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1000 results found for “Malaria”
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Name :
Lymphotactin MouseDescription:
Lymphotactin (XCL1) Mouse 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-037Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Lymphotactin (XCL1) Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.1kDa.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
reater 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 is < 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
VGTEVLEESS CVNLQTQRLP VQKIKTYIIW EGAMRAVIFV TKRGLKICAD PEAKWVKAAI KTVDGRASTR KNMAETVPTG AQRSTSTAIT 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 :
SAA4 HumanDescription:
Serum Amyloid A4 Human Recombinant
Serum amyloid A-4 protein, Constitutively expressed serum amyloid A protein, C-SAA, SAA4, CSAA.
Product # :
CYT-002Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SAA4 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 131 amino acids (21-130 a.a.) and having a molecular mass of 14.9kDa. The SAA4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SAA4 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 5mM DTT, 0.2M NaCl and 0.5mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SAA4 is a constitutively expressed protein which is a member of the SAA family. SAA4 is a major acute phase reactant and an apolipoprotein of the HDL complex. SAA4 is constitutively expressed only in humans and mice; it is connected almost completely with lipoproteins of the high density range. The physiological function of SAA4 is unknown, and its serum concentration has no association with those of other major apolipoproteins. SAA4 mRNA and protein occurrence in macrophage derived foam cells of coronary and carotid arteries implied a specific role of human SAA4 during inflammation including atherosclerosis.
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Synonyms
Serum amyloid A-4 protein, Constitutively expressed serum amyloid A protein, C-SAA, SAA4, CSAA.
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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 MWRSFFKEAL QGVGDMGRAY WDIMISNHQN SNRYLYARGN YDAAQRGPGG VWAAKLISRS RVYLQGLIDY YLFGNSSTVL EDSKSNEKAE EWGRSGKDPD RFRPDGLPKK Y.
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 :
IFI30 HumanDescription:
IFN Gamma-Inducible protein 30 Human Recombinant
IFI30, Gamma-IFN-Inducible Lysosomal Thiol Reductase, IFN Gamma-Inducible Protein 30 Preproprotein, Gamma-IFN-Inducible Protein IP-30, Legumaturain, GILT, IP30, IFI-30, MGC32056, EC 1.8.
Product # :
CYT-183Price :
Quantity :
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Shipped with Ice Packs
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Description
IFI30 Human Recombinant produced in E. coli is a single polypeptide chain containing 199 amino acids (58-232) and having a molecular mass of 22.5 kDa. IFI30 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The IFI30 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
IFNI30 inducible lysosomal thiol reductase (IFI30), is a part of the GILT family. IFI30 is a lysosomal thiol reductase which at low pH is capable of decreasing protein’s disulfide bonds. IFI30 is expressed constitutively in antigen-presenting cells and induced by gamma-IFN in other cell types. Also, IFI30 plays an important role in MHC class II-restricted antigen processing. IFI30 facilitates the generation of MHC class II-restricted epitopes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds and Also facilitates MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or cross-presentation.
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Synonyms
IFI30, Gamma-IFN-Inducible Lysosomal Thiol Reductase, IFN Gamma-Inducible Protein 30 Preproprotein, Gamma-IFN-Inducible Protein IP-30, Legumaturain, GILT, IP30, IFI-30, MGC32056, EC 1.8.
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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 MGSMNAPLVN VTLYYEALCG GCRAFLIREL FPTWLLVMEI LNVTLVPYGN AQEQNVSGRW EFKCQHGEEE CKFNKVEACV LDELDMELAF LTIVCMEEFE DMERSLPLCL QLYAPGLSPD TIMECAMGDR GMQLMHANAQ RTDALQPPHE YVPWVTVNGK PLEDQTQLLT LVCQLYQGK.
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Background
What is the molecular weight/Mw of IFI30 HUMAN Protein?
IFI30 HUMAN Protein has a total Mw of 22.5kDa.
What is the source or expression system of IFI30 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFI30 HUMAN Protein?
IFI30 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFI30 HUMAN Protein?
The biological functionality of IFI30 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IFI30 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNAPLVN VTLYYEALCG GCRAFLIREL FPTWLLVMEI LNVTLVPYGN AQEQNVSGRW EFKCQHGEEE CKFNKVEACV LDELDMELAF LTIVCMEEFE DMERSLPLCL QLYAPGLSPD TIMECAMGDR GMQLMHANAQ RTDALQPPHE YVPWVTVNGK PLEDQTQLLT LVCQLYQGK.
What applications can IFI30 HUMAN Protein be used in?
IFI30 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFI30 HUMAN Protein?
The endotoxin level is minimal, IFI30 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 17 MouseDescription:
Interleukin-17 Mouse Recombinant
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.
Product # :
CYT-378Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-17 Murine Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 268 (2x134 a.a.) amino acids and having a molecular mass of 30 kDa. The IL-17 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) 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 ED50 as determined by the dose-dependant induction of IL-6 production in cultured mouse NIH 3T3 fibroblasts was found to be 0.4 ng/ml, corresponding to a specific activity of 2,500,000 units/mg.More Info
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Introduction
IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.
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Synonyms
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17 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 17 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
MAAIIPQSSA CPNTEAKDFL QNVKVNLKVF NSLGAKVSSR RPSDYLNRST SPWTLHRNED PDRYPSVIWE AQCRHQRCVN AEGKLDHHMN SVLIQQEILV LKREPESCPF TFRVEKMLVG VGCTCVASIV RQAA.
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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 0.942 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 IL-17 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 :
IL 31 HumanDescription:
Interleukin-31 Human Recombinant
Interleukin 31, IL31, IL-31.
Product # :
CYT-625Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL-31 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (24-164 a.a.) and having a molecular mass of 15.8 kDa.
Source
Escherichia Coli.
Formulation
The IL-31 (1mg/ml) was lyophilized with 20mM Phosphate buffer, 150mM NaCl pH-7.4.
Purity
Greater than 95.0% as determined by(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by its ability to activate STAT following receptor ligand interaction and found to be <5ng/ml, corresponding to a specific activity of 200,000 units.More Info
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Introduction
IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis. -
Synonyms
Interleukin 31, IL31, IL-31.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-31 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-31 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 IL-31 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
SHTLPVRLLR PSDDVQKIVE ELQSLSKMLL KDVEEEKGVL VSQNYTLPCL SPDAQPPNNI HSPAIRAYLK TIRQLDNKSV IDEIIEHLDK LIFQDAPETN ISVPTDTHEC KRFILTISQQ FSECMDLALK SLTSGAQQAT T.
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 7 RatDescription:
Interleukin-7 Rat Recombinant
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Product # :
CYT-163Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL 7 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 15.0kDa.The IL 7 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 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2ng/ml, corresponding to a specific activity of >5,000,000IU/mg.More Info
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Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
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Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-7 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 IL-7 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
DCHIKDKDGK AFGSVLMISI NQLDKMTGTD SDCPNNEPNF FKKHLCDDTK EAAFLNRAAR KLRQFLKMNI SEEFNDHLLR VSDGTQTLVN CTSKEEKTIK EQKKNDPCFL KRLLREIKTC WNKILKGSI
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 :
GMFB MouseDescription:
Glia Maturation Factor Beta Mouse Recombinant
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.
Product # :
CYT-006Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Glia Maturation Factor-Beta (GMF-Beta) Mouse Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.6kDa. GMF-Beta, Mouse Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GMF-beta 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.More Info
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Introduction
GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.
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Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GMF-B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMF-beta 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 GMFB 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
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H. -
Background
What is the molecular weight/Mw of GMFB MOUSE Protein?
GMFB MOUSE Protein has a total Mw of 16.6kDa.
What is the source or expression system of GMFB MOUSE Protein?
Escherichia Coli.
What is the Purity of GMFB MOUSE Protein?
GMFB MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of GMFB MOUSE Protein?
The biological functionality of GMFB MOUSE Protein will be determined in the future.
What is the amino acid sequence of GMFB MOUSE Protein?
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.
What applications can GMFB MOUSE Protein be used in?
GMFB MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GMFB MOUSE Protein?
The endotoxin level is minimal, GMFB MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CST3 Mouse, ActiveDescription:
Cystatin-C Mouse Recombinant, Active
Cystatin-C, Cystatin-3, Cst3, CST3
Product # :
PRO-2433Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CST3 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140 a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CST3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The IC50 value is < 1.0nM. The inhibitory function of Cystatin 3 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25°C.
More Info
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Introduction
Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.
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Synonyms
Cystatin-C, Cystatin-3, Cst3, CST3
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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
ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA 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.
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Name :
CD4 (26-396) HumanDescription:
CD4 (26-396) Human Recombinant
CD4 Molecule, T-Cell Surface Glycoprotein CD4, T-Cell Surface Antigen T4/Leu-3, CD4 Antigen (P55), CD4 Receptor, CD4 Antigen, CD4mut, T-cell surface glycoprotein CD4.
Product # :
CYT-885Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (26-396 a.a) and having a molecular mass of 44kDa. CD4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CD4 protein solution (0.25mg/ml) containing 20mM Tris Hcl, PH8.0 and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
CD4 is a cell-surface glycoprotein found on the mature helper T cells and immature thymocytes, as well as on monocytes and macrophages. (Some cytotoxic T cells have CD4 protein as well.) Normally, about 65% of T cells in the blood are CD4+ (have CD4 protein protruding from their membrane). A mature T cell with either have CD4 or CD8, but not both. During one stage of development T cells develop CD4 and CD8 receptors, but they eventually are differentiated in the thymus and become more specialized.
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Synonyms
CD4 Molecule, T-Cell Surface Glycoprotein CD4, T-Cell Surface Antigen T4/Leu-3, CD4 Antigen (P55), CD4 Receptor, CD4 Antigen, CD4mut, T-cell surface glycoprotein CD4.
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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 MGSHMKKVVL GKKGDTVELT CTASQKKSIQ FHWKNSNQIK ILGNQGSFLT KGPSKLNDRA DSRRSLWDQG NFPLIIKNLK IEDSDTYICE VEDQKEEVQL LVFGLTANSD THLLQGQSLT LTLESPPGSS PSVQCRSPRG KNIQGGKTLS VSQLELQDSG TWTCTVLQNQ KKVEFKIDIV VLAFQKASSI VYKKEGEQVE FSFPLAFTVE KLTGSGELWW QAERASSSKS WITFDLKNKE VSVKRVTQDP KLQMGKKLPL HLTLPQALPQ YAGSGNLTLA LEAKTGKLHQ EVNLVVMRAT QLQKNLTCEV WGPTSPKLML SLKLENKEAK VSKREKAVWV LNPEAGMWQC LLSDSGQVLL ESNIKVLPTW STPVQP.
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 :
CoV-2-Spike (1-260)Description:
Coronavirus 2019 Spike (1-260 a.a.), Recombinant
Product # :
SARS-022Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
The HEK293 derived recombinant protein contains the Coronavirus 2019-Spike N-Terminal Domain, Wuhan-Hu-1 strain, amino acids 1-260 fused to Fc tag at C-terminal.
Source
HEK293
Formulation
CoV-2 spike protein solution is supplied in DPBS.
Purity
Protein is >95% pure as determined SDS-PAGE.
More Info
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Introduction
A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.
The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.
While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
CoV-2 Spike Protein is shipped on ice packs. Upon arrival, Store at -20°C.
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Purification Method
Purified by Protein-G chromatographic technique.
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 :
DHFR HumanDescription:
Dihydrofolate Reductase Human Recombinant
Dihydrofolate reductase, DHFR, DHFRP1.
Product # :
ENZ-443Price :
Quantity :
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Shipped with Ice Packs
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- sds-page
Description
DHFR Human Recombinant fused with a 20 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.6kDa.The DHFR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DHFR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 2mM DTT and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >2000 pmol/min/ug is defined as the amount of enzyme that converts 1.0 pmole of dihydrofolic acid to tetrahydrofolic acid per minute at pH 6.5 at 25C.
sds-page
More Info
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Introduction
Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes.
DHFR deficiency is associated with megaloblastic anemia.
DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid.
DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women. -
Synonyms
Dihydrofolate reductase, DHFR, DHFRP1.
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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 MVGSLNCIVA VSQNMGIGKN GDLPWPPLRN EFRYFQRMTT TSSVEGKQNL VIMGKKTWFS IPEKNRPLKG RINLVLSREL KEPPQGAHFL SRSLDDALKL TEQPELANKV DMVWIVGGSS VYKEAMNHPG HLKLFVTRIM QDFESDTFFP EIDLEKYKLL PEYPGVLSDV QEEKGIKYKF EVYEKND.
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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Description:
SARS-Associated Coronavirus Nucleocapsid Core Recombinant
Product # :
SARS-255Price :
Quantity :
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Shipped with Ice Packs
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Description
The E.Coli derived 35 kDa recombinant protein contains Nucleocapsid protein 1-49, 192-220 amino acids immunodominant regions. The 2 regions are separated with 3 glycine residues.
Formulation
50mM Tris-HCl, pH-8, 60mM NaCl and 50% glycerol.
Purity
SARS Core protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.
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Stability
SARS Core protein is shipped at ambient temperature. Upon arrival, store at -20C.
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Applications
SARS Core antigen is suitable for ELISA and Western blots, excellent antigen for detection of SARS with minimal specificity problems.
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Specificity
SARS Core protein is Immunoreactive with sera of SARS-infected individuals.
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Purification Method
SARS Core protein was purified by proprietary chromatographic technique.
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 11 MouseDescription:
Interleukin-11 Mouse Recombinant
AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.
Product # :
CYT-646Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-11 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19.1kDa. The Mouse IL-11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a 0.2µm filtered concentrated (1mg/ml) 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 the dose-dependant stimulation of the proliferation of murine T11 was found to be less than 2.0 ng/ml, corresponding to a specific activity of 500,000IU/mg.More Info
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Introduction
IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.
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Synonyms
AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 11 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
MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL.
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 :
IL10 HumanDescription:
Interleukin-10 Human Recombinant
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Product # :
CYT-500Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-10 Human Recombinant produced in E.coli is a single non-glycosylated polypeptide chains containing 161 amino acids each and having a molecular mass of 18.6kDa.The IL-10 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1mg/ml) 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 the dose-dependent co-stimulation (with murine IL-4) of MC/9 cells was found to be less than 2.0ng/ml, corresponding to a specific activity of 5.0×105 IU/mg.More Info
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Introduction
Recombinant IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
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Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL10 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-10 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
MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.
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 :
PECI HumanDescription:
Peroxisomal D3,D2-Enoyl-CoA Isomerase Human Recombinant
EC 5.3.3.8, ACBD2, DRS1, HCA88, PECI, Peroxisomal 3,2-trans-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, Delta(3),delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Diazepam-binding inhibitor-related protein 1, DBI-related protein 1, DRS-1, Hepatocellular carcinoma-associated antigen 88, Renal carcinoma antigen NY-REN-1, KIAA0536, dJ1013A10.
Product # :
ENZ-531Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PECI Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-364 a.a.) and having a molecular mass of 42.3 kDa. The PECI is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PECI Human solution (1mg/ml) containing 20mM Tris-HCl, pH-8 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PECI is an enzyme that localized to the peroxisomal matrix and encloses one ACB (acyl-CoA-binding) domain. PECI is expressed abundantly in liver, heart and skeletal muscle. PECI functions to catalyze the isomerization of both 3-cis and 3-trans double bonds into the 2-trans form in an array of enoyl-CoA species. PECI takes part in the beta-oxidation of unsaturated fatty acids.
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Synonyms
EC 5.3.3.8, ACBD2, DRS1, HCA88, PECI, Peroxisomal 3,2-trans-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, Delta(3),delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Diazepam-binding inhibitor-related protein 1, DBI-related protein 1, DRS-1, Hepatocellular carcinoma-associated antigen 88, Renal carcinoma antigen NY-REN-1, KIAA0536, dJ1013A10.
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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 MNRTAMRASQ KDFENSMNQV KLLKKDPGNE VKLKLYALYK QATEGPCNMP KPGVFDLINK AKWDAWNALG SLPKEAARQN YVDLVSSLSP SLESSSQVEP GTDRKSTGFE TLVVTSEDGI TKIMFNRPKK KNAINTEMYH EIMRALKAAS KDDSIITVLT GNGDYYSSGN DLTNFTDIPP GGVEEKAKNN AVLLREFVGC FIDFPKPLIA VVNGPAVGIS VTLLGLFDAV YASDRATFHT PFSHLGQSPE GCSSYTFPKI MSPAKATEML IFGKKLTAGE ACAQGLVTEV FPDSTFQKEV WTRLKAFAKL PPNALRISKE VIRKREREKL HAVNAEECNV LQGRWLSDEC TNAVVNFLSR KSKL.
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 :
DDAH1 HumanDescription:
Dimethylarginine Dimethylaminohydrolase 1 Human Recombinant
DDAH, DDAH-1, Dimethylargininase-1, dimethylargininase-1, Dimethylarginine Dimethylaminohydrolase 1.
Product # :
ENZ-014Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DDAH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285a.a.) and having a molecular mass of 33.5kDa.DDAH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DDAH1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 50mM NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Dimethylarginine dimethylaminohydrolase 1, is a part of the Dimethylarginine Dimethylaminohydrolase gene family. DDAH1 participates in nitric oxide generation by regulating cellular concentrations of methylarginines, that in turn inhibit nitric oxide synthase activity. Deficiency of DDAH1 results in ADMA (asymmetric dimethylarginine) increase and a decrease in cGMP generation.
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Synonyms
DDAH, DDAH-1, Dimethylargininase-1, dimethylargininase-1, Dimethylarginine Dimethylaminohydrolase 1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAGLGHP AAFGRATHAV VRALPESLGQ HALRSAKGEE VDVARAERQH QLYVGVLGSK LGLQVVELPA DESLPDCVFV EDVAVVCEET ALITRPGAPS RRKEVDMMKE ALEKLQLNIV EMKDENATLD GGDVLFTGRE FFVGLSKRTN QRGAEILADT FKDYAVSTVP VADGLHLKSF CSMAGPNLIA IGSSESAQKA LKIMQQMSDH RYDKLTVPDD IAANCIYLNI PNKGHVLLHR TPEEYPESAK VYEKLKDHML IPVSMSELEK VDGLLTCCSV LINKKVDS
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 :
CAMK2N1 HumanDescription:
Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 Human Recombinant
PRO1489; RP11-401M16.1, Calcium/calmodulin-dependent protein kinase II inhibitor 1, CaMKII inhibitory protein alpha, CaMKIIN-alpha, CAMK2N1.
Product # :
PRO-1873Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CAMK2N1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (1-78 a.a) and having a molecular mass of 10.9kDa. CAMK2N1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAMK2N1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Calcium/Calmodulin Dependent Protein Kinase II Inhibitor 1 (CAMK2N1), which interacts with CAMK2B, is a part of the CAMK2N family. CAMK2N1 is also interacts with CAMK2A in a way which requires CAMK2A activation by Ca2+. CAMK2N1 is potent and specific inhibitor of CaM-kinase II (CAMK2).
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Synonyms
PRO1489; RP11-401M16.1, Calcium/calmodulin-dependent protein kinase II inhibitor 1, CaMKII inhibitory protein alpha, CaMKIIN-alpha, CAMK2N1.
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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 MGSMSEVLPY GDEKLSPYGD GGDVGQIFSC RLQDTNNFFG AGQNKRPPKL GQIGRSKRVV IEDDRIDDVL KNMTDKAPPG V.
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 :
CAPSL HumanDescription:
Calcyphosine-Like Human Recombinant
Calcyphosine-like protein, CAPSL, MGC26610.
Product # :
PRO-185Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CAPSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (1-208) and having a molecular mass of 26.3 kDa.The CAPSL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAPSL protein at 1mg/ml in 20mM Tris-HCL, pH-8, 0.2M NaCl, 5mM DTT and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CAPSL is a calcium-binding protein holding two conserved calcium-binding motifs (EF-hands) which are found in a superfamily of calcium sensors and calcium signal modulators. In addition, the CAPSL gene is in the same linkage disequilibrium (LD) block as the IL7R gene and there is well known association between the CAPSL-IL7R locus and type 1 diabetes.
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Synonyms
Calcyphosine-like protein, CAPSL, MGC26610.
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Physical Appearance
CAPSL 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 MAGTARHDRE MAIQAKKKLT TATDPIERLR LQCLARGSAG IKGLGRVFRI MDDDNNRTLD FKEFMKGLND YAVVMEKEEV EELFQRFDKD GNGTIDFNEF LLTLRPPMSR ARKEVIMQAF RKLDKTGDGV ITIEDLREVY NAKHHPKYQN GEWSEEQVFR KFLDNFDSPY DKDGLVTPEE FMNYYAGVSA SIDTDVYFII MMRTAWKL
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 :
CCL28 MouseDescription:
Mucosae-Associated Epithelial Chemokine Mouse Recombinant (CCL28)
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-369Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL28 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.6 kDa. The CCL28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer pH-7.4 and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 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
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.
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Background
What is the molecular weight/Mw of CCL28 MOUSE Protein?
CCL28 MOUSE Protein has a total Mw of 12.6kDa.
What is the source or expression system of CCL28 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL28 MOUSE Protein?
CCL28 MOUSE Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 MOUSE Protein?
Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL28 MOUSE Protein?
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.
What applications can CCL28 MOUSE Protein be used in?
CCL28 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 MOUSE Protein?
The endotoxin level is minimal, CCL28 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CD5L MouseDescription:
CD5 Molecule-Like Mouse Recombinant
CD5 antigen-like, Apoptosis inhibitor expressed by macrophages, Apoptosis inhibitory 6 CT-2, SP-alpha, Cd5l' Aim, Api6.
Product # :
PRO-2243Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CD5L produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 339 amino acids (22-352a.a.) and having a molecular mass of 37.6 kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CD5L is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CD5L protein solution (0.25mg/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
CD5 antigen-like (CD5L) participates in the regulation of the immune system. CD5L functions as an inhibitor of apoptosis. CD5L is expressed in the spleen, lymph node, thymus and bone marrow.
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Synonyms
CD5 antigen-like, Apoptosis inhibitor expressed by macrophages, Apoptosis inhibitory 6 CT-2, SP-alpha, Cd5l' Aim, Api6.
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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
ESPTKVQLVG GAHRCEGRVE VEHNGQWGTV CDDGWDRRDV AVVCRELNCG AVIQTPRGAS YQPPASEQRV LIQGVDCNGT EDTLAQCELN YDVFDCSHEE DAGAQCENPD SDLLFIPEDV RLVDGPGHCQ GRVEVLHQSQ WSTVCKAGWN LQVSKVVCRQ LGCGRALLTY GSCNKSTQGK GPIWMGKMSC SGQEANLRSC LLSRLENNCT HGEDTWMECE DPFELKLVGG DTPCSGRLEV LHKGSWGSVC DDNWGEKEDQ VVCKQLGCGK SLHPSPKTRK IYGPGAGRIW LDDVNCSGKE QSLEFCRHRL WGYHDCTHKE DVEVICTDFD VLEHHHHHH.
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 :
TPMT HumanDescription:
Thiopurine S-methyltransferase Human Recombinant
TPMT, Thiopurine S-methyltransferase, EC 2.1.1.67, Thiopurine methyltransferase.
Product # :
PKA-255Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
TPMT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 245 amino acids (1-245) and having a molecular mass of 28 kDa. Thiopurine S-methyltransferase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml solution containing 20mM Tris 8.0, 0.2mM PMSF and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
TPMT, thiopurine S-methyltransferase, is a cytosolic enzyme that metabolizes thiopurine drugs via S-adenosyl-L-methionine as the S-methyl donor and S-adenosyl-L-homocysteine as a byproduct. TPMT activity exhibits autosomal codominant genetic polymorphism, and patients inheriting TPMT-deficiency are at high risk of potentially fatal hematopoietic toxicity.
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Synonyms
TPMT, Thiopurine S-methyltransferase, EC 2.1.1.67, Thiopurine methyltransferase.
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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
MDGTRTSLDI EEYSDTEVQK NQVLTLEEWQ DKWVNGKTAF HQEQGHQLLK KHLDTFLKGKSGLRVFFPLC GKAVEMKWFA DRGHSVVGVE ISELGIQEFF TEQNLSYSEE PITEIPGTKVFKSSSGNISL YCCSIFDLPR TNIGKFDMIW DRGALVAINP GDRKCYADTM FSLLGKKFQY LLCVLSYDPT KHPGPPFYVP HAEIERLFGK ICNIRRLEKV DAFEERHKSW GIDCLFEKLYLLTEK.
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 :
HAVCR1 Human, HEKDescription:
Hepatitis A Virus Cellular Receptor 1 Human Recombinant, HEK
Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.
Product # :
HAV-223Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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Description
HAVCR1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser21-Thr288) containing a total of 283 amino acids, having a calculated molecular mass of 30.5kDa. HAVCR1 is fused to a 2 aa N-terminal linker, a 2 aa C-terminal linker and a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
HAVCR1 was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% (w/v) Trehalose.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.
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Synonyms
Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. HAVCR1 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
ASSVKVGGEA GPSVTLPCHY SGAVTSMCWN RGSCSLFTCQ NGIVWTNGTH VTYRKDTRYK LLGDLSRRDV SLTIENTAVS DSGVYCCRVE HRGWFNDMKI TVSLEIVPPK VTTTPIVTTV PTVTTVRTST TVPTTTTVPM TTVPTTTVPT TMSIPTTTTV LTTMTVSTTT SVPTTTSIPT TTSVPVTTTV STFVPPMPLP RQNHEPVATS PSSPQPAETH PTTLQGAIRR EPTSSPLYSY TTDGNDTVTE SSDGLWNNNQ TQLFLEHSLL TANTTKLHHH 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.
- View Data Sheet
Name :
CCL12 MouseDescription:
Monocyte Chemotactic Protein-5 Mouse Recombinant (CCL12)
C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.
Product # :
CHM-266Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
MCP-5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 82 amino acids and having a molecular mass of 9.3kDa. The MCP5 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 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.More Info
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Introduction
MCP-5 (CCL12) is a cloned mouse CC chemokine most closely related to human MCP1 (66% amino acid sequence identity in the mature protein). MCP5 is expressed constitutively in the thymus and the lymph nodes. Under inflammatory conditions, moreover CCL12 expression is induced in activated macrophages and mast cells. The mouse MCP1 gene is mapped to the CC chemokine cluster on chromosome 11. Recombinant CCL12 is a potent chemoattractant for monocytes and lymphocytes but not neutrophils. At high concentrations, MCP-5 also chemoattracts eosinophils. CCL12 is a functional ligand for CCR2.
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Synonyms
C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCP5 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 MCP5 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
GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.
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Background
What is the molecular weight/Mw of CCL12 MOUSE Protein?
CCL12 MOUSE Protein has a total Mw of 9.3kDa.
What is the source or expression system of CCL12 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL12 MOUSE Protein?
CCL12 MOUSE Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL12 MOUSE Protein?
Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.
What is the amino acid sequence of CCL12 MOUSE Protein?
GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.
What applications can CCL12 MOUSE Protein be used in?
CCL12 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL12 MOUSE Protein?
The endotoxin level is minimal, CCL12 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.