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1000 results found for “coagulation factors”
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Name :
TGFB3 AntibodyDescription:
Transforming Growth Factor-beta 3 Polyclonal Rabbit Anti Human Antibody
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Product # :
ANT-040Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
lyophilized from 1mg/ml solution in 0.2µm sterile filtered solution in phosphate buffered saline.
More Info
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Introduction
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
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Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
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Stability
Store at 4°C. For long term storage freezes in working aliquots at -20°C. Repeated freezing and thawing is not recommended.
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Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
IgG Anti Human TGFb-3 is developed in rabbit using recombinant Human TGFb-3 produced in plants.
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Applications
To detect Human TGFb-3 by WB analysis this IgG can be used in a dilution of 1/500-1/1000.
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Antigen Amino Acid Sequence
ALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS
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Type
Polyclonal Rabbit Antibody.
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Purification Method
Purified IgG prepared by affinity chromatography on protein G.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NFATC1 AntibodyDescription:
Nuclear factor of activated T-cells cytoplasmic 1, Mouse Anti Human
Nuclear factor of activated T-cells cytoplasmic 1, NFAT transcription complex cytosolic component, NF-ATc1, NFATc1, NF-ATc, NFATc, NFAT2, MGC138448.
Product # :
ANT-436Price :
Quantity :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 0.02% Sodium Azide and 10% Glycerol.
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Introduction
NFATC1 is a component of the nuclear factor of activated T cells DNA-binding transcription complex. This complex consists of at least 2 components: a preexisting cytosolic component that translocates to the nucleus upon T cell receptor (TCR) stimulation, and an inducible nuclear component. Proteins belonging to this family of transcription factors play an essential role in inducible gene transcription during immune response. NFATC1 is an inducible nuclear component. NFATC1 functions as a major molecular target for the immunosuppressive drugs such as cyclosporin A. Different isoforms of NFATC1 may regulate inducible expression of different cytokine genes.
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Synonyms
Nuclear factor of activated T-cells cytoplasmic 1, NFAT transcription complex cytosolic component, NF-ATc1, NFATc1, NF-ATc, NFATc, NFAT2, MGC138448.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human NFATC1 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human NFATC1 amino acids 428-716 purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
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Clone
PAT1C3AT.
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Applications
NFATC1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
NFATC1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
VTN HumanDescription:
Vitronectin Human Recombinant
Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.
Product # :
PRO-2008Price :
Quantity :
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Shipped with Ice Packs
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Description
VTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 482 amino acids (20-478 a.a) and having a molecular mass of 54.7kDa. VTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VTN protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Vitronectin (VTN) which is a part of the pexin family is a cell adhesion and spreading factor found in serum and tissues. VTN interacts with glycosaminoglycans and proteoglycans. VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to numerous serpin serine protease inhibitors. Scientists have been noticed an over expression of VTN, integrins and plasminogen in migrating cells during wound healing.
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Synonyms
Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDQESCKG RCTEGFNVDK KCQCDELCSY YQSCCTDYTA ECKPQVTRGD VFTMPEDEYT VYDDGEEKNN ATVHEQVGGP SLTSDLQAQS KGNPEQTPVL KPEEEAPAPE VGASKPEGID SRPETLHPGR PQPPAEEELC SGKPFDAFTD LKNGSLFAFR GQYCYELDEK AVRPGYPKLI RDVWGIEGPI DAAFTRINCQ GKTYLFKGSQ YWRFEDGVLD PDYPRNISDG FDGIPDNVDA ALALPAHSYS GRERVYFFKG KQYWEYQFQH QPSQEECEGS SLSAVFEHFA MMQRDSWEDI FELLFWGRTS AGTRQPQFIS RDWHGVPGQV DAAMAGRIYI SGMAPRPSLA KKQRFRHRNR KGYRSQRGHS RGRNQNSRRP SRATWLSLFS SEESNLGANN YDDYRMDWLV PATCEPIQSV FFFSGDKYYR VNLRTRRVDT VDPPYPRSIA QYWLGCPAPG HL.
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 :
G CSF MouseDescription:
Granulocyte-Colony Stimulating Factor Mouse Recombinant
CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.
Product # :
CYT-410Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Granulocyte Colony Stimulating Factor Mouse Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 178 amino acids and having a molecular mass of approximately 18.9kDa. G-CSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
G-CSF Lyophilized from 10mM NaCitrate, pH 4.0 and 150mM NaCl.
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 a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 2 x 107IU/mg.More Info
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Introduction
Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.
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Synonyms
CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF 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 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
VPLVTVSAL PPSLPLPRSF LLKSLEQVRK IQASGSVLLE QLCATYKLCH PEELVLLGHS LGIPKASLSG CSSQALQQTQ CLSQLHSGLC LYQGLLQALS GISPALAPTL DLLQLDVANF ATTIWQQMEN LGVAPTVQPT QSAMPAFTSA FQRRAGGVLA ISYLQGFLET ARLALHHLA.
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Background
What is the molecular weight/Mw of G CSF MOUSE Protein?
G CSF MOUSE Protein has a total Mw of 18.9kDa.
What is the source or expression system of G CSF MOUSE Protein?
Escherichia Coli.
What is the Purity of G CSF MOUSE Protein?
G CSF MOUSE Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF MOUSE Protein?
The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a Specific Activity of 2 x 107IU/mg.
What is the amino acid sequence of G CSF MOUSE Protein?
VPLVTVSAL PPSLPLPRSF LLKSLEQVRK IQASGSVLLE QLCATYKLCH PEELVLLGHS LGIPKASLSG CSSQALQQTQ CLSQLHSGLC LYQGLLQALS GISPALAPTL DLLQLDVANF ATTIWQQMEN LGVAPTVQPT QSAMPAFTSA FQRRAGGVLA ISYLQGFLET ARLALHHLA.
What applications can G CSF MOUSE Protein be used in?
G CSF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF MOUSE Protein?
The endotoxin level is minimal, G CSF 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 :
BLyS Human, HisDescription:
B cell Activating Factor Human Recombinant, His Tag
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Product # :
CYT-545Price :
Quantity :
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Shipped with Ice Packs
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- sds-page
Description
BLyS Human Recombinant fused to His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (134-285 a.a.) and having a molecular mass of 21 kDa. BAFF is fused to a 38 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Recombinant His Tag BAFF contains PBS pH-7.4 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Binds to tnfrsf13b/taci and tnfrsf17/bcma. tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. a third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin. -
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
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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 KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL
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Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 21kDa.
What is the source or expression system of BLYS Protein?
Escherichia Coli.
What is the Purity of BLYS Protein?
BLYS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BLYS Protein?
The biological functionality of BLYS Protein will be determined in the future.
What is the amino acid sequence of BLYS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL
What applications can BLYS Protein be used in?
BLYS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BLYS Protein?
The endotoxin level is minimal, BLYS 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 7 Human, YeastDescription:
Interleukin-7 Human Recombinant, Yeast
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Product # :
CYT-298Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-7 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 17.4 kDa. The IL-7 is purified by proprietary chromatographic techniques.
Source
Saccharomyces cerevisiae.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM phosphate buffer.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent stimulation of thymidine uptake by murine pre-B cell line 2E8 is < 0.5 ng/ml, corresponding to a specific activity of > 2 x 106 units/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 Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 -7 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Asp-Cys-Asp-Ile-Glu.
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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 0.418 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-7 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 :
NDUFAF1 HumanDescription:
NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 1 Human Recombinant
Complex I intermediate-associated protein 30, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 1, NDUFAF1, CIA30, CGI-65, CGI65.
Product # :
ENZ-661Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NDUFAF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 326 amino acids (25-327) and having a molecular mass of 37kDa.NDUFAF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NDUFAF1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4 (NDUFAF4) is involved in the compilation of mitochondrial NADH: ubiquinone oxidoreductase complex (complex I). In addition, NDUFAF4 is involved in cell proliferation and survival of hormone-dependent tumor cells. NDUFAF4 may also be a regulator of breast tumor cell invasion. NDUFAF4 gene mutations cause the mitochondrial complex I deficiency.
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Synonyms
Complex I intermediate-associated protein 30, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 1, NDUFAF1, CIA30, CGI-65, CGI65.
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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 MGSYPFLGIR FAEYSSSLQK PVASPGKASS QRKTEGDLQG DHQKEVALDI TSSEEKPDVS FDKAIRDEAI YHFRLLKDEI VDHWRGPEGH PLHEVLLEQA KVVWQFRGKE DLDKWTVTSD KTIGGRSEVF LKMGKNNQSA LLYGTLSSEA PQDGESTRSG YCAMISRIPR GAFERKMSYD WSQFNTLYLR VRGDGRPWMV NIKEDTDFFQ RTNQMYSYFM FTRGGPYWQE VKIPFSKFFF SNRGRIRDVQ HELPLDKISS IGFTLADKVD GPFFLEIDFI GVFTDPAHTE EFAYENSPEL NPRLFK.
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 :
HTF BovineDescription:
Holo Transferrin Bovine
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
Product # :
PRO-510Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bovine Holo Transferrin is a glycoprotein of approximately 80 kDa.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 97.0% as determined by Cellulose Acetate.
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
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Physical Appearance
Sterile Filtered Pink lyophilized (freeze-dried) powder.
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Stability
Lyophilized Bovine HTF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bovine HTF 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 Bovine HTF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
FDA approved Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG, HBc, ALT and Syphilis.Viral inactivation by pasteurization (60°C for 10 hours) has been validated using three different test viruses, with removal of 8-14.5 logs of virus documented. The purification process has also been found to remove significant additional quantities of virus.
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Applications
Bovine Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.
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 :
KLK1 Human, HisDescription:
Kallikrein-1 Human Recombinant, His Tag
KLK1, KLK-1, HK1, HK-1, KLKR, KLK6, Tissue Kallikrein, hKLK1, EC 3.4.21.35, Kidney/pancreas/salivary gland kallikrein, Kallikrein-1.
Product # :
ENZ-690Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Kallikrein-1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 259 amino acids (25-262) and having a molecular mass of 28.7kDa.KLK1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KLK1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikreins are serine protease enzymes having various physiological functions.
Kallikreins are implicated in carcinogenesis and have potenital as novel cancer disease biomarkers. KLK1 is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK1 is functionally conserved in its ability to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen.
Human Kallikrein-1, also called as Kallidinogenase, Kininogenase or Kininogenin, is an active protein enzyme present in saliva, pancreatic juices, and urine that catalyzes the proteolysis of bradykininogen to bradykinin.
Kallikrein-1, which derived from human or porcine, have been used as drugs for a long time, they are mainly used in the treatment f light to medium hypertension and occlusion of cerebral and surrounding blood vessels.
KLK1 demonstrates both trypsin- and chymotrypsin-like selectivities with Tyr/Arg preferred at site P1, Ser/Arg strongly preferred at P1', and Phe/Leu at P2.
rs5517 in the KLK1 gene is considerably connected with hypertension in a Chinese Han population. KLK1 is expressed de novo in endothelial cells and mediates relaxation of human umbilical veins. The K allele of KLK1 promoter and TT genotype of TGF-beta1 are a genetic KLK1 -130 GN and -128 G-C, and the defenselessness factor contributing to progressive renal descent in Taiwanese primary vesicoureteric reflux children.
Induction of KLK1 in carotid arteriosclerosis doesn’t lead to kallikrein-kinins pathway activation. Transgenic rats expressing KLK1 have impaired renal response to acute volume expansion Endothelial cells synthesize and release active form of KLK1on the surface which is important function in maintenance of circulation homeostasis.
KLK1 participates in epidermal desquamation through cleavage of desmoglein 1 and regulation by lympho-epithelial Kazal-type-related inhibitor (LEKTI). -
Synonyms
KLK1, KLK-1, HK1, HK-1, KLKR, KLK6, Tissue Kallikrein, hKLK1, EC 3.4.21.35, Kidney/pancreas/salivary gland kallikrein, Kallikrein-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 MIVGGWECEQ HSQPWQAALY HFSTFQCGGI LVHRQWVLTA AHCISDNYQL WLGRHNLFDD ENTAQFVHVS ESFPHPGFNM SLLENHTRQA DEDYSHDLML LRLTEPADTI TDAVKVVELP TQEPEVGSTC LASGWGSIEP ENFSFPDDLQ CVDLKILPND ECKKVHVQKV TDFMLCVGHL EGGKDTCVGD SGGPLMCDGV LQGVTSWGYV PCGTPNKPSV AVRVLSYVKW IEDTIAENS.
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 :
KLK5 HumanDescription:
Kallikrein-5 Human Recombinant
Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.
Product # :
ENZ-630Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KLK5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (67-293) and having a molecular mass of 27.8kDa.KLK5 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KLK5 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikrein-5 (KLK5) is a member of the serine protease family of proteolytic enzymes. KLK5 is expressed in various tissues including the salivary gland, stomach, uterus, lung, thymus, prostate, colon, brain, thyroid, and trachea. KLK5 expression is up-regulated by estrogens and progestins. KLK5 is secreted and may be involved in desquamation in the epidermis. Kallikreins which are a subgroup of serine proteases, have distinct physiological functions. Many kallikreins are associated with carcinogenesis and some have potential as novel cancer and other disease biomarkers. The KLK5 gene is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19.
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Synonyms
Kallikrein-5, Kallikrein-like protein 2, KLK-L2, Stratum corneum tryptic enzyme, KLK5, SCTE, UNQ570/PRO1132, KLKL2.
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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 MGSHMIINGS DCDMHTQPWQ AALLLRPNQL YCGAVLVHPQ WLLTAAHCRK KVFRVRLGHY SLSPVYESGQ QMFQGVKSIP HPGYSHPGHS NDLMLIKLNR RIRPTKDVRP INVSSHCPSA GTKCLVSGWG TTKSPQVHFP KVLQCLNISV LSQKRCEDAY PRQIDDTMFC AGDKAGRDSC QGDSGGPVVC NGSLQGLVSW GDYPCARPNR PGVYTNLCKF TKWIQETIQA NS.
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 :
CDC25A HumanDescription:
Cell Division Cycle 25A Human Recombinant
M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.
Product # :
ENZ-091Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDC25A 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 560 amino acids (1-524 a.a.) and having a molecular mass of 63.2kDa. The CDC25A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDC25A solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 20% glycerol, 0.2M NaCl and 1mM EDTA.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
M-phase inducer phosphatase 1 (CDC25A) belongs to the CDC25 family of phosphatases. CDC25A is essential for progression from G1 to the S phase of the cell cycle. CDC25A activates the cyclin-dependent kinase CDC2 by eliminating 2 phosphate groups. CDC25A is specifically degraded in reaction to DNA damage, which inhibits cells with chromosomal abnormalities from progressing in the course of cell division. CDC25A is an oncogene, though its exact function in oncogenesis has not been determined.
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Synonyms
M-phase inducer phosphatase 1, Dual specificity phosphatase Cdc25A, CDC25A, CDC25A2.
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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 KDRWGSMELG PEPPHRRRLL FACSPPPASQ PVVKALFGAS AAGGLSPVTN LTVTMDQLQG LGSDYEQPLE VKNNSNLQRM GSSESTDSGF CLDSPGPLDS KENLENPMRR IHSLPQKLLG CSPALKRSHS DSLDHDIFQL IDPDENKENE AFEFKKPVRP VSRGCLHSHG LQEGKDLFTQ RQNSAPARML SSNERDSSEP GNFIPLFTPQ SPVTATLSDE DDGFVDLLDG ENLKNEEETP SCMASLWTAP LVMRTTNLDN RCKLFDSPSL CSSSTRSVLK RPERSQEESP PGSTKRRKSM SGASPKESTN PEKAHETLHQ SLSLASSPKG TIENILDNDP RDLIGDFSKG YLFHTVAGKH QDLKYISPEI MASVLNGKFA NLIKEFVIID CRYPYEYEGG HIKGAVNLHM EEEVEDFLLK KPIVPTDGKR VIVVFHCEFS SERGPRMCRY VRERDRLGNE YPKLHYPELY VLKGGYKEFF MKCQSYCEPP SYRPMHHEDF KEDLKKFRTK SRTWAGEKSK REMYSRLKKL.
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 :
PRCP HumanDescription:
Prolylcarboxypeptidase Human Recombinant
Angiotensinase-C, PRCP, Proline Carboxypeptidase.
Product # :
ENZ-1178Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PRCP Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (22-496 a.a) containing a total of 481 amino acids, having a molecular mass of 54.3 kDa. PRCP is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The PRCP solution (0.25mg/ml) contains 30% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 3,000 pmol/min/μg, and is defined as the amount of enzyme that converts 1pmole of Z-ProAla-OH/min. at pH-4 at 25˚C.
More Info
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Introduction
PRCP is a plasma protein which takes part in the cleavage of C-terminal amino acids linked to proline in proteinfor example angiotensin-2 & 3 at acidic pHenvironment rather than at neutral pHwhich exhibit less activity. This cleavage is important since Angiotensin-2 takes part in regulation of blood pressure & electrolyte balance which is essential to hypertension.
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Synonyms
Angiotensinase-C, PRCP, Proline Carboxypeptidase.
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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
LRPALRALGS LHLPTNPTSL PAVAKNYSVL YFQQKVDHFG FNTVKTFNQR YLVADKYWKK NGGSILFYTG NEGDIIWFCN NTGFMWDVAE ELKAMLVFAE HRYYGESLPF GDNSFKDSRH LNFLTSEQAL ADFAELIKHL KRTIPGAENQ PVIAIGGSYG GMLAAWFRMK YPHMVVGALA ASAPIWQFED LVPCGVFMKI VTTDFRKSGP HCSESIHRSW DAINRLSNTG SGLQWLTGALHLCSPLTSQD IQHLKDWISE TWVNLAMVDY PYASNFLQPL PAWPIKVVCQ YLKNPNVSDS LLLQNIFQAL NVYYNYSGQV KCLNISETAT SSLGTLGWSY QACTEVVMPF CTNGVDDMFE PHSWNLKELS DDCFQQWGVR PRPSWITTMY GGKNISSHTN IVFSNGELDP WSGGGVTKDI TDTLVAVTIS EGAHHLDLRT KNALDPMSVL LARSLEVRHM KNWIRDFYDS AGKQ 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 :
Leptin N82K Human, PEGDescription:
Leptin N82K Human Recombinant, Pegylated
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1107Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pegylated Leptin N82K Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Pegylated Leptin N82K Human Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3 Having 35-40% protein.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Pegylated Leptin Human is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated Leptin in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo Pegylated Leptin has profound weight reducing effect (as compared to the non-pegylated recombinant human leptin), resulting mainly from reduced food intake.
More Info
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Introduction
Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pegylated Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pegylated Leptin N82K 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 Pegylated Leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CEBPB AntibodyDescription:
CCAAT/enhancer-binding protein beta, Mouse Anti Human
CCAAT/enhancer-binding protein beta, C/EBP beta, Liver activator protein, Nuclear factor NF-IL6, Transcription factor 5, TCF-5, CEBPB, LAP, TCF5, CRP2, IL6DBP, MGC32080.
Product # :
ANT-406Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
CEBPB is an intronless gene and its protein is a bZIP transcription factor which can bind as a homodimer to certain DNA regulatory regions. CEBPB can also form heterodimers with the related proteins CEBP-alpha, CEBP-delta, and CEBP-gamma. CEBPB is important in the regulation of genes involved in immune and inflammatory responses and has been shown to bind to the IL-1 response element in the IL-6 gene, as well as to regulatory regions of several acute-phase and cytokine genes. In addition, CEBPB can bind the promoter and upstream element and stimulate the expression of the collagen type I gene.
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Synonyms
CCAAT/enhancer-binding protein beta, C/EBP beta, Liver activator protein, Nuclear factor NF-IL6, Transcription factor 5, TCF-5, CEBPB, LAP, TCF5, CRP2, IL6DBP, MGC32080.
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Immunogen
Anti-human CEBPB mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CEBPB amino acids 1-271 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P47A1AT.
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Applications
CEBPB antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 2,000. Recommended starting dilution is 1:1,000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
CEBPB antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TSNAX HumanDescription:
Translin-Associated Factor X Human Recombinant
TRAX, Translin-associated protein X, Translin-associated factor X.
Product # :
PRO-1292Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TSNAX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (1-290 a.a.) and having a molecular mass of 35kDa.TSNAX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TSNAX protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TSNAX is a member of translin family. TSNAX particularly interacts with translin, a DNA-binding protein that binds consensus sequences at breakpoint junctions of chromosomal translocations. TSNAX works in combination with TSN as an endonuclease involves in the activation of the RNA-induced silencing complex (RISC). TSNAX has bipartite nuclear targeting sequences that afford nuclear transport for translin, which lacks any nuclear targeting motifs.
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Synonyms
TRAX, Translin-associated protein X, Translin-associated factor X.
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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 MGSMSNKEGS GGFRKRKHDN FPHNQRREGK DVNSSSPVML AFKSFQQELD ARHDKYERLV KLSRDITVES KRTIFLLHRI TSAPDMEDIL TESEIKLDGV RQKIFQVAQE LSGEDMHQFH RAITTGLQEY VEAVSFQHFI KTRSLISMDE INKQLIFTTE DNGKENKTPS SDAQDKQFGT WRLRVTPVDY LLGVADLTGE LMRMCINSVG NGDIDTPFEV SQFLRQVYDG FSFIGNTGPY EVSKKLYTLK QSLAKVENAC YALKVRGSEI PKHMLADVFS VKTEMIDQEE GIS.
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 :
NEFL HumanDescription:
Neurofilament Light Human Recombinant
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
Product # :
PRO-2584Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
NEFL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (2-543 a.a) containing 551 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 62.5kDa (calculated).
Source
Escherichia Coli.
Formulation
NEFL filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 15mM Tris and 85mM Glycine, pH 8.5.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NEFL or Neurofilament light polypeptide is a protein that is encoded through the NEFL gene. NEFL is correlated to a disease called Charcot–Marie–Tooth. The protein’s light subunit is determined by immunoassays in the plasma and cerebrospinal fluid, if present, it can indicate on axonal damage in neurological diseases. By doing so, NEFL can act as a marker for Huntington's disease, Amyotrophic Lateral Sclerosis and multiple sclerosis.
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Synonyms
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
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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 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
MKHHHHHHAS SFSYEPYYST SYKRRYVETP RVHISSVRSG YSTARSAYSS YSAPVSSSLS VRRSYSSSSG SLMPSLENLD LSQVAAISND LKSIRTQEKA QLQDLNDRFA SFIERVHELE QQNKVLEAEL LVLRQKHSEP SRFRALYEQE IRDLRLAAED ATNEKQALQG EREGLEETLR NLQARYEEEV LSREDAEGRL MEARKGADEA ALARAELEKR IDSLMDEISF LKKVHEEEIA ELQAQIQYAQ ISVEMDVTKP DLSAALKDIR AQYEKLAAKN MQNAEEWFKS RFTVLTESAA KNTDAVRAAK DEVSESRRLL KAKTLEIEAC RGMNEALEKQ LQELEDKQNA DISAMQDTIN KLENELRTTK SEMARYLKEY QDLLNVKMAL DIEIAAYRKL LEGEETRLSF TSVGSITSGY SQSSQVFGRS AYGGLQTSSY LMSTRSFPSY YTSHVQEEQI EVEETIEAAK AEEAKDEPPS EGEAEEEEKD KEEAEEEEAA EEEEAAKEES EEAKEEEEGG EGEEGEETKE AEEEEKKVEG AGEEQAAKKK D.
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 :
ARL11 HumanDescription:
ADP-Ribosylation Factor-Like 11 Human Recombinant
ADP-ribosylation factor-like protein 11, ADP-ribosylation factor-like tumor suppressor protein 1, ARL11, ARLTS1.
Product # :
PRO-884Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ARL11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-196 a.a.) and having a molecular mass of 23.6kDa.ARL11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARL11 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT,30% glycerol, 100mM NaCl and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ARL11 (ADP-ribosylation factor-like protein 11) belongs to the ARF family of the Ras superfamily of small GTPases which are known to be involved in multiple regulatory pathways altered in human carcinogenesis. ARFs are highly conserved guanine nucleotide binding proteins which enhance the ADP-ribosyltransferase activity of choleratoxin. ARFs are important in eukaryotic vesicular trafficking pathways and they have a vital role in the activation of phospholipase D (PC-PLD). ARL11 is assumed to act as a tumor suppressor which may have a role in the regulation of apoptosis.
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Synonyms
ADP-ribosylation factor-like protein 11, ADP-ribosylation factor-like tumor suppressor protein 1, ARL11, ARLTS1.
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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 MGSVNSRGHK AEAQVVMMGL DSAGKTTLLY KLKGHQLVET LPTVGFNVEP LKAPGHVSLT LWDVGGQAPL RASWKDYLEG TDILVYVLDS TDEARLPESA AELTEVLNDP NMAGVPFLVL ANKQEAPDAL PLLKIRNRLS LERFQDHCWE LRGCSALTGE GLPEALQSLW SLLKSRSCMC LQARAHGAER GDSKRS.
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 :
ANGPTL4 HumanDescription:
Angiopoietin-like Protein 4 Human Recombinant
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
Product # :
CYT-249Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The ANGPTL4 Human Recombinant is manufactured with N-terminal fusion of His Tag. The Angiopoietin-like Protein 4 His -Tagged Fusion Protein is 25 kDa protein containing 204 amino acid residues of the Angiopoietin-like Protein 4 and 16 additional amino acid residues - His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
FIAF (fasting-induced adipose factor) a.k.a ANGPTL4 or PGAR or HFARP is an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. ANGPTL4 is found in human and mouse blood plasma both as a native protein and in a truncated form. In human white adipose tissue and SGBS adipocytes, only the native form of ANGPTL4 could be detected, whereas in mice the differentiation of mouse 3T3-L1 adipocytes is associated with the production of truncated ANGPTL4. However, the truncated ANGPTL4 is produced by human liver. In human blood plasma FIAF is mainly presented in a truncated form (FIAF-S2), whose levels treatment increases (as shown by experimental data). There is an inter individual variation in ANGPTL4 levels of both the truncated and the native form, however those levels were not influenced by prolonged semistarvation and are not associated with body mass index.
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Synonyms
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Angiopoietin-like Protein 4 Human recombinant at -20°C. Aliquot the ANGPTL4 after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted ANGPTL4 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
Add 0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
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Amino Acid Sequence
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.
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Background
Angiopoietin-like Protein 4 Human Recombinant: A Promising Therapeutic Approach for Metabolic Disorders
Abstract:
Angiopoietin-like protein 4 (ANGPTL4) is a multifunctional protein involved in the regulation of lipid metabolism and energy homeostasis. It has emerged as a potential therapeutic target for metabolic disorders, including obesity, dyslipidemia, and insulin resistance. The availability of human recombinant ANGPTL4 protein has provided researchers with a valuable tool to investigate its biological functions and explore its therapeutic potential. This concise review provides an overview of the role of ANGPTL4 in metabolic regulation and discusses the potential of ANGPTL4 human recombinant protein as a therapeutic intervention.Introduction:
Metabolic disorders are a global health challenge with significant implications for cardiovascular health. ANGPTL4, a member of the angiopoietin-like protein family, has gained attention for its role in lipid metabolism and energy balance. ANGPTL4 influences the uptake, storage, and utilization of lipids, as well as glucose metabolism, making it an attractive target for therapeutic interventions.Mechanisms of ANGPTL4 Action:
ANGPTL4 exerts its effects through multiple mechanisms. It inhibits lipoprotein lipase (LPL) activity, reducing the hydrolysis of triglycerides and leading to elevated plasma triglyceride levels. ANGPTL4 also promotes adipose tissue lipolysis, facilitating the release of fatty acids for energy utilization. Moreover, ANGPTL4 affects glucose metabolism by modulating insulin signaling and glucose uptake in various tissues.Role of ANGPTL4 in Metabolic Regulation:
ANGPTL4 plays a critical role in lipid and glucose metabolism. It regulates plasma lipid levels by modulating LPL activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL4 also influences energy homeostasis by promoting lipid mobilization from adipocytes and regulating fatty acid oxidation. Additionally, ANGPTL4 impacts glucose metabolism by modulating insulin sensitivity and glucose uptake in skeletal muscle and adipose tissue.Therapeutic Potential of ANGPTL4 Human Recombinant Protein:
The availability of ANGPTL4 human recombinant protein opens new avenues for therapeutic interventions targeting metabolic disorders. Administration of ANGPTL4 recombinant protein or modulation of ANGPTL4 activity offers potential strategies to improve lipid profiles, reduce adiposity, and enhance insulin sensitivity. Preclinical studies have shown promising results, demonstrating the potential of ANGPTL4 as a therapeutic target for metabolic disorders.Conclusion:
ANGPTL4 represents a promising target for therapeutic interventions in metabolic disorders. Its involvement in the regulation of lipid and glucose metabolism makes it an attractive candidate for the development of novel treatment approaches. The availability of ANGPTL4 human recombinant protein enables further exploration of its therapeutic potential and may contribute to the development of effective interventions for metabolic disorders.What is the molecular weight/Mw of ANGPTL4 Protein?
ANGPTL4 Protein has a total Mw of 25kDa.
What is the source or expression system of ANGPTL4 Protein?
Escherichia Coli.
What is the Purity of ANGPTL4 Protein?
ANGPTL4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL4 Protein?
The biological functionality of ANGPTL4 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL4 Protein?
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.
What applications can ANGPTL4 Protein be used in?
ANGPTL4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL4 Protein?
The endotoxin level is minimal, ANGPTL4 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 :
LGALS7 Human, HisDescription:
Galectin-7 Human Recombinant, His Tag
Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.
Product # :
CYT-617Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- SDS-PAGE
Description
Galectin-7 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids (1-136 a.a.) and having a molecular mass of 17.2kDa. The Galectin-7 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-7 solution (1 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
SDS-PAGE
More Info
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Introduction
Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Human Galectin-7 belongs to the prototypical Galectins containing a single CRD, which is initially identified in human epidermis as a monomer. The Galectin-7 expression is induced by tumor suppressor protein p53 and associated with apoptosis. Galectin-7 is a pro-apoptotic protein which functions intracellularlly upstream of JNK activation and mitochondrial cytochrome c release. The correlation of Galectin-7 with the UV-induced apoptosis of keratinocytes presents a critical mechanism in the maintenance of epidermal homeostasis. Human Galectin-7 is localized in both nucleus and cytoplasm.
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Synonyms
Galectin-7, Gal-7, HKL-14, PI7, p53-induced gene 1 protein, LGALS7, PIG1, LGALS7B, GAL7, LGALS7A.
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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 MSNVPHKSSL PEGIRPGTVL RIRGLVPPNA SRFHVNLLCG EEQGSDAALH FNPRLDTSEV VFNSKEQGSW GREERGPGVP FQRGQPFEVL IIASDDGFKA VVGDAQYHHF RHRLPLARVR LVEVGGDVQL DSVRIF.
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Background
What is the molecular weight/Mw of LGALS7 HUMAN, HIS Protein?
LGALS7 HUMAN, HIS Protein has a total Mw of 17.2kDa.
What is the source or expression system of LGALS7 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of LGALS7 HUMAN, HIS Protein?
LGALS7 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS7 HUMAN, HIS Protein?
The biological functionality of LGALS7 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of LGALS7 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MSNVPHKSSL PEGIRPGTVL RIRGLVPPNA SRFHVNLLCG EEQGSDAALH FNPRLDTSEV VFNSKEQGSW GREERGPGVP FQRGQPFEVL IIASDDGFKA VVGDAQYHHF RHRLPLARVR LVEVGGDVQL DSVRIF.
What applications can LGALS7 HUMAN, HIS Protein be used in?
LGALS7 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS7 HUMAN, HIS Protein?
The endotoxin level is minimal, LGALS7 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
C-JUN HumanDescription:
Jun Proto-Oncogene Human Recombinant
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
Product # :
PKA-323Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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- biological activity
- More Info
Description
C-JUN amino acids 1-81 produced in E.coli, is a non-glycosylated, polypeptide chain having a molecular mass of 52 kDa.C-JUN is a maltose binding protein (MBP) fusion protein with an amino-terminal polyhistidine tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
C-JUN is supplied as lyophilized powder containing no additives.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
C-Jun is phosphorylatable in vitro, using either recombinant active JNK1 or JNK2, or with JNK immunoprecipitated from stimulated cells. This phosphorylation can be monitored by Western blot analysis using an antibody directed to c-Jun [pS73], in conjunction with chemiluminescence detection methods. Optimization of the cell stimulation protocol, cell lysis procedure, and reaction conditions may be required for each specific application.More Info
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Introduction
C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.
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Synonyms
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Solubility
It is recommended to centrifuge the vial prior to opening in order to bring the contents to the bottom. The reconstitution of the lyophilized c-Jun is recommended in 40mM Tris, pH 7.5, to a concentration of 0.2-1.0 mg/ml.
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Note
Kinase activity may vary depending on the substrate and reaction conditions.
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 :
L-AsparaginaseDescription:
L-Asparaginase
Product # :
ENZ-287Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
- More Info
Description
L-asparaginase was purified from E.coli ASI.357.
Source
Escherichia Coli.
Formulation
The enzyme was lyophilized with no additives.
Purity
Greater than 96.0% as determined by SDS-PAGE.
Biological Activity
One IU of L- Asparaginase is defined as that amount of enzyme required to generate 1 µmol of ammonia per minute at pH 7.3 and 37°C.
More Info
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Introduction
L-Asparaginase is an enzyme that depletes L-Asparagine "an important nutrient for cancer cells" resulting in cancer/tumor cell starvation. L-asparaginase is an anti-tumor agent derived from E.coli.,which can inhibit the growth of malignant cells. It is used mainly for the induction of remission in acute lymphoblastic leukaemia. Because of the lymph node origin of malignant B cells in Multiple Myeloma, L-Asparagine is an essential amino acid for their cell metabolism, and, consequently, L-Asparaginase may be of value in managing the disease.
The rationale behind asparaginase is that it takes advantage of the fact that ALL cellsare unable to synthesize the non-essential amino acidasparaginewhereas normal cells are able to make their own asparagine. These leukemic cells depend on circulating asparagine. Asparaginase however catalyzes the conversion of L-asparagine to aspartic acidand ammonia. This deprives the leukemic cell of circulating asparagine. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized L-Asparaginase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution L-Asparaginase 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 L-Asparaginase in 18M-cm H2O at 1mg/ml.
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Background
L-Asparaginase Enzyme: Unraveling Its Therapeutic Potential in Cancer Treatment
Abstract: L-Asparaginase is an enzyme that plays a crucial role in cancer therapy by depleting the levels of asparagine in the blood, thereby inhibiting the growth of cancer cells.
This research paper provides a comprehensive analysis of L-Asparaginase, including its biochemical properties, mechanisms of action, therapeutic applications, and clinical implications.
The paper explores the significance of L-Asparaginase as a key enzyme in cancer treatment and highlights its potential for improving patient outcomes.
- Introduction L-Asparaginase is an enzyme widely used in cancer therapy, particularly in the treatment of acute lymphoblastic leukemia (ALL). This section introduces L-Asparaginase and its role in cancer treatment, emphasizing its importance in medical research and clinical practice.
- Biochemical Properties of L-Asparaginase L-Asparaginase belongs to the class of enzymes known as hydrolases and catalyzes the hydrolysis of asparagine to aspartic acid and ammonia. This section discusses the biochemical properties of L-Asparaginase, including its structure, catalytic mechanism, and factors influencing its activity and stability.
- Mechanisms of Action L-Asparaginase exerts its anti-cancer effects by depleting circulating asparagine, an essential amino acid for cancer cell survival. This section delves into the mechanisms of action of L-Asparaginase, including its ability to selectively target cancer cells and induce metabolic stress, leading to cell death. The impact of asparagine deprivation on cancer cell metabolism and survival is also explored.
- Therapeutic Applications of L-Asparaginase L-Asparaginase has demonstrated therapeutic efficacy in the treatment of various malignancies, including ALL and certain solid tumors. This section provides an overview of the therapeutic applications of L-Asparaginase, highlighting its use as a first-line treatment in ALL and its potential in other cancer types. The challenges and limitations associated with L-Asparaginase therapy are also discussed.
- Clinical Implications and Future Perspectives L-Asparaginase therapy has shown promising results in improving patient outcomes, but it is not without side effects and challenges. This section discusses the clinical implications of L-Asparaginase treatment, including its impact on patient survival, toxicity profile, and the development of resistance. Additionally, the future prospects of L-Asparaginase therapy, such as the development of novel formulations and combination strategies, are explored.
- Conclusion L-Asparaginase is a vital enzyme in cancer treatment, particularly in the management of ALL. This research paper has provided a comprehensive analysis of L-Asparaginase, highlighting its biochemical properties, mechanisms of action, therapeutic applications, and clinical implications. Further research on L-Asparaginase and its optimization in cancer therapy will enhance our understanding and pave the way for improved treatments.
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Unit Definition
One unit of enzyme catalyzes hydrolyzation of 10 nanomoles of dUTP to dUMP in one hour at 85 Centigrade.
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Specific Activity
250IU/mg.
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 :
HHEX HumanDescription:
Hematopoietically Expressed Homeobox Human Recombinant
Hematopoietically Expressed Homeobox, Hematopoietically-Expressed Homeobox Protein HHEX, Homeobox Hematopoietically Expressed, Proline-Rich Homeodomain-Containing Transcription Factor, Homeobox Protein PRH, Homeobox Protein HEX, HOX11L-PEN, PRHX, HMPH, PRH, HEX.
Product # :
PRO-1624Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HHEX Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-270) and having a molecular mass of 32.4kDa. HHEX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HHEX solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
The homeobox protein family of transcription factors has many members that take part in developmental processes such as HHEX. HHEX is known to interact with Promyelocytic leukemia protein and expression in specific hematopoietic lines indicates that this protein is involved in hematopoietic differentiation.
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Synonyms
Hematopoietically Expressed Homeobox, Hematopoietically-Expressed Homeobox Protein HHEX, Homeobox Hematopoietically Expressed, Proline-Rich Homeodomain-Containing Transcription Factor, Homeobox Protein PRH, Homeobox Protein HEX, HOX11L-PEN, PRHX, HMPH, PRH, HEX.
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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 MGSMQYPHPG PAAGAVGVPL YAPTPLLQPA HPTPFYIEDI LGRGPAAPTP APTLPSPNSS FTSLVSPYRT PVYEPTPIHP AFSHHSAAAL AAAYGPGGFG GPLYPFPRTV NDYTHALLRH DPLGKPLLWS PFLQRPLHKR KGGQVRFSND QTIELEKKFE TQKYLSPPER KRLAKMLQLS ERQVKTWFQN RRAKWRRLKQ ENPQSNKKEE LESLDSSCDQ RQDLPSEQNK GASLDSSQCS PSPASQEDLE SEISEDSDQE VDIEGDKSYF NAG
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 :
SDHAF1 HumanDescription:
Succinate Dehydrogenase Complex Assembly Factor 1 Human Recombinant
Succinate Dehydrogenase Complex Assembly Factor 1, LYR Motif-Containing Protein 8, LYR Motif Containing 8, SDH Assembly Factor 1, LYRM8, Succinate Dehydrogenase Assembly Factor 1, Mitochondrial, Succinate dehydrogenase assembly factor 1, mitochondrial.
Product # :
PRO-2123Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
- purity
- More Info
Description
SDHAF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 15.2kDa. SDHAF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SDHAF1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol, 2mM DTT and 0.1mM PMSF.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Succinate dehydrogenase assembly factor 1 (SDHAF1) is a member of the complex I LYR family. SDHAF1 plays an important role in succinate dehydrogenase complex (SDH) assembly, a complex which is involved in complex II of the mitochondrial electron transport chain. SDHAF1 functions through taking part in mitochondrial biosynthesis of iron-sulfur centers for complex II.
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Synonyms
Succinate Dehydrogenase Complex Assembly Factor 1, LYR Motif-Containing Protein 8, LYR Motif Containing 8, SDH Assembly Factor 1, LYRM8, Succinate Dehydrogenase Assembly Factor 1, Mitochondrial, Succinate dehydrogenase assembly factor 1, mitochondrial.
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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 MGSMSRHSRL QRQVLSLYRD LLRAGRGKPG AEARVRAEFR QHAGLPRSDV LRIEYLYRRG RRQLQLLRSG HATAMGAFVR PRAPTGEPGG VGSQPDDGDS PRNPHDSTGA PETRPDGR.
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 :
IGFBP5 HumanDescription:
Insulin-Like Growth Factor Binding Protein-5 Human Recombinant
IGFBP-5, IBP-5, IGF-binding protein 5.
Product # :
CYT-464Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IGFBP5 Human Recombinant produced in E.Coli is non-glycosylated homodimer containing 2x252 amino acids and having a molecular mass of 28.6kDa. IGFBP5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IBP-5 was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium Citrate pH-3.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by its ability to inhibit IGF-II induced proliferation of MCF-7. The expected ED50 for this effect is < 0.4µg/ml, corresponding to a specific activity of > 2500 IU/mg in the presence of 15ng/ml of rHuIGF-II.More Info
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Introduction
IGFBP5 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
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Synonyms
IGFBP-5, IBP-5, IGF-binding protein 5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IBP5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGFBP 5 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 Insulin-Like Growth Factor Binding Protein-5 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
LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE.
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Background
What is the molecular weight/Mw of IGFBP5 HUMAN Protein?
IGFBP5 HUMAN Protein has a total Mw of 28.6kDa.
What is the source or expression system of IGFBP5 HUMAN Protein?
Escherichia Coli.
What is the Purity of IGFBP5 HUMAN Protein?
IGFBP5 HUMAN Protein is >96% pure as determined by SDS-PAGE.
What is the Biological Activity of IGFBP5 HUMAN Protein?
The ED50, calculated by its ability to inhibit IGF-II induced proliferation of MCF-7. The expected ED50 for this effect is < 0.4µg/ml, corresponding to a specific activity of > 2500 IU/mg in the presence of 15ng/ml of rHuIGF-II.
What is the amino acid sequence of IGFBP5 HUMAN Protein?
LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE.
What applications can IGFBP5 HUMAN Protein be used in?
IGFBP5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGFBP5 HUMAN Protein?
The endotoxin level is minimal, IGFBP5 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.