVSCAA GVTISSVEKK LMAFQPAPKV IRCMTNTPVV VQEGATVYAT GTHALVEDGQ LLEQLMSSVG FCTEVEEDLI DAVTGLSGSG PAYAFMALDA LADGGVKMGL PRRLAIQLGA QALLGAAKML LDSEQHPCQL KDNVCSPGGA TIHALHFLES GGFRSLLINA VEASCIRTRE LQSMADQEKI SPAALKKTLL DRVKLESPTV STLTPSSPGK LLTRSLALGG KKD.
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 :
MAP1LC3B HumanDescription:
Microtubule-Associated Protein 1 Light Chain 3 Beta Human Recombinant
Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.
Product # :
PRO-076Price :
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Description
MAP1LC3B produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-120a.a.) and having a molecular mass of 16.2kDa.MAP1LC3B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAP1LC3B protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
1mM DTT, 100mM NaCl and 20% glycerol.Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
MAP1LC3B is a member of the MAP1 LC3 family. MAP1LC3B is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, that are involved in microtubule assembly and important for neurogenesis. In addition, MAP1LC3B takes part in formation of autophagosomal vacuoles and is expressed mainly in heart, testis, brain and skeletal muscle.
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Synonyms
Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.
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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 MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVYASQETFG
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 :
HBQ1 HumanDescription:
Hemoglobin Theta 1 Human Recombinant
Hemoglobin Theta 1, Hemoglobin Theta-1 Chain, Hemoglobin Subunit Theta-1, Theta-1-globin.
Product # :
PRO-1616Price :
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Description
HBQ1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-142) and having a molecular mass of 17.9kDa.HBQ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HBQ1 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
HBQ1 is a member of the Hemoglobin family. Hemoglobin is a 66.7 kDa protein attached to four iron-binding, methenelinked tetrapyrrole rings (heme). The globin part of Hemoglobin contains 2 alpha chains and 2 beta chains organized as couples creating a tetramer. Every one of the 4 globin chains covalently connects with a heme group. The bonds between alpha and beta chains are frailer than between parallel globin chains, thus creating a cleavage plane which is vital for oxygen binding and release. Relaxation of the alpha1-beta2 cleavage plane results in high affinity for oxygen.
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Synonyms
Hemoglobin Theta 1, Hemoglobin Theta-1 Chain, Hemoglobin Subunit Theta-1, Theta-1-globin.
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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 MGSMALSAED RALVRALWKK LGSNVGVYTT EALERTFLAF PATKTYFSHL DLSPGSSQVR AHGQKVADAL SLAVERLDDL PHALSALSHL HACQLRVDPA SFQLLGHCLL VTLARHYPGD FSPALQASLD KFLSHVISAL VSEYR
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 :
MYLPF HumanDescription:
Myosin Light chain, Phosphorylatable, Fast Skeletal Muscle Human Recombinant
Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.
Product # :
PRO-243Price :
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Description
MYLPF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a) and having a molecular mass of 21.2kDa.MYLPF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYLPF protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Myosin regulatory light chains, including MRCL3, MYLPF and MYL9, regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of myosin regulatory light chains, catalyzed by MLCK in the presence of calcium and calmodulin, increases the actin-activated myosin ATPase activity, thus regulating the contractile activity. MYLPF is vital for fast and slow skeletal muscle development.
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Synonyms
Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.
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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 MAPKRAKRRT VEGGSSSVFS MFDQTQIQEF KEAFTVIDQN RDGIIDKEDL RDTFAAMGRL NVKNEELDAM MKEASGPINF TVFLTMFGEK LKGADPEDVI TGAFKVLDPE GKGTIKKKFL EELLTTQCDR FSQEEIKNMW AAFPPDVGGN VDYKNICYVI THGDAKDQE.
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 :
NDUFA2 HumanDescription:
NADH Dehydrogenase 1 Alpha Subcomplex 2 Human Recombinant
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2, Complex I-B8, CI-B8, NADH-ubiquinone oxidoreductase B8 subunit, NDUFA2, CD14, CIB8.
Product # :
ENZ-660Price :
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Description
NDUFA2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 122 amino acids (1-99) and having a molecular mass of 13.3kDa.NDUFA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFA2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (NDUFA5) is a member of the complex I NDUFA5 subunit family. The human NDUFA5 gene codes for the B13 subunit of complex I of the respiratory chain that transfers electrons from NADH to ubiquinone. The NDUFA5 protein localizes to the inner mitochondrial membrane as part of the seven component-containing, water soluble 'iron-sulfur protein' (IP) fraction of complex I, even though its exact role is undetermined.
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Synonyms
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2, Complex I-B8, CI-B8, NADH-ubiquinone oxidoreductase B8 subunit, NDUFA2, CD14, CIB8.
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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 MGSMAAAAAS RGVGAKLGLR EIRIHLCQRS PGSQGVRDFI EKRYVELKKA NPDLPILIRE CSDVQPKLWA RYAFGQETNV PLNNFSADQV TRALENVLSG KA.
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 :
NNMT Human, ActiveDescription:
Nicotinamide N-Methyltransferase Human Recombinant, Active
Nicotinamide N-methyltransferase, EC 2.1.1.1, NNMT.
Product # :
ENZ-1060Price :
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Description
NNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (1-264 a.a) and having a molecular mass of 37.7kDa.NNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NNMT protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 8.0) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 100 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37C.
More Info
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Introduction
NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.
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Synonyms
Nicotinamide N-methyltransferase, EC 2.1.1.1, NNMT.
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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 MESGFTSKDT YLSHFNPRDY LEKYYKFGSR HSAESQILKH LLKNLFKIFC LDGVKGDLLI DIGSGPTIYQ LLSACESFKE IVVTDYSDQN LQELEKWLKK EPEAFDWSPV VTYVCDLEGN RVKGPEKEEK LRQAVKQVLK CDVTQSQPLG AVPLPPADCV LSTLCLDAAC PDLPTYCRAL RNLGSLLKPG GFLVIMDALK SSYYMIGEQK FSSLPLGREA VEAAVKEAGY TIEWFEVISQ SYSSTMANNE GLFSLVARKL SRPL.
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 :
BAG3 HumanDescription:
BCL2-Associated Athanogene 3 Human Recombinant
BIS, CAIR-1, BAG-3, BAG Family Molecular Chaperone Regulator 3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Docking protein CAIR-1, BAG3, MGC104307.
Product # :
PRO-760Price :
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Description
BAG3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 595 amino acids (1-575 a.a.) and having a molecular mass of 63.7 kDa. The BAG3 protein is fused to a 20 amino acid His Tag at N-terminus and purified by standard chromatogrpahy techniques.
Source
Escherichia Coli.
Formulation
The BAG3 protein contains 20mM Tris buffer pH-8, 1mM EDTA, 10% glycerol and 0.1mM PMSF.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
BAG3 Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. BAG3 has anti-apoptotic activity. BAG proteins participate with Hip for their binding to Hsc70/Hsp70 ATPase domain and encourage substrate release. BAG proteins have about 45 amino acid BAG domain close to the C terminus however they differ noticeably in their N-terminal regions. BAG3 includes a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact particularly with the Hsc70 ATPase domain in vitro and in mammalian cells. They bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. BAG3 plays a role as a protein-refolding cochaperone of the bcl2 binding protein BAG family and as upregulated in response to persistent stress of cellular calcium balance dysregulation. BAG3 has been shown to diminish stress-induced apoptosis.
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Synonyms
BIS, CAIR-1, BAG-3, BAG Family Molecular Chaperone Regulator 3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Docking protein CAIR-1, BAG3, MGC104307.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSAATHSPMM QVASGNGDRD PLPPGWEIKI DPQTGWPFFV DHNSRTTTWN DPRVPSEGPK ETPSSANGPS REGSRLPPAR EGHPVYPQLR PGYIPIPVLH EGAENRQVHP FHVYPQPGMQ RFRTEAAAAA PQRSQSPLRG MPETTQPDKQ CGQVAAAAAA QPPASHGPER SQSPAASDCS SSSSSASLPS SGRSSLGSHQ LPRGYISIPV IHEQNVTRPA AQPSFHQAQK THYPAQQGEY QTHQPVYHKI QGDDWEPRPL RAASPFRSSV QGASSREGSP ARSSTPLHSP SPIRVHTVVD RPQQPMTHRE TAPVSQPENK PESKPGPVGP ELPPGHIPIQ VIRKEVDSKP VSQKPPPPSE KVEVKVPPAP VPCPPPSPGP SAVPSSPKSV ATEERAAPST APAEATPPKP GEAEAPPKHP GVLKVEAILE KVQGLEQAVD NFEGKKTDKK YLMIEEYLTK ELLALDSVDP EGRADVRQAR RDGVRKVQTI LEKLEQKAID VPGQVQVYEL QPSNLEADQP LQAIMEMGAV AADKGKKNAG NAEDPHTETQ QPEATAAATS NPSSMTDTPG NPAAP.
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 :
HAAO HumanDescription:
3-Hydroxyanthranilate 3,4-Dioxygenase Human Recombinant
3-hydroxyanthranilate 3,4-dioxygenase, 3-hydroxyanthranilate oxygenase, 3-HAO, 3-hydroxyanthranilic acid dioxygenase, HAD, HAAO, HAO.
Product # :
ENZ-617Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HAAO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-286 a.a.) and having a molecular mass of 35kDa.HAAO is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HAAO 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
-
Introduction
HAAO is a monomeric cytosolic protein which is a member of intramolecular dioxygenases family containing nonheme ferrous iron. The HAAO protein catalyzes the synthesis of quinolinic acid (QUIN) from 3-hydroxyanthranilic acid. QUIN is an excitotoxin whose toxicity is facilitated by its ability to activate glutamate N-methyl-D-aspartate receptors. Amplified cerebral levels of QUIN may contribute to the pathogenesis of neurologic and inflammatory disorders. HAAO is widely distributed in peripheral organs, such as liver and kidney, and is also present in low amounts in the central nervous system.
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Synonyms
3-hydroxyanthranilate 3,4-dioxygenase, 3-hydroxyanthranilate oxygenase, 3-HAO, 3-hydroxyanthranilic acid dioxygenase, HAD, HAAO, HAO.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMERRLG VRAWVKENRG SFQPPVCNKL MHQEQLKVMF IGGPNTRKDY HIEEGEEVFY QLEGDMVLRV LEQGKHRDVV IRQGEIFLLP ARVPHSPQRF ANTVGLVVER RRLETELDGL RYYVGDTMDV LFEKWFYCKD LGTQLAPIIQ EFFSSEQYRT GKPIPDQLLK EPPFPLSTRS IMEPMSLDAW LDSHHRELQA GTPLSLFGDT YETQVIAYGQ GSSEGLRQNV DVWLWQLEGS SVVTMGGRRL SLAPDDSLLV LAGTSYAWER TQGSVALSVT QDPACKKPLG.
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 :
Epoetin Fc HumanDescription:
Erythropoietin-Alpha Fc-Chimera Human Recombinant
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
Product # :
CYT-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Erythropoietin-alpha Fc-Chimera Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.
Source
Chinese Hamster Ovary Cells(CHO).
Formulation
Each mg of lyophilized powder contains 1x PBS pH-7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.More Info
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Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
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Synonyms
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Erythropoietin-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha 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 Erythropoietin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 140kDa.
What is the source or expression system of EPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).
What is the Purity of EPOETIN Protein?
EPOETIN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EPOETIN Protein?
The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.
What applications can EPOETIN Protein be used in?
EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPOETIN Protein?
The endotoxin level is minimal, EPOETIN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CTH HumanDescription:
Cystathionase Human Recombinant
Cystathionine gamma-lyase, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH.
Product # :
ENZ-212Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CTH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-405) and having a molecular mass of 46.7kDa.CTH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTH solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Cystathionine gamma-lyase or cystathionase (CTH) is a member of the trans-sulfuration enzymes family. CTH is an enzyme which breaks down cystathionine into cysteine and alpha-ketobutyrate. The CTH catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Glutathione synthesis in the liver is dependent upon the availability of cysteine. Mutations in the CTH gene cause cystathioninuria.
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Synonyms
Cystathionine gamma-lyase, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG APGQHSGFEY SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY FRQVASEFGL KISFVDCSKI KLLEAAITPE TKLVWIETPT NPTQKVIDIE GCAHIVHKHG DIILVVDNTF MSPYFQRPLA LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ NSLGAVPSPI DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL PAIMTHASVL KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP SGSHS.
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 :
AMMECR1L HumanDescription:
AMMECR1-Like Human Recombinant
AMMECR1-like protein, AMMECR1L, AMMECR1-Like.
Product # :
PRO-2077Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AMMECR1L Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 333 amino acids (1-310) and having a molecular mass of 36.9 kDa.AMMECR1L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The AMMECR1L solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
AMMECR1-Like, also known as AMMECR1L, is a Protein Coding gene which contains one AMMECR1 domain.
-
Synonyms
AMMECR1-like protein, AMMECR1L, AMMECR1-Like.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGKRRCV PPLEPKLAAG CCGVKKPKLS GSGTHSHGNQ STTVPGSSSG PLQNHQHVDS SSGRENVSDL TLGPGNSPIT RMNPASGALS PLPRPNGTAN TTKNLVVTAE MCCYCFDVLY CHLYGFPQPR LPRFTNDPYP LFVTWKTGRD KRLRGCIGTF SAMNLHSGLR EYTLTSALKD SRFPPLTREE LPKLFCSVSL LTNFEDASDY LDWEVGVHGI RIEFINEKGV KRTATYLPEV AKEQDWDQIQ TIDSLLRKGG FKAPITSEFR KTIKLTRYRS EKVTISYAEY IASRQHCFQN GTLHAPPLYN HYS.
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 :
SOD2 HumanDescription:
Superoxide Dismutase-2 Human Recombinant
MNSOD, MVCD6, IPOB, Mn superoxide dismutase, EC=1.15.1.1.
Product # :
PRO-819Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SOD2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 219 amino acids (25-222 a.a.) and having a molecular mass of 24.4kDa. SOD2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
SOD2 Human solution containing 20mM Tris-HCl pH-8 & 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,200 units/mg, in which one unit will inhibit the rate of reduction of cytochrome c by 50% in a coupled system, using xanthine and Xanthine oxidase at pH 7.8 at 25C in a 1.5 ml reaction volume.More Info
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Introduction
SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in SOD2 gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. SOD2 destroys radicals which are usually produced within the cells and which are toxic to biological systems.
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Synonyms
MNSOD, MVCD6, IPOB, Mn superoxide dismutase, EC=1.15.1.1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKHSLPDLPY DYGALEPHIN AQIMQLHHSK HHAAYVNNLN VTEEKYQEAL AKGDVTAQIA LQPALKFNGG GHINHSIFWT NLSPNGGGEP KGELLEAIKR DFGSFDKFKE KLTAASVGVQ GSGWGWLGFN KERGHLQIAA CPNQDPLQGT TGLIPLLGID VWEHAYYLQY KNVRPDYLKA IWNVINWENV TERYMACKK.
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 :
PNPO HumanDescription:
Pyridoxamine 5'-Phosphate Oxidase Human Recombinant
Pyridoxine-5'-phosphate oxidase, Pyridoxamine-phosphate oxidase, PNPO, PDXPO, FLJ10535.
Product # :
ENZ-030Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PNPO Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (57-261 a.a.) and having a molecular mass of 25.9kDa. The PNPO is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PNPO solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Pyridoxine-5'-phosphate oxidase (PNPO) is the rate-limiting enzyme in vitamin B6 synthesis. Vitamin B6 (Pyridoxal 5-prime-phosphate or PLP) is vital for normal cellular function, and some cancer cells have notable differences in vitamin B6 metabolism compared to their normal counterparts.Vitamin B6 is an essential co-factor for enzymes involved in both homocysteine metabolism and synthesis of neurotransmitters such as catecholamine. Mutations in the PNPO gene result in PNPO deficiency, a form of neonatal epileptic encephalopathy.
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Synonyms
Pyridoxine-5'-phosphate oxidase, Pyridoxamine-phosphate oxidase, PNPO, PDXPO, FLJ10535.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDPVKQFAAW FEEAVQCPDI GEANAMCLAT CTRDGKPSAR MLLLKGFGKD GFRFFTNFES RKGKELDSNP FASLVFYWEP LNRQVRVEGP VKKLPEEEAE CYFHSRPKSS QIGAVVSHQS SVIPDREYLR KKNEELEQLY QDQEVPKPKS WGGYVLYPQV MEFWQGQTNR LHDRIVFRRG LPTGDSPLGP MTHRGEEDWL YERLAP.
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 :
ldhA E. coliDescription:
Fermentative D-lactate Dehydrogenase, NAD-Dependent E.Coli Recombinant
D-lactate dehydrogenase, D-LDH, Fermentative lactate dehydrogenase, ldhA, hslI, htpH, b1380, JW1375.
Product # :
ENZ-632Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ldhA E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 39.1kDa.ldhA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ldhA solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol and 100mM NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
D-lactate dehydrogenase (ldha) is a member of the D-isomer specific 2-hydroxyacid dehydrogenase family. In enzymology, an ldha (cytochrome) is an enzyme which catalyzes the chemical reaction. Therefore, the 2 substrates of the ldha enzyme are (D)-lactate and ferricytochrome c, whereas its 2 products are pyruvate and ferrocytochrome c.
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Synonyms
D-lactate dehydrogenase, D-LDH, Fermentative lactate dehydrogenase, ldhA, hslI, htpH, b1380, JW1375.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKLAVY STKQYDKKYL QQVNESFGFE LEFFDFLLTE KTAKTANGCE AVCIFVNDDG SRPVLEELKK HGVKYIALRC AGFNNVDLDA AKELGLKVVR VPAYDPEAVA EHAIGMMMTL NRRIHRAYQR TRDANFSLEG LTGFTMYGKT AGVIGTGKIG VAMLRILKGF GMRLLAFDPY PSAAALELGV EYVDLPTLFS ESDVISLHCP LTPENYHLLN EAAFEQMKNG VMIVNTSRGA LIDSQAAIEA LKNQKIGSLG MDVYENERDL FFEDKSNDVI QDDVFRRLSA CHNVLFTGHQ AFLTAEALTS ISQTTLQNLS NLEKGETCPN ELV.
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 :
CDK5 HumanDescription:
Cyclin-dependent Kinase 5 Human Recombinant
Cyclin-dependent kinase 5, Cell division protein kinase 5, Serine/threonine-protein kinase PSSALRE, Tau protein kinase II catalytic subunit, CDK5, CDKN5, TPKII catalytic subunit, cyclin dependent kinase 5.
Product # :
PKA-047Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDK5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-292) and having a molecular mass of 35.8kDa. CDK5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDK5 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Cell division protein kinase 5 (CDK5) belongs to the cyclin-dependent kinase family. CDK5 is essential for appropriate development of the brain and in order to be activated CDK5 must link to CDK5R1 or CDK5R2. CDK5 doesn't need phosphorylation on the T loop so that binding with the activator is enough to activate the kinase. CDK5 is engaged in the processes of neuronal maturation and migration, phosphorylating the central intracellular adaptor of the reeling signaling chain.
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Synonyms
Cyclin-dependent kinase 5, Cell division protein kinase 5, Serine/threonine-protein kinase PSSALRE, Tau protein kinase II catalytic subunit, CDK5, CDKN5, TPKII catalytic subunit, cyclin dependent kinase 5.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMQKYEK LEKIGEGTYG TVFKAKNRET HEIVALKRVR LDDDDEGVPS SALREICLLK ELKHKNIVRL HDVLHSDKKL TLVFEFCDQD LKKYFDSCNG DLDPEIVKSF LFQLLKGLGF CHSRNVLHRD LKPQNLLINR NGELKLADFG LARAFGIPVR CYSAEVVTLW YRPPDVLFGA KLYSTSIDMW SAGCIFAELA NAGRPLFPGN DVDDQLKRIF RLLGTPTEEQ WPSMTKLPDY KPYPMYPATT SLVNVVPKLN ATGRDLLQNL LKCNPVQRIS AEEALQHPYF SDFCPP.
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 :
CEBP Gamma HumanDescription:
CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
Product # :
PRO-434Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.
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Synonyms
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.
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 :
GRHPR HumanDescription:
Glyoxylate Reductase/Hydroxypyruvate Reductase Human Recombinant
EC 1.1.1.79, GLXR, GLYD, GRHPR, PH2.
Product # :
ENZ-521Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
GRHPR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-328 a.a.) and having a molecular mass of 37.8 kDa. The GRHPR is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GRHPR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 5mM DTT and 0.2M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GRHPR located in the cytosol, belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family of proteins. GRHPR is widely expressed in liver. GRHPR has widespread tissue expression and is involved in metabolism. GRHPR is an enzyme with hydroxypyruvate reductase, glyoxylate reductase, and D-glycerate dehydrogenase enzymatic activities.
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Synonyms
EC 1.1.1.79, GLXR, GLYD, GRHPR, PH2.
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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 MRPVRLMKVF VTRRIPAEGR VALARAADCE VEQWDSDEPI PAKELERGVA GAHGLLCLLS DHVDKRILDA AGANLKVIST MSVGIDHLAL DEIKKRGIRV GYTPDVLTDT TAELAVSLLL TTCRRLPEAI EEVKNGGWTS WKPLWLCGYG LTQSTVGIIG LGRIGQAIAR RLKPFGVQRF LYTGRQPRPE EAAEFQAEFV STPELAAQSD FIVVACSLTP ATEGLCNKDF FQKMKETAVF INISRGDVVN QDDLYQALAS GKIAAAGLDV TSPEPLPTNH PLLTLKNCVI LPHIGSATHR TRNTMSLLAA NNLLAGLRGE PMPSELKL.
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 :
CCL22 MouseDescription:
Macrophage-Derived Chemokine Mouse Recombinant (CCL22)
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.
Product # :
CHM-370Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CCL22 Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.8kDa. The Mouse CCL22 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCL22 filtered (0.2µm) and lyophilized from a concentrated solution containing 20mM phosphate buffer & 150mM NaCl pH-7.4.
Purity
Greater than 97.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
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Introduction
MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4. CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph
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Synonyms
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL22 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 CCL22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
GPYGANVEDS ICCQDYIRHP LPSRLVKEFF WTSKSCRKPG VVLITVKNRD ICADPRQVWV KKLLHKLS.
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Background
What is the molecular weight/Mw of CCL22 MOUSE Protein?
CCL22 MOUSE Protein has a total Mw of 7.8kDa.
What is the source or expression system of CCL22 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL22 MOUSE Protein?
CCL22 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL22 MOUSE Protein?
Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL22 MOUSE Protein?
GPYGANVEDS ICCQDYIRHP LPSRLVKEFF WTSKSCRKPG VVLITVKNRD ICADPRQVWV KKLLHKLS.
What applications can CCL22 MOUSE Protein be used in?
CCL22 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL22 MOUSE Protein?
The endotoxin level is minimal, CCL22 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NKp46 AntibodyDescription:
Natural Cytotoxicity Receptor NKp46, Mouse Anti Human
Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.
Product # :
ANT-303Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
A natural cytotoxicity receptor (NCR) NKp46 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. The three known NCRs include NKp46 and NKp30, which are expressed on circulating NKcells, and NKp44, which is expressed only on activating NK cells. NKp46 has been implicated in NK cell-mediated lysis of several autologous tumor cells, pathogen-infected cell lines and mononuclear phagocytes infected with an intracellular bacterium. The Lysis of tumor cells by NK-cells involves recognition by NKp46 of heparan sulfate moieties of membrane heparan sulfate proteoglycans. Furthermore, NKp46 is a surface receptor involved in NK-cell cell death by apoptosis. NKp46 has two extracellular Ig-like domains followed by a ~40 residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. The extracellular Ig-like domain of NKp46 (22-255aa) is purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. In addition, engagement of the antigen with the monoclonal antibody stimulates intracellular calcium levels and the synthesis of cytokines. CD59 is an NKp46 coreceptor (by physical association) together they activate cytotoxicity of human NK-cells, their engagement results in tyrosine phosphorylation of CD3-zeta chains associated with NKp46. Reduced cell surface expression of NKp46 and other NK-cell receptors is linked to the impaired NK-cell cytolytic function in viremic HIV-1 infection.
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Synonyms
Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.
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Physical Appearance
Sterile Filtered colorless solution.
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Immunogen
Anti-human NKp46 mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human NKp46 amino acids 22-255 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
Pn1D9AT.
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Applications
NKp46 antibody has been tested by immunofluorescent staining with flow cytometric analysis and by Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
NKp46 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CCL20 Human, HisDescription:
Macrophage Inflammatory protein-3 alpha (CCL20) Human Recombinant, His Tag
S Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20.
Product # :
CHM-252Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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- purity
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Description
MIP 3a Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 91 amino acids (27-96 a.a.) and having a molecular mass of 10.3kDa. The MIP 3a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MIP 3a solution (0.25 mg/ml) contains Phosphate Buffered Saline pH7.4 and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CCL-20 is a chemotactic factor that draws lymphocytes & neutrophils, rathar than monocytes. MIP-3 alpha inhibits proliferation of myeloid progenitors in colony formation assays. MIP3A plays a role in the formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. CCL-20 holdes antibacterial activity e.coli atcc 25922 and s.aureus atcc 29213. CCL-20 gene transcription is activated by H. pylori, which activates NF-kappaB through intracellular signal pathway which involves IkappaB kinase and NF-kappaB-inducing kinase. MIP-3 alpha is invloved in chemokine-mediated lymphocyte trafficking during gastric inflammation in Helicobacter infection. CCL-20 expression is involved in the recruitment of CD45R0-positive T cell subsets into the intestinal lamina propria. MIP-3A is in charge of the advancement of pulpal inflammation through the recruitment of C-C motif Receptor 6-expressing lymphocytes Vaginal epithelial cells respond to factors present in semen by secreting MIP-3 alpha, which increases langerhans cells recruitment during HIV transmission.
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Synonyms
S Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20.
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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 MASNFDCCLG YTDRILHPKF IVGFTRQLAN EGCDINAIIF HTKKKLSVCA NPKQTWVKYI VRLLSKKVKN M.
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Background
What is the molecular weight/Mw of CCL20 HUMAN, HIS Protein?
CCL20 HUMAN, HIS Protein has a total Mw of 10.3kDa.
What is the source or expression system of CCL20 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL20 HUMAN, HIS Protein?
CCL20 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL20 HUMAN, HIS Protein?
The biological functionality of CCL20 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL20 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MASNFDCCLG YTDRILHPKF IVGFTRQLAN EGCDINAIIF HTKKKLSVCA NPKQTWVKYI VRLLSKKVKN M.
What applications can CCL20 HUMAN, HIS Protein be used in?
CCL20 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL20 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL20 HUMAN, HIS 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.