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1000 results found for “Syntaxin”
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Name :
SDF 1b HumanDescription:
Stromal Cell Derived Factor-1 Beta Human Recombinant (CXCL12)
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b.
Product # :
CHM-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stromal Cell-Derived Factor-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8508 Dalton. The SDF-1b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CXCL12 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by its ability to chemoattract human peripheral T cells activated with PHA and IL-2 using a concentation of 20-80ng/ml corresponding to a Specific Activity of 12,500-50,000IU/mg.More Info
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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 Stromal Cell-Derived Factor-1b 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 Lys-Pro-Val-Ser-Leu.
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Protein content
Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 1.06 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of SDF-1b as a Reference Standard.
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 :
BD 1 RatDescription:
Beta Defensin -1 Rat Recombinant
Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.
Product # :
CYT-062Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BD-1 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4.1kDa.The BD-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BD-1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.More Info
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Introduction
The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
Beta Defensin is highly expressed by epithelial cells.
Beta-defensin 1 may play a role in the pathogenesis of severe sepsis. -
Synonyms
Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BD-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 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 BD-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.
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Background
What is the molecular weight/Mw of BD1 Protein?
BD1 Protein has a total Mw of 4.1kDa.
What is the source or expression system of BD1 Protein?
Escherichia Coli.
What is the Purity of BD1 Protein?
BD1 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BD1 Protein?
Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.
What is the amino acid sequence of BD1 Protein?
DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.
What applications can BD1 Protein be used in?
BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD1 Protein?
The endotoxin level is minimal, BD1 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 :
BD 4 RatDescription:
BD 4 Rat
Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.
Product # :
CYT-066Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BD-4 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.4kDa.The BD-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BD-4 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.More Info
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Introduction
Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues. -
Synonyms
Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BD-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-4 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 BD-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.
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Background
What is the molecular weight/Mw of BD4 Protein?
BD4 Protein has a total Mw of 4.4kDa.
What is the source or expression system of BD4 Protein?
Escherichia Coli.
What is the Purity of BD4 Protein?
BD4 Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BD4 Protein?
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.
What is the amino acid sequence of BD4 Protein?
QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.
What applications can BD4 Protein be used in?
BD4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD4 Protein?
The endotoxin level is minimal, BD4 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 :
TACI Human, HisDescription:
Tumor Necrosis Factor Receptor 13B Human Recombinant, His Tag
CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.
Product # :
CYT-032Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TACI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids (1- 165a.a.) and having a molecular mass of 20.9kDa. The TACI is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TACI solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
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Synonyms
CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.
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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 MGSMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYS.
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 :
KRAS 2A HumanDescription:
Kirsten Rat Sarcoma Viral Oncogene, Isoform 2A Human Recombinant
GTPase KRas, K-Ras 2, Ki-Ras, c-K-ras, c-Ki-ras, KRAS, KRAS2, RASK2, C-K-RAS, CFC2, K-RAS2A, K-RAS2B, K-RAS4A, K-RAS4B, KI-RAS, KRAS1, NS, NS3, Kirsten rat sarcoma viral oncogene homolog.
Product # :
PRO-1446Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KRAS 2A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-186 a.a) and having a molecular mass of 23.8kDa.KRAS 2A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KRAS 2A protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Kirsten Rat Sarcoma Viral Oncogene, Isoform 2A (KRAS-2A) belongs to the small GTPase superfamily. The KRAS-2A protein is involved in a variety of malignancies, including lung adenocarcinoma, mucinous adenoma, ductal carcinoma of the pancreas and colorectal carcinoma. Ras family members impact cell growth and differentiation events in a subcellular membrane compartmentalization-based signaling system under normal conditions. Oncogenic Ras can deregulate processes which control both cell proliferation and apoptosis.
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Synonyms
GTPase KRas, K-Ras 2, Ki-Ras, c-K-ras, c-Ki-ras, KRAS, KRAS2, RASK2, C-K-RAS, CFC2, K-RAS2A, K-RAS2B, K-RAS4A, K-RAS4B, KI-RAS, KRAS1, NS, NS3, Kirsten rat sarcoma viral oncogene homolog.
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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 MGSHMTEYKL VVVGAGGVGK SALTIQLIQN HFVDEYDPTI EDSYRKQVVI DGETCLLDIL DTAGQEEYSA MRDQYMRTGE GFLCVFAINN TKSFEDIHHY REQIKRVKDS EDVPMVLVGN KCDLPSRTVD TKQAQDLARS YGIPFIETSA KTRQRVEDAF YTLVREIRQY RLKKISKEEK TPGCVKIKKC.
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 :
PRDX2 HumanDescription:
Peroxiredoxin-2 Human Recombinant
PRP, TSA, PRX2, NKEFB, PRXII, TDPX1, MGC4104, PRDX2, Peroxiredoxin-2, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Natural killer cell-enhancing factor B, NKEF-B.
Product # :
ENZ-414Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PRDX2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids and having a molecular mass of 21.8 kDa.The PRDX2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Peroxiredoxin solution contains 20mM Tris-HCl pH-8, & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The specific activity is > 2000 pmole/min/µg. Enzymatic activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25°C for 1 minute.
More Info
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Introduction
PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer. -
Synonyms
PRP, TSA, PRX2, NKEFB, PRXII, TDPX1, MGC4104, PRDX2, Peroxiredoxin-2, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Natural killer cell-enhancing factor B, NKEF-B.
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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
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN.
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 :
Leptin tA Mouse, PEGDescription:
Leptin Antagonist Triple Mutant Pegylated Mouse Recombinant
Product # :
CYT-566Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Mouse Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Leptin Antagonist Triple Mutant Mouse Recombinant half-life in circulation after SC injection was over 20 hours.
Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Mouse Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
a-ActininDescription:
Actinin Alpha
Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.
Product # :
PRO-518Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ultra pure Alpha Actinin having a Molecular mass of 95,000 Dalton.
Source
Chicken Gizzard.
Formulation
The protein was lyophilized from a 1mg/ml solution containing 10mM Tris acetate buffer pH 7.6, 0.1mM EDTA, 2mM DTT, and 20mM NaCl.
Purity
Greater than 95.0% as determined by analysis 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
Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized a-Actinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution a-Actinin 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 a-Actinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Protein standard in 1D and 2D SDS gelelectrophoresis
Immunoassays
Immunization.
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 :
CSNK1D HumanDescription:
Casein Kinase 1 Delta Human Recombinant
Casein kinase I isoform delta, CKI-delta, CKId, Tau-protein kinase CSNK1D, CSNK1D, HCKID, delta isoform 2, Casein Kinase 1 Delta, Casein kinase 1.
Product # :
PKA-306Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CSNK1D Human Recombinant produced in E. coli is a single polypeptide chain containing 429 amino acids (1-409) and having a molecular mass of 48.9kDa.CSNK1D is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CSNK1D solution (1mg/ml) contains 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
Casein kinase I gene family members take part in the control of cytoplasmic and nuclear processes, including DNA replication and repair. Casein Kinase 1 Delta (CSNK1D) is a member of the casein kinase I (CKI) gene family. CSNK1D is a vital serine/threonine-protein kinase which regulates diverse cellular growth and survival processes including Wnt signaling and circadian rhythms. CSNK1D phosphorylates a great amount of proteins.
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Synonyms
Casein kinase I isoform delta, CKI-delta, CKId, Tau-protein kinase CSNK1D, CSNK1D, HCKID, delta isoform 2, Casein Kinase 1 Delta, Casein kinase 1.
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Physical Appearance
CSNK1D is supplied as a 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 MELRVGNRYR LGRKIGSGSF GDIYLGTDIA AGEEVAIKLE CVKTKHPQLH IESKIYKMMQ GGVGIPTIRW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL CKGYPSEFAT YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGASRA ADDAERERRD REERLRHSRN PATRGLPSTA SGRLRGTQEV APPTPLTPTS HTANTSPRPV SGMERERKVS MRLHRGAPVN ISSSDLTGRQ DTSRMSTSQN SIPFEHHGK.
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 :
MTPN HumanDescription:
Myotrophin Human Recombinant
Protein V-1, GCDP, Myotrophin, FLJ31098, FLJ99857.
Product # :
CYT-723Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MTPN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-118 a.a.) and having a molecular mass of 15 kDa. The MTPN is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MTPN Human solution containing 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MTPN is an ankyrin repeat protein, that stimulates protein synthesis and cardiomyocyte growth to commence cardiac hypertrophy by activating the NF-kappaB signaling cascade. Myotrophin participates in cerebellar morphogenesis and takes part in differentiation of cerebellar neurons, particularly of granule cells. High levels of MTPN are expressed in human dilated cardiomyopathic and ischemic hearts.
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Synonyms
Protein V-1, GCDP, Myotrophin, FLJ31098, FLJ99857.
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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 MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ.
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 :
NAA10 HumanDescription:
N Alpha-Acetyltransferase 10, NatA Catalytic Subunit Human Recombinant
N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.
Product # :
ENZ-158Price :
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Description
NAA10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (1-235 a.a.) and having a molecular mass of 28.6kDa (the molecular weight on SDS-PAGE will appear higher).NAA10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAA10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NAA10 is a member of the acetyltransferase family. NAA10 interacts with NAA15, HIF-1 and with the ribosome. In its binding to HIF-1, NAA10 functions as a protein acetyltransferase by regulating its stability. In various cell lines, NAA10 is downregulated in response to hypoxia. NAA10 is expressed during the course of the development of the brain.
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Synonyms
N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.
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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 MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGAIENKV ESKGNSPPSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DYNLRB2 HumanDescription:
Dynein Light Chain Roadblock-Type 2 Human Recombinant
Dynein light chain roadblock-type 2, Dynein light chain 2B cytoplasmic, Roadblock domain-containing protein 2, DYNLRB2, DNCL2B, DNLC2B, ROBLD2, MGC62033.
Product # :
PRO-174Price :
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Description
DYNLRB2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids (1-96 a.a.) and having a molecular mass of 13kDa. The DYNLRB2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DYNLRB2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Dynein light chain roadblock-type 2 (DYNLRB2) functions as one of several non-catalytic accessory components of the cytoplasmic dynein complex which are considered to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein functions as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.
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Synonyms
Dynein light chain roadblock-type 2, Dynein light chain 2B cytoplasmic, Roadblock domain-containing protein 2, DYNLRB2, DNCL2B, DNLC2B, ROBLD2, MGC62033.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEVEETLKR IQSHKGVIGT MVVNAEGIPI RTTLDNSTTV QYAGLLHHLT MKAKSTVRDI DPQNDLTFLR IRSKKHEIMV APDKEYLLIV IQNPCE.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ASMT HumanDescription:
Acetylserotonin O-Methyltransferase Human Recombinant
HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.
Product # :
ENZ-664Price :
Quantity :
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Description
ASMT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298 a.a) and having a molecular mass of 35.3kDa.ASMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ASMT solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) , 1M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ASMT is a member of the methyltransferase superfamily. ASMT participates in melatonin biosynthesis. ASMT Expressed in brain, retina and pineal gland, ASMT utilities to catalyze the final reaction in the synthesis of melatonin, particularly the conversion of S-adenosyl-L-methionine and N-acetylserotonin to S-adenosyl-Lhomocysteine and melatonin.
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Synonyms
HIOMT, HIOMTY, Acetylserotonin O-methyltransferase , Hydroxyindole O-methyltransferase , ASMT.
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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 MGSSEDQAYR LLNDYANGFM VSQVLFAACE LGVFDLLAEA PGPLDVAAVA AGVRASAHGT ELLLDICVSL KLLKVETRGG KAFYRNTELS SDYLTTVSPT SQCSMLKYMG RTSYRCWGHL ADAVREGRNQ YLETFGVPAE ELFTAIYRSE GERLQFMQAL QEVWSVNGRS VLTAFDLSVF PLMCDLGGDF FKDPLPEADL YILARVLHDW ADGKCSHLLE RIYHTCKPGG GILVIESLLD EDRRGPLLTQ LYSLNMLVQT EGQERTPTHY HMLLSSAGFR DFQFKKTGAI YDAILARK
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 :
BABAM1 HumanDescription:
BRISC And BRCA1 A Complex Member 1 Human Recombinant
BRISC and BRCA1-A complex member 1, Mediator of RAP80 interactions and targeting subunit of 40 kDa, New component of the BRCA1-A complex, BABAM1, C19orf62, MERIT40, NBA1, HSPC142, BRISC And BRCA1 A Complex Member 1.
Product # :
PRO-2057Price :
Quantity :
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Description
BABAM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329 a.a.) and having a molecular mass of 38.9kDa.BABAM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BABAM1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
BRISC And BRCA1 A Complex Member 1, also known as BABAM1, is a part of the BRCA1-A complex. The BRCA1-A complex identifies 'Lys-63'- linked ubiquitinated histones H2A and H2AX at DNA lesions sites and also holds deubiquitinase activity which removes in particular 'Lys-63'-linked ubiquitin on histones H2A and H2AX. BABAM1 is necessary to preserve the stability of BRE/BRCC45 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component.
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Synonyms
BRISC and BRCA1-A complex member 1, Mediator of RAP80 interactions and targeting subunit of 40 kDa, New component of the BRCA1-A complex, BABAM1, C19orf62, MERIT40, NBA1, HSPC142, BRISC And BRCA1 A Complex Member 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEVAEPS SPTEEEEEEE EHSAEPRPRT RSNPEGAEDR AVGAQASVGS RSEGEGEAAS ADDGSLNTSG AGPKSWQVPP PAPEVQIRTP RVNCPEKVII CLDLSEEMSL PKLESFNGSK TNALNVSQKM IEMFVRTKHK IDKSHEFALV VVNDDTAWLS GLTSDPRELC SCLYDLETAS CSTFNLEGLF SLIQQKTELP VTENVQTIPP PYVVRTILVY SRPPCQPQFS LTEPMKKMFQ CPYFFFDVVY IHNGTEEKEE EMSWKDMFAF MGSLDTKGTS YKYEVALAGP ALELHNCMAK LLAHPLQRPC QSHASYSLLE EEDEAIEVEA TV.
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 (37-159), HisDescription:
Streptavidin (37-159 a.a) Recombinant, His Tag
Product # :
PRO-1495Price :
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Description
Streptavidin Recombinant produced in E. coli is a single polypeptide chain containing 148 amino acids (37-159) and having a molecular mass of 15.6kDa. Streptavidin is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The Streptavidin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.
Purity
Greater than 90% 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 widely 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 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 MGSHMAEAGI TGTWYNQLGS TFIVTAGADG ALTGTYESAV GNAESRYVLT GRYDSAPATD GSGTALGWTV AWKNNYRNAH SATTWSGQYV GGAEARINTQ WLLTSGTTEA NAWKSTLVGH DTFTKVKP.
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 :
FBXO6 HumanDescription:
F-Box Protein 6 Human Recombinant
FBG2, FBS2, FBX6, Fbx6b, F-box only protein 6, F-box protein that recognizes sugar chains 2, F-box/G-domain protein 2, FBXO6.
Product # :
PRO-1522Price :
Quantity :
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Description
FBXO6 Human Recombinant produced in E. coli is a single polypeptide chain containing 316 amino acids (1-293) and having a molecular mass of 36.3kDa. FBXO6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FBXO6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
F-Box Protein 6, also known as FBXO6, is a part of the F-box protein family which is characterized by a roughly forty amino acid motif, the F-box. The F-box proteins are one of the 4 subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box) that operates in phosphorylation-dependent ubiquitination. The F-box proteins are divided into three categories: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing different protein-protein interaction modules or no recognizable motifs. FBXO6 is a part of the Fbxs category, and its C-terminal area is very similar to that of rat NFB42 (neural F Box 42 kDa) which is involved in the control of the cell cycle.
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Synonyms
FBG2, FBS2, FBX6, Fbx6b, F-box only protein 6, F-box protein that recognizes sugar chains 2, F-box/G-domain protein 2, FBXO6.
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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 MGSMDAPHSK AALDSINELP ENILLELFTH VPARQLLLNC RLVCSLWRDL IDLMTLWKRK CLREGFITKD WDQPVADWKI FYFLRSLHRN LLRNPCAEED MFAWQIDFNG GDRWKVESLP GAHGTDFPDP KVKKYFVTSY EMCLKSQLVD LVAEGYWEEL
LDTFRPDIVV KDWFAARADC GCTYQLKVQL ASADYFVLAS FEPPPVTIQQ WNNATWTEVS YTFSDYPRGV RYILFQHGGR DTQYWAGWYG PRVTNSSIVV SPKMTRNQAS SEAQPGQKHG QEEAAQSPYR AVVQIF.
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 :
CCDC104 HumanDescription:
Coiled-Coil Domain Containing 104 Human Recombinant
Coiled-Coil Domain Containing 104, Coiled-CoilDomain- Protein104, CCDC104.
Product # :
PRO-1728Price :
Quantity :
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Description
CCDC104 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 365 amino acids (1-342 a.a) and having a molecular mass of 41.8kDa.CCDC104 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCDC104 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CCDC104 also known as coiled-coil domain-containing protein 104 is a 342 amino acid protein that exists as two alternatively spliced isoforms. CCDC104 undergoes post-translational phosphorylation following DNA damage, most likely by either ATR or ATM. Among the diseases associated with CCDC104 are pancreatic cancer, and pancreatitis.
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Synonyms
Coiled-Coil Domain Containing 104, Coiled-CoilDomain- Protein104, CCDC104.
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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 MGSMAAEEED EVEWVVESIA GFLRGPDWSI PILDFVEQKC EVFDDEEESK LTYTEIHQEY KELVEKLLEG YLKEIGINED QFQEACTSPL AKTHTSQAIL QPVLAAEDFT IFKAMMVQKN IEMQLQAIRI IQERNGVLPD CLTDGSDVVS DLEHEEMKIL REVLRKSKEE YDQEEERKRK KQLSEAKTEE PTVHSSEAAI MNNSQGDGEH FAHPPSEVKM HFANQSIEPL GRKVERSETS SLPQKDLKIP GLEHASIEGP IANLSVLGTE ELRQREHYLK QKRDKLMSMR KDMRTKQIQN MEQKGKPTGE VEEMTEKPEM TAEEKQTLLK RRLLAEKLKE EVINK
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 :
CCNA2 HumanDescription:
Cyclin-A2 Human Recombinant
Cyclin-A2, Cyclin-A, CCNA2, CCN1, CCNA.
Product # :
PKA-033Price :
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Description
CCNA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 456 amino acids (1-432 a.a) and having a molecular mass of 51.1kDa.CCNA2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCNA2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CCNA2 is a member of the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. Various cyclins demonstrate distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. Contrary to cyclin A1, which is present only in germ cells, CCNA2 is expressed in all tissues tested. CCNA2 binds and activates CDC2 or CDK2 kinases, and consequently promotes both cell cycle G1/S and G2/M transitions.
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Synonyms
Cyclin-A2, Cyclin-A, CCNA2, CCN1, CCNA.
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Physical Appearance
Sterile Filtered clear 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 MGSHMLGNSA PGPATREAGS ALLALQQTAL QEDQENINPE KAAPVQQPRT RAALAVLKSG NPRGLAQQQR PKTRRVAPLK DLPVNDEHVT VPPWKANSKQ PAFTIHVDEA EKEAQKKPAE SQKIEREDAL AFNSAISLPG PRKPLVPLDY PMDGSFESPH
TMDMSIVLED EKPVSVNEVP DYHEDIHTYL REMEVKCKPK VGYMKKQPDI TNSMRAILVD WLVEVGEEYK LQNETLHLAV NYIDRFLSSM SVLRGKLQLV GTAAMLLASK FEEIYPPEVA EFVYITDDTY TKKQVLRMEH LVLKVLTFDL AAPTVNQFLT QYFLHQQPAN CKVESLAMFL
GELSLIDADP YLKYLPSVIA GAAFHLALYT VTGQSWPESL IRKTGYTLES LKPCLMDLHQ TYLKAPQHAQ QSIREKYKNS KYHGVSLLNP PETLNL.
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 :
FURIN HumanDescription:
Furin Human Recombinant
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
Product # :
PRO-2199Price :
Quantity :
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Description
FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FURIN protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.
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Synonyms
Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.
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 :
KRT8 Human, HisDescription:
Cytokeratin 8 Human Recombinant, His Tag
Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.
Product # :
PRO-1567Price :
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Description
KRT8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 506 amino acids (1-483 a.a) and having a molecular mass of 56kDa. KRT8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KRT8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytokeratin 8 (KRT8) belongs to the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. KRT8 typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. KRT8 has a role in retaining cellular structural integrity and also functions in signal transduction and cellular differentiation. KRT8 gene mutations cause cryptogenic cirrhosis.
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Synonyms
Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.
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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 MGSMSIRVTQ KSYKVSTSGP RAFSSRSYTS GPGSRISSSS FSRVGSSNFR GGLGGGYGGA SGMGGITAVT VNQSLLSPLV LEVDPNIQAV RTQEKEQIKT LNNKFASFID KVRFLEQQNK MLETKWSLLQ QQKTARSNMD NMFESYINNL RRQLETLGQE KLKLEAELGN MQGLVEDFKN KYEDEINKRT EMENEFVLIK KDVDEAYMNK VELESRLEGL TDEINFLRQL YEEEIRELQS QISDTSVVLS MDNSRSLDMD SIIAEVKAQY EDIANRSRAE AESMYQIKYE ELQSLAGKHG DDLRRTKTEI SEMNRNISRL QAEIEGLKGQ RASLEAAIAD AEQRGELAIK DANAKLSELE AALQRAKQDM ARQLREYQEL MNVKLALDIE IATYRKLLEG EESRLESGMQ NMSIHTKTTS GYAGGLSSAY GGLTSPGLSY SLGSSFGSGA GSSSFSRTSS SRAVVVKKIE TRDGKLVSES SDVLPK.
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 :
PRDX2 RatDescription:
Peroxiredoxin-2 Rat Recombinant
Peroxiredoxin-2, Prdx2, Prdx, Thiol-specific antioxidant protein, TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1.
Product # :
ENZ-910Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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- formulation
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Description
PRDX2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-198 a.a) and having a molecular mass of 24.3kDa. PRDX2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PRDX2 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer. -
Synonyms
Peroxiredoxin-2, Prdx2, Prdx, Thiol-specific antioxidant protein, TSA, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 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 MGSHMASGNA HIGKPAPDFT GTAVVDGAFK EIKLSDYRGK YVVLFFYPLD FTFVCPTEII AFSDHAEDFR KLGCEVLGVS VDSQFTHLAW INTPRKEGGL GPLNIPLLAD VTKSLSQNYG VLKNDEGIAY RGLFIIDAKG VLRQITVNDL PVGRSVDEAL RLVQAFQYTD EHGEVCPAGW KPGSDTIKPN VDDSKEYFSK HN.
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 :
GIMAP6 HumanDescription:
GTPase, IMAP Family Member 6 Human Recombinant
GTPase IMAP Family Member 6, Immune Associated Nucleotide 2, Immune Associated Nucleotide 6, IAN6, IAN2, hIAN2, hIAN6.
Product # :
PRO-1628Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
GIMAP6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-292) and having a molecular mass of 35.0kDa.GIMAP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GIMAP6 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
GIMAP6 is a member of the GTPases of immunity-associated proteins (GIMAP) family. GIMAP proteins contain GTP-binding and coiled-coil motifs, and may play roles in the regulation of cell survival. Decreased expression of this gene may play a role in non-small cell lung cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, which is found in a cluster with seven additional GIMAP genes on the long arm of chromosome 7.
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Synonyms
GTPase IMAP Family Member 6, Immune Associated Nucleotide 2, Immune Associated Nucleotide 6, IAN6, IAN2, hIAN2, hIAN6.
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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 MGSMEEEEYE QIPQENPPEE LSQDPVLELS GGLREKEQKT PRRLRLILMG KTGSGKSATG NSILGRDVFE SKLSTRPVTK TSQRRSREWA GKELEVIDTP NILSPQVSPE VADAICQAIV LSAPGPHAVL LVTQLGRFTD EDQQVVRRLQ EVFGVGVLGH TILVFTRKED LAGGSLEDYV RETNNQALAW LDVTLARRHC GFNNRAQGEE QEAQLRELME KVEAIMWENE GDYYSNKAYQ YTQQNFRLKE LQERQVSQGQ GSEDVPGEES WLEGLSQIQK ESEEAHRCLL GKADL
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 :
TXNL1 HumanDescription:
Thioredoxin-Like 1 Human Recombinant
Thioredoxin-like protein 1, TRP32, Txl, 32 kDa thioredoxin-related protein, TXNL, Thioredoxin-like 32kDa, TXL-1.
Product # :
PRO-084Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
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Description
TXNL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-289.a.a) and having a molecular mass of 34.4kDa. TXNL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TXNL1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
TXNL1 is a cytoplasmic protein which takes part in endocytotic signaling pathways and acts as a redox sensor. TXNL1 is universally expressed in the body and its goal is to couple oxidative stress to endocytosis, thereby regulating the GDI. Moreover, overexpression of TXNL1 inhibits cell proliferation by predisposing the cell to G0/G1 arrest, signifying that TXNL1 also functions as a transcriptional repressor.
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Synonyms
Thioredoxin-like protein 1, TRP32, Txl, 32 kDa thioredoxin-related protein, TXNL, Thioredoxin-like 32kDa, TXL-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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK YPQAVFLEVD VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE EKIKQHLEND PGSNEDTDIP KGYMDLMPFI NKAGCECLNE SDEHGFDNCL RKDTTFLESD CDEQLLITVA FNQPVKLYSM KFQGPDNGQG PKYVKIFINL PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN VNSVTIFVQS NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH
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 :
PRPS2 HumanDescription:
Phosphoribosyl Pyrophosphate Synthetase 2 Human Recombinant
Phosphoribosyl Pyrophosphate Synthetase 2, Phosphoribosyl Pyrophosphate Synthase II, Ribose-Phosphate Diphosphokinase 2, EC 2.7.6.1, PRS-II, Ribose-Phosphate Pyrophosphokinase 2, PPRibP Synthetase , PRS II, PPRibP, PRSII, Ribose-phosphate pyrophosphokinase 2.
Product # :
PKA-009Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
- purity
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Description
PRPS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321 a.a) and having a molecular mass of 37.4kDa. PRPS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
PRPS2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Phosphoribosyl Pyrophosphate Synthetase 2, also known as PRPS2 is a member of the ribose-phosphate pyrophosphokinase family. PRPS2 catalyzes the synthesis of 5-phosphoribosyl 1-pyrophosphate from ATP and D-ribose 5-phosphate.
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Synonyms
Phosphoribosyl Pyrophosphate Synthetase 2, Phosphoribosyl Pyrophosphate Synthase II, Ribose-Phosphate Diphosphokinase 2, EC 2.7.6.1, PRS-II, Ribose-Phosphate Pyrophosphokinase 2, PPRibP Synthetase , PRS II, PPRibP, PRSII, Ribose-phosphate pyrophosphokinase 2.
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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 MGSMPNIVLF SGSSHQDLSQ RVADRLGLEL GKVVTKKFSN QETSVEIGES VRGEDVYIIQ SGCGEINDNL MELLIMINAC KIASSSRVTA VIPCFPYARQ DKKDKVGESR APISAKLVAN MLSVAGADHI ITMDLHASQI QGFFDIPVDN LYAEPAVLQW IRENIAEWKN CIIVSPDAGG AKRVTSIADR LNVEFALIHK ERKKANEVDR MVLVGDVKDR VAILVDDMAD TCGTICHAAD KLLSAGATKV YAILTHGIFS GPAISRINNA AFEAVVVTNT IPQEDKMKHC TKIQVIDISM ILAEAIRRTH NGESVSYLFS HVPL.
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.