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Name :
Leptin qA Rat, PEGDescription:
Leptin Quadruple Antagonist, Pegylated Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1241Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Rat Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro.
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of rat pegylated leptin antagonist and filter sterilization rat pegylated leptin antagonist 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 Rat Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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 :
PTH (7-84) N15 HumanDescription:
Parathyroid Hormone (7-84) N15 Labeled Human Recombinant
Parathyrin, PTH, Parathormone.
Product # :
HOR-013Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PTH (7-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8900 Dalton labeled by the stable isotope N15.The PTH (7-84) N15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTH (7-84) N15 protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptor in three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone. In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb. In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
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Synonyms
Parathyrin, PTH, Parathormone.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PTH (7-84) N15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH (7-84) N15 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 PTH (7-84) N15 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ
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 :
REXO2 HumanDescription:
RNA Exonuclease 2 Human Recombinant
REX2, RNA exonuclease 2 homolog (S. cerevisiae), CGI-114, RFN, SFN, Oligoribonuclease, mitochondrial, RNA exonuclease 2 homolog, Small fragment nuclease,REXO2, SMFN.
Product # :
ENZ-715Price :
Quantity :
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Shipped with Ice Packs
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Description
REXO2 Human Recombinant produced in E. coli is a single polypeptide chain containing 235 amino acids (26-237) and having a molecular mass of 26.8kDa. REXO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The REXO2 solution (1mg/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
EXO2 is a 3'-to-5' exonuclease specific for small (primarily 5 nucleotides or less in length) single-stranded RNA and DNA oligomers. RNA Exonuclease 2 (REXO2) takes part in DNA repair, replication, and recombination, and in RNA processing and degradation. EXO2 is involved in resistance of human cells to UV-C-induced cell death via its part in the DNA repair process.
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Synonyms
REX2, RNA exonuclease 2 homolog (S. cerevisiae), CGI-114, RFN, SFN, Oligoribonuclease, mitochondrial, RNA exonuclease 2 homolog, Small fragment nuclease,REXO2, SMFN.
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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 MGSVREGGAA MAAGESMAQR MVWVDLEMTG LDIEKDQIIE MACLITDSDL NILAEGPNLI IKQPDELLDS MSDWCKEHHG KSGLTKAVKE STITLQQAEY EFLSFVRQQT PPGLCPLAGN SVHEDKKFLD KYMPQFMKHL HYRIIDVSTV KELCRRWYPE EYEFAPKKAA SHRALDDISE SIKELQFYRN NIFKKKIDEK KRKIIENGEN EKTVS.
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 :
TNNT2 HumanDescription:
Cardiac Muscle Troponin T Recombinant Human
CMH2, RCM3, TnTC, cTnT, CMPD2, MGC3889, TNNT2, Troponin T- cardiac muscle, Cardiac muscle troponin T, troponin T type 2 (cardiac).
Product # :
PRO-2603Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Cardiac Muscle Troponin T Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 297 amino acids and having a molecular mass of 35.8kDa.TNNT2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNNT2 is supplied as a 0.2 μm filtered solution conteining 10mM Tris-HCl, pH8.0, 50% glycerol and 250mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
TNNT2 is the tropomyosin-binding subunit of the troponin complex, which is situated on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration. Mutations in TNNT2 gene can lead to familial hypertrophic cardiomyopathy as well as dilated cardiomyopathy. TNNT2 mutation takes part in hypertrophic cardiomyopathy.
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Synonyms
CMH2, RCM3, TnTC, cTnT, CMPD2, MGC3889, TNNT2, Troponin T- cardiac muscle, Cardiac muscle troponin T, troponin T type 2 (cardiac).
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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
SDIEEVVEEY EEEEQEEAAV EEEEDWREDE DEQEEAAEED AEAEAETEET RAEEDEEEEE AKEAEDGPME ESKPKPRSFM PNLVPPKIPD GERVDFDDIH RKRMEKDLNE LQALIEAHFE NRKKEEEELV SLKDRIERRR AERAEQQRIR NEREKERQNR LAEERARREE EENRRKAEDE ARKKKALSNM MHFGGYIQKQ AQTERKSGKR QTEREKKKKI LAERRKVLAI DHLNEDQLRE KAKELWQSIY NLEAEKFDLQ EKFKQQKYEI NVLRNRINDN QKVSKTRGKA KVTGRWK.
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 :
GM-CSF RatDescription:
Granulocyte Macrophage-Colony Stimulating Factor Rat Recombinant
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Product # :
CYT-395Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Granulocyte Macrophage Colony Stimulating Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14590.65 Dalton. GM-CSF Rat Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GM-CSF Rat was lyophilized with no additives.
Purity
Greater than 96.0% as determined by:
(a)Analysis by RP-HPLC.
(b)Analysis by SDS-PAGE.Biological Activity
The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.
More Info
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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor 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
MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
VTTFEDFIKN LKGFLFDIPF DCWKPVQK.
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Background
What is the molecular weight/Mw of GM-CSF RAT Protein?
GM-CSF RAT Protein has a total Mw of 14.59kDa.
What is the source or expression system of GM-CSF RAT Protein?
Escherichia Coli.
What is the Purity of GM-CSF RAT Protein?
GM-CSF RAT Protein is >96% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF RAT Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.
What is the amino acid sequence of GM-CSF RAT Protein?
MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
VTTFEDFIKN LKGFLFDIPF DCWKPVQK.
What applications can GM-CSF RAT Protein be used in?
GM-CSF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF RAT Protein?
The endotoxin level is minimal, GM-CSF RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NRP1 MouseDescription:
Neuropilin 1 Mouse Recombinant
Neuropilin-1, A5 protein, CD304, Nrp1, Nrp.
Product # :
CYT-971Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NRP1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856 a.a.) and having a molecular mass of 94.7kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NRP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Neuropilin 1 (Nrp1) is a transmembrane glycoprotein which functions as a co-receptor for several extracellular ligands including class III/IV semaphorins, some isoforms of vascular endothelial growth factor and transforming growth factor beta. Nrp1 binds vascular endothelial growth factor (VEGF)-A and is believed to serve as a coreceptor for kinase insert domain-containing receptor (KDR) by connecting with KDR and enhancing VEGF signaling. Nrp1 is a marker of regulatory T cells.
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Synonyms
Neuropilin-1, A5 protein, CD304, Nrp1, Nrp.
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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
FRSDKCGGTI KIENPGYLTS PGYPHSYHPS EKCEWLIQAP EPYQRIMINF NPHFDLEDRD CKYDYVEVID GENEGGRLWG KFCGKIAPSP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TAPTGVIKSP GFPEKYPNSL ECTYIIFAPK MSEIILEFES FDLEQDSNPP GGMFCRYDRL EIWDGFPEVG PHIGRYCGQK TPGRIRSSSG VLSMVFYTDS AIAKEGFSAN YSVLQSSISE DFKCMEALGM ESGEIHSDQITASSQYGTNW SVERSRLNYP ENGWTPGEDS YKEWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYRVD ISSNGEDWIS LKEGNKAIIF QGNTNPTDVV LGVFSKPLIT RFVRIKPVSW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITASN QADRNWMPEN IRLVTSRTGW ALPPSPHPYT NEWLQVDLGD EKIVRGVIIQ GGKHRENKVF MRKFKIAYSN NGSDWKTIMD DSKRKAKSFE GNNNYDTPEL RTFSPLSTRF IRIYPERATH SGLGLRMELL GCEVEAPTAG PTTPNGNPVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTIIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDSHAQL RWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQSSAHC MTFWYHMSGS HVGTLRVKLR YQKPEEYDQL VWMVVGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PTDLDKKNTE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH HHH
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 :
Lymphotactin RatDescription:
Lymphotactin (XCL1) Rat Recombinant
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Product # :
CHM-038Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Lymphotactin (XCL1) Rat Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.0kDa.Lymphotactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a chemotaxis bioassay using human XCR1 transfected murine BaF3 cells < 100 ng/ml, corresponding to a specific activity of > 1.0 × 104 IU/mg.
More Info
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Introduction
XCL1 is a small cytokine belongs to the XC chemokine family that is also known as lymphotactin. XCL1 is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
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Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized XCL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Lymphotactin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Lymphotactin 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
VGTEVLQESI CVSLRTQRLP VQKIKTYTIK EGAMRAVIFV TKRGLRICAD PQAKWVKTAI KTVDGRASAS KSKAETIPTQ AQRSASTAVT LTG.
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 :
CTF1 RatDescription:
Cardiotrophin-1 Rat Recombinant
Cardiotrophin-1, CT-1, Ctf1.
Product # :
CYT-199Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.More Info
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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction. -
Synonyms
Cardiotrophin-1, CT-1, Ctf1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
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Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.4kDa.
What is the source or expression system of CTF1 Protein?
Escherichia Coli.
What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF1 Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.
What is the amino acid sequence of CTF1 Protein?
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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 :
IL 13 RatDescription:
Interleukin-13 Rat Recombinant
NC300, ALRH, BHR1, P600, IL-13.
Product # :
CYT-391Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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Description
Interleukin-13 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 113 amino acids and having a molecular mass of 12.7 kDa.The IL-13 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
ED50 range = 2-6 ng/mL as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.More Info
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Introduction
IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.
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Synonyms
NC300, ALRH, BHR1, P600, IL-13.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 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 Interleukin 13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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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 0.69 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 calibrated solution of IL-13 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.
- View Data Sheet
Name :
IL2RA Human, sf9Description:
Interleukin-2 Receptor alpha Human Recombinant, sf9
Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.
Product # :
CYT-1020Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL2RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 461 amino acids (22-240 a.a.) and having a molecular mass of 52.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).IL2RA is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL2RA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
IL2-Ra is one of the three constituent subunits of the IL2 receptor.
IL-2Ra is released into the serum after increased cellular expression such as increased activation of B and T cells. Clinical manifestations of IL2-Ra elevation include autoimmune conditions and some leukemias and lymphomas. -
Synonyms
Interleukin 2 Receptor Subunit Alpha, Interleukin 2 Receptor, Alpha, IL-2 Receptor Subunit Alpha, IL-2R Subunit Alpha, TAC Antigen, P55, Insulin-Dependent Diabetes Mellitus 10, Interleukin-2 Receptor Subunit Alpha, CD25 Antigen, IL-2-RA, IDDM10, IL2-RA, IMD41, TCGFR, CD25, IL2R.
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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
ADPELCDDDP PEIPHATFKA MAYKEGTMLN CECKRGFRRI KSGSLYMLCT GNSSHSSWDN QCQCTSSATR NTTKQVTPQP EEQKERKTTE MQSPMQPVDQ ASLPGHCREP PPWENEATER IYHFVVGQMV YYQCVQGYRA LHRGPAESVC KMTHGKTRWT QPQLICTGEM ETSQFPGEEK PQASPEGRPE SETSCLVTTT DFQIQTEMAA TMETSIFTTE YQLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL36RN MouseDescription:
Interleukin-36 Receptor Antagonist Mouse Recombinant
Product # :
CYT-154Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL36RN Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.0kDa.The IL36RN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Fully biologically active when compared to standard. Measured by its ability to inhibit IL-36a, IL-36b or IL-36g induced IL-6 secretion by NIH-3T3 mouse embryonic fibroblast cells. The ED50 for this effect is typically 0.8-4ug/ml (corresponding to a specific activity of 250-125units/mg) in the presence of 15ng/ml of recombinant mouse IL-36b.More Info
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Introduction
IL36RA belongs to the IL-1 family of proteins. IL36RA is produced as a 156 aa protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation site but, IL36RA is secreted as a 17 kDa monomer. Cells known to express IL36Ra/IL1F5 include monocytes, B cells, keratinocytes, dendritic cells/Langerhans cells and gastric fundus Parietal and Chief cells.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IL 36RN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 36RN should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized IL36RN 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
VLSGALCFRM KDSALKVLYL HNNQLLAGGL HAEKVIKGEE ISVVPNRALD ASLSPVILGV QGGSQCLSCG TEKGPILKLE PVNIMELYLG AKESKSFTFY RRDMGLTSSF ESAAYPGWFL CTSPEADQPV RLTQIPEDPA WDAPITDFYF QQCD
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 :
GDA Human, ActiveDescription:
Guanine Deaminase Human Recombinant, Active
Guanine Deaminase, Guanine Aminohydrolase, Guanine Aminase, P51-Nedasin, EC 3.5.4.3, GUANASE, GAH, Cytoplasmic PSD95 Interactor, KIAA1258, NEDASIN, CYPIN.
Product # :
ENZ-982Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GDA Human Recombinant produced in E. coli is a single polypeptide chain containing 477 amino acids (1-454) and having a molecular mass of 53kDa.GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 10% glycerol, 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,000 pmol/min/ug, and is defined as the amount of enzyme that convert guanine to xanthine per minute at pH 8.0 at 37C.More Info
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Introduction
GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.
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Synonyms
Guanine Deaminase, Guanine Aminohydrolase, Guanine Aminase, P51-Nedasin, EC 3.5.4.3, GUANASE, GAH, Cytoplasmic PSD95 Interactor, KIAA1258, NEDASIN, CYPIN.
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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 MGSMCAAQMP PLAHIFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE ASQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHASQ YSFAGSSIDL PLLEWLTKYT FPAEHRFQNI DFAEEVYTRV VRRTLKNGTT TACYFATIHT DSSLLLADIT DKFGQRAFVG KVCMDLNDTF PEYKETTEES IKETERFVSE MLQKNYSRVK PIVTPRFSLS CSETLMGELG NIAKTRDLHI QSHISENRDE VEAVKNLYPS YKNYTSVYDK NNLLTNKTVM AHGCYLSAEE LNVFHERGAS IAHCPNSNLS LSSGFLNVLE VLKHEVKIGL GTDVAGGYSY SMLDAIRRAV MVSNILLINK VNEKSLTLKE VFRLATLGGS QALGLDGEIG NFEVGKEFDA ILINPKASDS PIDLFYGDFF GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.
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 :
UMOD CanineDescription:
Uromodulin Canine
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
Product # :
ENZ-334Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
UMOD is an 85-kDa glycoprotein which is produced in the thick ascending limb of Henle´s loop and early distal convoluted tubules of the nephron.
Source
Canine Urine.
Formulation
The UMOD protein was lyophilized from 0.4µm filtered solution at a concentration of 0.1mg/ml containing deionized water.
More Info
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Introduction
Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.
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Synonyms
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UMOD should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
RSCSECHSNA TCMEDGMVTT CSCLVGFTGS GFECVDLDEC AIPGAHNCSE GSSCMNTLGS YLCTCPDGFR LTPGLGCIDV DECSEPGLSR CHALATCINN KGNYSCVCPA GYRGDGQHCE CSPGSCGPGL DCVPVGDALV CADPCQEHRI LDEYWRSTEY GAGYTCDVGL NGWYRFTGPG GVRLAETCVP VLHCNTAAPM WLNGTHPTRD QGIVNRTACA HWRGHCCLWD ASIQVKACAG GYYVYNLTET PECYLAYCTD PTSVLGTCEE CSVEEDCKSH DGMWSCQCKQ DFNVTDLFLL DRLECRPNDI KVSLSKCQLK SLGFEKVFMY LRDSQCSGFN ERGDRDWVSV VTPARDGPCG TVMVRNETHA TYSNTLYLAD EIVIRDRNIK INFECSYPLD MKVSLETSLQ PIVSSLNISV GGTGMFTVRM ALFQTPDYTQ PYQGSSVTLT TEAFLYVGTM LDGGDLSRFA LLMTNCYATP SSNATDPLKY FIIQDRCPRT TDSTIQVVEN GESPQGRFSV QMFRFAGNYD LVYLHCEVYL CDIINEKCKP TCSGTRFRSG GIIDQSRVLN LGPITRKNVQ AVVSRAASS.
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 :
TNFRSF10A Human FcDescription:
TRAIL Receptor-1 Human Recombinant Fc
Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.
Product # :
CYT-877Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TRAIL R1 Fc Human Recombinant (24-240) produced in E.Coli is a non-glycosylated, disulfide-linked homodimer containing two polypeptide chains of 217 amino acids each and having a molecular mass of 41kDa [including tag] each chain. TRAILR1 is fused to a 236 amino acid Fc tag at C-terminal and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to inhibit Trail-mediated cytotoxicity in mouse L-929 cells, is less than 1.25ng/ml.More Info
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Introduction
Human TNFRSF10A is a type 1 transmembrane protein in the TNF R superfamily. TNFRSF10A is not expressed in rodents. The trimeric ligand Trail binds TNFRSF10A and induces apoptosis, and recombinant, soluble forms of the receptor inhibit Trail-induced apoptosis. TNFRSF10A is expressed generally in damaged, infected, and malignant cells. TNFRSF10A functions in immune surveillance, inducing apoptosis in cancer cells but not normal cells.
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Synonyms
Tumor Necrosis Factor Receptor Superfamily Member 10a, TRAILR1, APO2, DR4, TNF-Related Apoptosis-Inducing Ligand Receptor 1, Death Receptor 4, TRAIL Receptor 1, TRAIL-R1, Tumor Necrosis Factor Receptor Superfamily Member 10a Variant 2, Tumor Necrosis Factor Receptor Superfamily Member 10A, Cytotoxic TRAIL Receptor, CD261 Antigen, TRAILR-1, CD261, TNFRSF10A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TNFRSF10A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TRAIL-R1 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 TNFRSF10A 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
ASGTEAAAAT PSKVWGSSAG RIEPRGGGRG ALPTSMGQHG PSARARAGRA PGPRPAREAS PRLRVHKTFK FVVVGVLLQV VPSSAATIKL HDQSIGTQQW EHSPLGELCP PGSHRSERPG ACNRCTEGVG YTNASNNLFA CLPCTACKSD EEERSPCTTT RNTACQCKPG TFRNDNSAEM CRKCSTGCPR GMVKVKDCTP WSDIECVHKE SGNGHNIEGR MDPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK.
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 :
Pen a 1.0101Description:
Tropomyosin Pen a 1.0101 Recombinant
Product # :
ALR-024Price :
Quantity :
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Description
Recombinant Tropomyosin Pen a 1.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 38kDa.Pen a 1.0101 is expressed with a 10xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Pen a 1.0101 is supplied in 20mM HEPES buffer pH-7.9 200mM NaCl and 6M Urea.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Pen a 1.0101 is a Tropomyosin and the only major allergen in brown shrimp Penaeus aztecus. The panallergen is highly conserved and soluble muscle protein. Pen a 1.0101 is has an alpha-helical homodimeric, coiled-coil structure.
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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.Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
DHH (C23II) HumanDescription:
Desert Hedgehog (C23II) Human Recombinant
HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.
Product # :
CYT-362Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
DHH (C23II) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 19.9kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological Activity was determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 15-45 μg/ml.More Info
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Introduction
DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development. -
Synonyms
HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) 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 DHH (C23II) 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
IIGPGRGPVG RRRYARKQLV PLLYKQFVPG VPERTLGASG PAEGRVARGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH VHVSVKADNS LAVRAGG.
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 :
SNCA NACP112 HumanDescription:
Alpha Synuclein NACP112 Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-162Price :
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Shipped with Ice Packs
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Description
A-Synuclein NACP112 Human Recombinant which is an alternatively spliced (103-129) form of a-Synuclein, produced in E.Coli is a single, non-glycosylated polypeptide chain of 112 amino acids having a molecular mass of 11.3kDa. The Recombinant Human a-Synuclein NACP112 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA NACP112 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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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
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKEGYQDYEP EA.
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 :
AKR1D1 HumanDescription:
Aldo-Keto Reductase Family 1 Member D1 Human Recombinant
3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-Keto Reductase Family 1, Member D1, SRD5B1, Delta(4)-3-Ketosteroid 5-Beta-Reductase, Delta 4-3-Ketosteroid-5-Beta-Reductase, Delta(4)-3-Oxosteroid 5-Beta-Reductase, CBAS2, Steroid-5-Beta-Reductase, Beta Polypeptide 1 (3-Oxo-5 Beta-Steroid Delta 4-Dehydrogenase Beta 1), Aldo-Keto Reductase Family 1, Member D1 (Delta 4-3-Ketosteroid-5-Beta-Reductase), Aldo-Keto Reductase Family 1 Member D1, 3-Oxo-5-Beta-Steroid 4-Dehydrogenase, EC 1.3.1.3, 3o5bred.
Product # :
ENZ-931Price :
Quantity :
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Description
AKR1D1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 326 amino acids (1-326 a.a.) and having a molecular mass of 37.3kDa. The AKR1D1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1D1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Aldo-keto reductase family 1 member D1 (AKR1D1) belongs to the AKR superfamily. The AKR family proteins are soluble NADPH oxidoreductases, which have vital roles in the metabolism of drugs, carcinogens and reactive aldehydes. AKR1D1 is also responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones that carry a delta (4)-3-1 structure. AKR1D1 is highly expressed in the liver, colon and testis. Deficiency of the AKR1D1 enzyme may contribute to hepatic dysfunction.
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Synonyms
3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-Keto Reductase Family 1, Member D1, SRD5B1, Delta(4)-3-Ketosteroid 5-Beta-Reductase, Delta 4-3-Ketosteroid-5-Beta-Reductase, Delta(4)-3-Oxosteroid 5-Beta-Reductase, CBAS2, Steroid-5-Beta-Reductase, Beta Polypeptide 1 (3-Oxo-5 Beta-Steroid Delta 4-Dehydrogenase Beta 1), Aldo-Keto Reductase Family 1, Member D1 (Delta 4-3-Ketosteroid-5-Beta-Reductase), Aldo-Keto Reductase Family 1 Member D1, 3-Oxo-5-Beta-Steroid 4-Dehydrogenase, EC 1.3.1.3, 3o5bred.
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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
MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR HIDGAYIYQN EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP TLERTLRVLQ LDYVDLYIIE VPMAFKPGDE IYPRDENGKW LYHKSNLCAT WEAMEACKDA GLVKSLGVSN FNRRQLELIL NKPGLKHKPV SNQVECHPYF TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK DALLNSLGKR YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE ALNKNVRFVE LLMWRDHPEY PFHDEY.
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 :
IL 9 RatDescription:
Interleukin-9 Rat Recombinant
Interleukin 9, Protein Il9, Il9.
Product # :
CYT-748Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-9 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa.The IL-9 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL9 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using murine TS1 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg.More Info
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Introduction
Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
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Synonyms
Interleukin 9, Protein Il9, Il9.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 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 Interleukin 9 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
MQRCSTSWGI QHTSYLIENL KDDPSSKCSC SANVTSCLCL PIPSDDCTTP CFQEGMSQVT NATQQSKFSP FFFRVKRIVE TLKSNKCQFF SCEKPCNQTT AGNTVSFLKS LLKTFQKTEV QVQRSRA.
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 :
PEF1 HumanDescription:
Penta-EF-Hand Domain Containing 1 Human Recombinant
Peflin, PEF protein with a long N-terminal hydrophobic domain, Penta-EF hand domain-containing protein 1, PEF1, ABP32, PEF1A.
Product # :
PRO-099Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- More Info
Description
PEF1 Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 320 amino acids (1-284 a.a.) and having a molecular mass of 34.5kDa. The PEF1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PEF1 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50% glycerol and 0.2M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Penta-EF-hand domain containing 1 (PEF1) is a member of the penta-EF-hand protein family, which shares similarities to the apoptosis linked gene ALG-2. PEF1 forms heterodimers with PDCD6/ALG2 and dissociates from PDCD6/ALG2 in the presence of Ca (2+). Furthermore, PEF1 proteins bind calcium and participate in a various calcium-dependent processes in vertebrates.
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Synonyms
Peflin, PEF protein with a long N-terminal hydrophobic domain, Penta-EF hand domain-containing protein 1, PEF1, ABP32, PEF1A.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASY PYRQGCPGAA GQAPGAPPGS
YYPGPPNSGG QYGSGLPPGG GYGGPAPGGP YGPPAGGGPY GHPNPGMFPS GTPGGPYGGA
APGGPYGQPP PSSYGAQQPG LYGQGGAPPN VDPEAYSWFQ SVDSDHSGYI SMKELKQALV
NCNWSSFNDE TCLMMINMFD KTKSGRIDVY GFSALWKFIQ QWKNLFQQYD RDRSGSISYT
ELQQALSQMG YNLSPQFTQL LVSRYCPRSA NPAMQLDRFI QVCTQLQVLT EAFREKDTAV
QGNIRLSFED FVTMTASRML.
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 :
TK2 HumanDescription:
Thymidine Kinase 2 Human Recombinant
Thymidine kinase 2 mitochondrial, Mt-TK, TK2, MTTK, MTDPS2.
Product # :
PKA-041Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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- More Info
Description
TK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 257 amino acids (34-265 a.a) and having a molecular mass of 30.2kDa.TK2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
TK2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 30% glycerol, 2mM DTT and 200mM NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Thymidine kinase 2 mitochondrial (TK2) is a member of the DCK/DGK family. TK2 is an enzyme, a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. Thymidine kinase is found in most living cells. Thymidine kinase is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases have a central function in the synthesis of DNA and thus in cell division, since they are part of the exceptional reaction chain to introduce deoxythymidine into the DNA. TK2 is a deoxyribonucleoside kinase which specifically phosphorylates thymidine, deoxycytidine, and deoxyuridine. TK2 localizes to the mitochondria and is essential for mitochondrial DNA synthesis. TK2 gene defects are a cause of mitochondrial DNA depletion syndrome type 2 (MTDPS2).
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Synonyms
Thymidine kinase 2 mitochondrial, Mt-TK, TK2, MTTK, MTDPS2.
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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 MGSHMVQRRA WPPDKEQEKE KKSVICVEGN IASGKTTCLE FFSNATDVEV LTEPVSKWRN VRGHNPLGLM YHDASRWGLT LQTYVQLTML DRHTRPQVSS VRLMERSIHS ARYIFVENLY RSGKMPEVDY VVLSEWFDWI LRNMDVSVDL IVYLRTNPET CYQRLKKRCR EEEKVIPLEY LEAIHHLHEE WLIKGSLFPM AAPVLVIEAD HHMERMLELF EQNRDRILTP ENRKHCP.
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 :
CD58 Human, Sf9Description:
CD58 Human Recombinant, Sf9
Lymphocyte function-associated antigen 3 isoform 1, CD58, ag3, LFA-3, LFA3, Surface glycoprotein LFA-3.
Product # :
PRO-2493Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD58 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 196 amino acids (29-215a.a.) and having a molecular mass of 22.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CD58 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD58 protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CD33 is putative adhesion molecule of myelomonocytic-derived cells which mediates sialic-acid dependent binding to cells. CD33 prefers to bind to alpha-2,6-linked sialic acid. The sialic acid recognition site is masked by cis interactions with sialic acids on the same cell surface. In the immune response, CD33 perform as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatases through their SH2 domains which block signal transduction through dephosphorylation of signaling molecules. In addition, CD33 induces apoptosis in acute myeloid leukemia.
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Synonyms
Lymphocyte function-associated antigen 3 isoform 1, CD58, ag3, LFA-3, LFA3, Surface glycoprotein LFA-3.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPFSQQIYG VVYGNVTFHV PSNVPLKEVL WKKQKDKVAE LENSEFRAFS SFKNRVYLDT VSGSLTIYNL TSSDEDEYEM ESPNITDTMK FFLYVLESLP SPTLTCALTN GSIEVQCMIP EHYNSHRGLI MYSWDCPMEQ CKRNSTSIYF KMENDLPQKI QCTLSNPLFN TTSSIILTTC IPSSGHSRHR HHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SORD HumanDescription:
Sorbitol Dehydrogenase Human Recombinant
EC 1.1.1.14, SORD1, SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase,SDH, (R,R)-butanediol dehydrogenase, L-iditol 2-dehydrogenase, Polyol dehydrogenase, Ribitol dehydrogenase, RDH, Xylitol dehydrogenase, XDH
Product # :
ENZ-1151Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SORD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-357a.a.) and having a molecular mass of 38.3kDa.SORD is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SORD solution (0.5mg/ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.5) and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity > 15unit/mg. Defined by the amount of enzyme that catalyze the reduction 1.0 umole of D-fructose to D-sorbitol per minute at pH 7.5 at 37˚C.
More Info
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Introduction
SORD, also referred to as sorbitol dehydrogenase, belongs to the zinc-containing alcohol dehydrogenase family. It is widely produced. The lens of the eyeand the kidney are the protein highest production areas. Zinc-dependent interconversion of polyols, like sorbitol and xylitol, are enzymatically catalysed to their respective ketoses by SORD.
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Synonyms
EC 1.1.1.14, SORD1, SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase,
SDH, (R,R)-butanediol dehydrogenase, L-iditol 2-dehydrogenase, Polyol dehydrogenase, Ribitol dehydrogenase, RDH, Xylitol dehydrogenase, XDH -
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
MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC TGAEASIQAG IYATRSGGTL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP
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 :
BDNF Human, CHODescription:
Brain-Derived Neurotrophic Factor Human Recombinant, CHO
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-1262Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
Description
Brain-derived Neurotrophic Factor Human Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 119 amino acids and having a total molecular mass of 27kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
CHO Cells
Formulation
The protein was lyophilized with 5% trehalose and 1x PBS
Purity
Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.sds-page
More Info
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Introduction
BDNF is crucial for the signal survival eukaryotes. BDNF is responsible for the development, repair, adaptation and proper functionality of the nervous system.
BDNF major roles include Neuron survival and development, synaptic flexibility, stress adaptation, Repair and recovery post injury/disease and Pain signaling.
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Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF 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
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
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Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
CHO Cells
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
BDNF CHO activity is determined by its ability to bind recombinant human TrkB Fc Chimera in a functional ELISA assay.
What is the amino acid sequence of BDNF Protein?
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
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References
Title:Generation of Neurons with Improved Cell Survival and Phenotype Maintenance Using a Degradation-Resistant Nurr1 Mutant†‡
Publication:Article first published online: 11 JUN 2009 DOI: 10.1002/stem.146 Copyright © 2009 AlphaMed Press.
Link:BDNF prospec publication
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.