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1000 results found for “Anti Human Cytokine”
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Name :
IL31 Canine, HisDescription:
Interleukin-31 Canine Recombinant, His Tag
IL-31, Interleukin 31, IL31.
Product # :
CYT-1016Price :
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Description
IL31 Canine Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids (24-159a.a.) and having a molecular mass of 16.1kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL31 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL31 Canine protein solution (1mg/ml) containing 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
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
IL-31, Interleukin 31, IL31.
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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. Please avoid freeze thaw cycles.
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Amino Acid Sequence
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQHHHH HH.
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 :
AICDA AntibodyDescription:
Activation-induced cytidine deaminase, Mouse Anti Human
Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.
Product # :
ANT-411Price :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
AICDA is an RNA-editing deaminase which belongs to the cytidine deaminase family. AICDA is involved in somatic hypermutation, gene conversion, and class-switch recombination of immunoglobulin genes. Defects in the AICDA gene are the cause of autosomal recessive hyper-IgM immunodeficiency syndrome type 2 (HIGM2).
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Synonyms
Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.
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Immunogen
Anti-human AICDA mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human AICDA amino acids 1-54 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
P2D3AT.
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Applications
AICDA 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 ~ 1,000. Recommended starting dilution is 1:500.
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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
AICDA 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 :
Resistin Human, HisDescription:
Resistin Human Recombinant, His Tag
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Product # :
CYT-256Price :
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Description
Resistin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing a 92 amino acids fragment (17-108) of the mature Human Resistin, having a total molecular mass of 14.23kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Resistin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Resistin protein solution is supplied in 20mM Tris-HCl pH 8.0, 5mM EDTA and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression. -
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
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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.Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ANGPTL3 (17-460) HumanDescription:
Angiopoietin-like Protein 3 (17-460 a.a.) Human Recombinant
Angiopoietin Like 3, Angiopoietin 5, ANGPT5, ANG-5, Angiopoietin-Related Protein 3 , Angiopoietin-Like Protein 3, Angiopoietin-Like 3, Angiopoietin-5, FHBL2, ANL3.
Product # :
CYT-986Price :
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Shipped with Ice Packs
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Description
ANGPTL3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 453 amino acids (17-460 a.a.) and having a molecular mass of 52.9kDa (Migrates at 25-70kDa on SDS-PAGE under reducing conditions). ANGPTL3 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ANGPTL3 protein solution (0.25mg/ml) contains Buffered Saline (pH 7.4),30% glycerol And 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.
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Synonyms
Angiopoietin Like 3, Angiopoietin 5, ANGPT5, ANG-5, Angiopoietin-Related Protein 3 , Angiopoietin-Like Protein 3, Angiopoietin-Like 3, Angiopoietin-5, FHBL2, ANL3.
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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
ADPSRIDQDN SSFDSLSPEP KSRFAMLDDV KILANGLLQL GHGLKDFVHK TKGQINDIFQ KLNIFDQSFY DLSLQTSEIK EEEKELRRTT YKLQVKNEEV KNMSLELNSK LESLLEEKIL LQQKVKYLEE QLTNLIQNQP ETPEHPEVTS LKTFVEKQDN SIKDLLQTVE DQYKQLNQQH SQIKEIENQL RRTSIQEPTE ISLSSKPRAP RTTPFLQLNE IRNVKHDGIP AECTTIYNRG EHTSGMYAIR PSNSQVFHVY CDVISGSPWT LIQHRIDGSQ NFNETWENYK YGFGRLDGEF WLGLEKIYSI VKQSNYVLRI ELEDWKDNKH YIEYSFYLGN HETNYTLHLV AITGNVPNAI PENKDLVFST WDHKAKGHFN CPEGYSGGWW WHDECGENNL NGKYNKPRAK SKPERRRGLS WKSQNGRLYS IKSTKMLIHP TDSESFEHHH HHH.
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Background
What is the molecular weight/Mw of ANGPTL3 Protein?
ANGPTL3 Protein has a total Mw of 52.9kDa.
What is the source or expression system of ANGPTL3 Protein?
Sf9, Baculovirus cells.
What is the Purity of ANGPTL3 Protein?
ANGPTL3 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL3 Protein?
The biological functionality of ANGPTL3 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL3 Protein?
ADPSRIDQDN SSFDSLSPEP KSRFAMLDDV KILANGLLQL GHGLKDFVHK TKGQINDIFQ KLNIFDQSFY DLSLQTSEIK EEEKELRRTT YKLQVKNEEV KNMSLELNSK LESLLEEKIL LQQKVKYLEE QLTNLIQNQP ETPEHPEVTS LKTFVEKQDN SIKDLLQTVE DQYKQLNQQH SQIKEIENQL RRTSIQEPTE ISLSSKPRAP RTTPFLQLNE IRNVKHDGIP AECTTIYNRG EHTSGMYAIR PSNSQVFHVY CDVISGSPWT LIQHRIDGSQ NFNETWENYK YGFGRLDGEF WLGLEKIYSI VKQSNYVLRI ELEDWKDNKH YIEYSFYLGN HETNYTLHLV AITGNVPNAI PENKDLVFST WDHKAKGHFN CPEGYSGGWW WHDECGENNL NGKYNKPRAK SKPERRRGLS WKSQNGRLYS IKSTKMLIHP TDSESFEHHH HHH.
What applications can ANGPTL3 Protein be used in?
ANGPTL3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL3 Protein?
The endotoxin level is minimal, ANGPTL3 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 :
TNF a Rat, HisDescription:
Tumor Necrosis Factor-alpha Rat Recombinant, His Tag
Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.
Product # :
CYT-900Price :
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Shipped with Ice Packs
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Description
TNF a Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (80-235a.a.) and having a molecular mass of 19.9kDa.TNF a is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNF a protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer. -
Synonyms
Tumor Necrosis Factor-alpha, TNF a His, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, N-terminal fragment, NTF, Intracellular domain 1, Intracellular domain 2, ICD2, C-domain 1, C-domain 2, Tumor necrosis factor, soluble form, Tnfa, Tnfsf2, RATTNF, Tnfa.
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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 MGSHMLRSSS QNSSDKPVAH VVANHQAEEQ LEWLSQRANA LLANGMDLKD NQLVVPADGL YLIYSQVLFK GQGCPDYVLL THTVSRFAIS YQEKVSLLSA IKSPCPKDTP EGAELKPWYE PMYLGGVFQL EKGDLLSAEV NLPKYLDITE SGQVYFGVIA L.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 13 Rhesus MacaqueDescription:
Interleukin-13 Rhesus Macaque Recombinant
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
Product # :
CYT-175Price :
Quantity :
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Shipped at Room temp
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Description
IL 13 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 114 amino acids and having a molecular mass of 12.6kDa.The IL 13 Rhesus Macaque is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 containing 3% trehalose.
Purity
Greater than 98.0% as determined by SDS-PAGE and HPLC analyses.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was < 5ng/ml, corresponding to a specific activity of > 2×105IU/mg.
More Info
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Introduction
IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.
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Synonyms
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-13 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-13 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
SPSPVPRSTA LKELIEELVN ITQNQKAPLC NGSMVWSINL TAGVYCAALE SLINVSGCSA IEKTQRMLNG FCPHKVSAGQ FSSLRVRDTK IEVAQFVKDL LVHLKKLFRE GRFN
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 :
NPPC HumanDescription:
Natriuretic Peptide C Human Recombinant
Natriuretic Peptide Precursor C, C-Type Natriuretic Peptide, CNP2, CNP.
Product # :
CYT-760Price :
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Description
NPPC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (24-126) and having a molecular mass of 13.2kDa.NPPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NPPC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
NPPC is proteolytically managed to create a secreted hormone of the natriuretic peptide family. NPPC is vasoactive and natriuretic and controls the evolution and differentiation of cartilaginous growth plate chondrocytes.
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Synonyms
Natriuretic Peptide Precursor C, C-Type Natriuretic Peptide, CNP2, CNP.
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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 MGSKPGAPPK VPRTPPAEEL AEPQAAGGGQ KKGDKAPGGG GANLKGDRSR LLRDLRVDTK SRAAWARLLQ EHPNARKYKG ANKKGLSKGC FGLKLDRIGS MSGLGC
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 :
CCL26 HumanDescription:
Eotaxin-3 Human Recombinant (CCL26)
C-C motif chemokine 26, Small-inducible cytokine A26, Eotaxin-3, Macrophage inflammatory protein 4-alpha, MIP-4-alpha, Thymic stroma chemokine-1, TSC-1, CC chemokine IMAC, CCL26, SCYA26, IMAC, MIP-4a, MGC126714, MIP-4alpha.
Product # :
CHM-362Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- SDS-PAGE
Description
Eotaxin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 8.4kDa. The Eotaxin-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Biological Activity
Determined by its ability to chemoattract BaF3 mouse pro-B cells transfected with mouse CCR3. The ED50 for this effect is typically 0.1-1.0 μg/ml.
SDS-PAGE
More Info
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Introduction
Eotaxin-3 (CCL26) is a small cytokine that belongs to the CC chemokine family also known as TARC (thymus and activation regulated chemokine). CCL26 is major eotaxin produced and released by alveolar epithelial cells which is involved in autoregulation of CCR3 receptors and other eotaxins. Eotaxin-3 is involved in immunoregulatory and inflammatory processes. Eotaxin-3 specifically binds and stimulates chemotaxis in T cells and elicits its effects by interacting with the chemokine receptor CCR4. CCL26 exhibits chemotactic activity for normal peripheral blood eosinophils and basophils. Eotaxin-3 may play a part in the eosinophil accumulation in atopic diseases. Eotaxin-3 is overexpressed in eosinophilic esophagitis, and the expression level correlates with disease severity. Eotaxin-3 is expressed constitutively in thymus, but only briefly in phytohemagglutinin-stimulated peripheral blood mononuclear cells. CCL26 is one of two Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 7.
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Synonyms
C-C motif chemokine 26, Small-inducible cytokine A26, Eotaxin-3, Macrophage inflammatory protein 4-alpha, MIP-4-alpha, Thymic stroma chemokine-1, TSC-1, CC chemokine IMAC, CCL26, SCYA26, IMAC, MIP-4a, MGC126714, MIP-4alpha.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL26 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 Eotaxin-3 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
TRGSDISKTC CFQYSHKPLP WTWVRSYEFT SNSCSQRAVI FTTKRGKKVC THPRKKWVQK YISLLKTPKQ L.
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Background
What is the molecular weight/Mw of CCL26 HUMAN Protein?
CCL26 HUMAN Protein has a total Mw of 8.4kDa.
What is the source or expression system of CCL26 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL26 HUMAN Protein?
CCL26 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL26 HUMAN Protein?
Determined by its ability to chemoattract BaF3 mouse pro-B cells transfected with mouse CCR3. The ED50 for this effect is typically 0.1-1.0 μg/ml.
What is the amino acid sequence of CCL26 HUMAN Protein?
TRGSDISKTC CFQYSHKPLP WTWVRSYEFT SNSCSQRAVI FTTKRGKKVC THPRKKWVQK YISLLKTPKQ L.
What applications can CCL26 HUMAN Protein be used in?
CCL26 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL26 HUMAN Protein?
The endotoxin level is minimal, CCL26 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.
- View Data Sheet
Name :
ANGPTL3 Human, HEKDescription:
Angiopoietin Like Protein 3 Human Recombinant, HEK
Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.
Product # :
CYT-766Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
ANGPTL3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 17-460) containing a total of 450 amino acids, having a molecular mass of 52.6kDa (calculated) and fused to a 6 aa His tag at C-Terminus.The Human ANGPTL3 is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ANGPTL3 and ANGPTL4 are angiopoietin-like proteins secreted and expressed mainly by the liver, their role being the regulation of triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. During different nutritional states (feeding/fasting) the levels of the circulating triglycerides are regulated by Angptl3 and Angptl4 through differential inhibition of Lipoprotein lipase (LPL) as shown by the experimental data. The molecular structure of ANGPTL3 is similar to that of the angiopoietins (vascular endothelial growth factors). Deletion mutants of human Angiopoietin 5 were used in order to demonstrate that the N-terminal domain (fragment 17-207) and not the C-terminal fibrinogen-like domain (fragment 207-460) increased the plasma triglyceride levels in mice.
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Synonyms
Angiopoietin 5, ANGPT5, ANGPTL3, Angiopoietin Like Protein 3.
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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.
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Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
SRIDQDNSSF DSLSPEPKSR FAMLDDVKIL ANGLLQLGHG LKDFVHKTKG QINDIFQKLN IFDQSFYDLS LQTSEIKEEE KELRRTTYKL QVKNEEVKNM SLELNSKLES LLEEKILLQQ KVKYLEEQLT NLIQNQPETP EHPEVTSLKT FVEKQDNSIK DLLQTVEDQY KQLNQQHSQI KEIENQLRRT SIQEPTEISL SSKPRAPRTT PFLQLNEIRN VKHDGIPAEC TTIYNRGEHT SGMYAIRPSN SQVFHVYCDV ISGSPWTLIQ HRIDGSQNFN ETWENYKYGF GRLDGEFWLG LEKIYSIVKQ SNYVLRIELE DWKDNKHYIE YSFYLGNHET NYTLHLVAIT GNVPNAIPEN KDLVFSTWDH KAKGHFNCPE GYSGGWWWHD ECGENNLNGK YNKPRAKSKP ERRRGLSWKS QNGRLYSIKS TKMLIHPTDS ESFEHHHHHH.
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Background
What is the molecular weight/Mw of ANGPTL3 Protein?
ANGPTL3 Protein has a total Mw of 52.6kDa.
What is the source or expression system of ANGPTL3 Protein?
HEK 293.
What is the Purity of ANGPTL3 Protein?
ANGPTL3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL3 Protein?
The biological functionality of ANGPTL3 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL3 Protein?
SRIDQDNSSF DSLSPEPKSR FAMLDDVKIL ANGLLQLGHG LKDFVHKTKG QINDIFQKLN IFDQSFYDLS LQTSEIKEEE KELRRTTYKL QVKNEEVKNM SLELNSKLES LLEEKILLQQ KVKYLEEQLT NLIQNQPETP EHPEVTSLKT FVEKQDNSIK DLLQTVEDQY KQLNQQHSQI KEIENQLRRT SIQEPTEISL SSKPRAPRTT PFLQLNEIRN VKHDGIPAEC TTIYNRGEHT SGMYAIRPSN SQVFHVYCDV ISGSPWTLIQ HRIDGSQNFN ETWENYKYGF GRLDGEFWLG LEKIYSIVKQ SNYVLRIELE DWKDNKHYIE YSFYLGNHET NYTLHLVAIT GNVPNAIPEN KDLVFSTWDH KAKGHFNCPE GYSGGWWWHD ECGENNLNGK YNKPRAKSKP ERRRGLSWKS QNGRLYSIKS TKMLIHPTDS ESFEHHHHHH.
What applications can ANGPTL3 Protein be used in?
ANGPTL3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL3 Protein?
The endotoxin level is minimal, ANGPTL3 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 :
GDF15 D HumanDescription:
Growth and Differentiation Factor 15 D-Variant Human Recombinant
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Product # :
CYT-314Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GDF15 D-variant (His substitutes Asp at position 7) Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.5kDa. The GDF15 D-variant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF15 D-variant is lyophilized without additives.
Purity
Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
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Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GDF15 D-variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF15 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.
-
Solubility
It is recommended to reconstitute the lyophilized GDF15 D-variant in sterile 5mM AcOH (acetic Acid) at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MARNGDDCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
-
Background
What is the molecular weight/Mw of GDF15 D HUMAN Protein?
GDF15 D HUMAN Protein has a total Mw of 24.5kDa.
What is the source or expression system of GDF15 D HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF15 D HUMAN Protein?
GDF15 D HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 D HUMAN Protein?
The biological functionality of GDF15 D HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF15 D HUMAN Protein?
MARNGDDCPL GPGRCCRLHT VRASLEDLGW ADWVLSPREV QVTMCIGACP SQFRAANMHA QIKTSLHRLK PDTVPAPCCV PASYNPMVLI QKTDTGVSLQ TYDDLLAKDC HCI.
What applications can GDF15 D HUMAN Protein be used in?
GDF15 D HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF15 D HUMAN Protein?
The endotoxin level is minimal, GDF15 D 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.
- View Data Sheet
Name :
ANKRD1 HumanDescription:
Ankyrin Repeat Domain 1 Human Recombinant
Ankyrin Repeat Domain 1 (Cardiac Muscle), Cardiac Ankyrin Repeat Protein, Cytokine-Inducible Gene C-193 Protein, Ankyrin Repeat Domain-Containing Protein 1, Cytokine-Inducible Nuclear Protein, Liver Ankyrin Repeat Domain 1, BA320F15.2, CARP, ALRP, CVARP, MCARP, HA1A2, C193.
Product # :
PRO-1219Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ANKRD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 342 amino acids (1-319) and having a molecular mass of 38.6 kDa.ANKRD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ANKRD1 solution contains 20mM Tris-HCl buffer (pH 8.5), 0.2M NaCl, 5mM DTT and 50% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
ANKRD1 takes part in endothelial cell activation and performs as a nuclear transcription factor which negatively controls the expression of cardiac genes.
-
Synonyms
Ankyrin Repeat Domain 1 (Cardiac Muscle), Cardiac Ankyrin Repeat Protein, Cytokine-Inducible Gene C-193 Protein, Ankyrin Repeat Domain-Containing Protein 1, Cytokine-Inducible Nuclear Protein, Liver Ankyrin Repeat Domain 1, BA320F15.2, CARP, ALRP, CVARP, MCARP, HA1A2, C193.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGS MMVLKVE ELVTGKKNGN GEAGEFLPED FRDGEYEAAV TLEKQEDLKT LLAHPVTLGE QQWKSEKQRE AELKKKKLEQ RSKLENLEDL EIIIQLKKRK KYRKTKVPVV KEPEPEIITE PVDVPTFLKA ALENKLPVVE KFLSDKNNPD VCDEYKRTAL HRACLEGHLA IVEKLMEAGA QIEFRDMLES TAIHWASRGG NLDVLKLLLN KGAKISARDK LLSTALHVAV RTGHYECAEH LIACEADLNA KDREGDTPLH DAVRLNRYKM IRLLIMYGAD LNIKNCAGKT PMDLVLHWQN GTKAIFDSLR ENSYKTSRIA TF
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 :
IFA1 PorcineDescription:
Interferon-alpha 1 Porcine Recombinant
Interferon alpha-1, Interferon-alpha, IFN-alpha-1, IFNA1, IFN-ALPHA-1, IFN1
Product # :
CYT-1197Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IFA1 porcine Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-189) containing 176 amino acids and having a molecular mass of 20.2kDa.IFA1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
IFA1 protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
IFNs are cytokines that are widely known to induce potent anti-viral activity. IFN-a exerts a variety of other biological effects, including antitumor and immunomodulatory activities and are increasingly used clinically to treat a range of malignancies, myelodysplasias and autoimmune diseases.
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Synonyms
Interferon alpha-1, Interferon-alpha, IFN-alpha-1, IFNA1, IFN-ALPHA-1, IFN1
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
DGSMCDLPQT HSLAHTRALR LLAQMRRISP FSCLDHRRDF GSPHEAFGGN QVQKAQAMAL VHEMLQQTFQ LFSTEGSAAA WNESLLHQFC TGLDQQLRDL EACVMQEAGL EGTPLLEEDS ILAVRKYFHR LTLYLQEKSY SPCAWEIVRA EVMRSFSSSR NLQDRLRKKE 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 :
TFF2 Human, HisDescription:
Trefoil Factor-2 Human Recombinant, His Tag
TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.
Product # :
CYT-611Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids (24-129) which includes a 10 amino acid His Tag fused at N-terminus and having a total molecular mass of 13.2 kDa. TFF2 Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 0.5mg/ml containing 20mM Tris pH-7.5, and 20mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.
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Synonyms
TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 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 add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.
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 :
LIF Human, Sf9Description:
Leukemia Inhibitory Factor Human Recombinant, Sf9
Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.
Product # :
CYT-1003Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- biological activity
- More Info
Description
LIF Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 189 amino acids (23-202a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). LIF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LIF protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 0.5 ng/ml.
More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADPSPLPITP VNATCAIRHP CHNNLMNQIR SQLAQLNGSA NALFILYYTA QGEPFPNNLD KLCGPNVTDF PPFHANGTEK AKLVELYRIV VYLGTSLGNI TRDQKILNPS ALSLHSKLNA TADILRGLLS NVLCRLCSKY HVGHVDVTYG PDTSGKDVFQ KKKLGCQLLG KYKQIIAVLA
QAFHHHHHH.
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 :
IL11RA RatDescription:
Interleukin 11 Receptor Subunit Alpha Rat Recombinant
Interleukin-11 receptor subunit alpha, IL-11 receptor subunit alpha, IL-11R subunit alpha, IL-11R-alpha, IL-11RA, Il11ra1.
Product # :
CYT-990Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
Interleukin 11 Receptor Subunit Alpha Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (24-371a.a.) and having a molecular mass of 39.2kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL11RA is fused with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL11RA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Interleukin 11 Receptor Subunit Alpha (IL11RA) which belongs to the hematopoietic cytokine receptor family is a receptor for interleukin-11. Interleukin 11 is a stromal cell-derived cytokine which is a member of a family of pleiotropic and redundant cytokines that employ the gp130 transducing subunit in their high affinity receptors. This specific receptor is quite similar to ciliary neurotrophic factor, since both contain an extracellular region with a two-domain structure composed of an immunoglobulin-like domain and a cytokine receptor-like domain. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 are able to utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex is involved in the control of proliferation and/or differentiation of skeletogenic progenitor or additional mesenchymal cells.
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Synonyms
Interleukin-11 receptor subunit alpha, IL-11 receptor subunit alpha, IL-11R subunit alpha, IL-11R-alpha, IL-11RA, Il11ra1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
TPCPQAWGPP GVQYGQPGRP VMLCCPGVNA GTPVSWFRDG DSRLLQGPDS GLGHRLVLAQ VDSRDEGTYV CRTLDGVFGG MVTLKLGSPP ARPEVSCQAV DYENFSCTWS PGRVSGLPTR YLTSYRKKTL PGAESQRESP STGPWPCPQD PLEASRCVVH GAEFWSEYRI NVTEVNPLGA STCLLDVRLQ RILRPDPPQG LRVESVPGYP RRLHASWTYP ASWRRQPHFL LKFRLQYRPA QHPAWSTVEP IGLEELITDA VAGLPHAVRV SARDFLDAGT WSAWSPEAWG TPSTGPLRDE VPDGSRGHEQ KLEAAAQEDS PAPPSPSLQP DPRPLDHRDP LEQVAVLAVE 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 :
MCP 4 Human, HisDescription:
Monocyte Chemotactic Protein-4 Human Recombinant (CCL13), His-Tag
CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.
Product # :
CHM-275Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MCP4 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 96 amino acids (24-98) and having a molecular mass of 10.8 kDa. The MCP-4 is fused to 21 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The His Tag 0.25mg/ml MCP4 protein solution contains PBS pH-7.4, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
CCL13 chemokine is part of the CC chemokine family (TARC). CCL13 protein induces chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils by binding cell surface G-protein linked chemokine receptors such as CCR2, CCR3 and CCR5. CCL13 is induced by the inflammatory cytokines IL1 & TNFA.
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Synonyms
CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.
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Physical Appearance
Sterile Filtered colorless clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
.AHTLKT
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 :
APOB HumanDescription:
Apolipoprotein-B Human
APOB, APO-B, Apolipoprotein B.
Product # :
CYT-1042Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- More Info
Description
Human APOB produced from Human plasma having a molecular mass of 550 kDa.
Source
Human Plasma.
Formulation
The protein was lyophilized in a solution contains 50mM NaCl, 50mM Na₂co₃, PH 10 and deoxycholate.
Purity
Greater than 90.0%.
More Info
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Introduction
ApoB is the main apolipoprotein of LDL, IDL, VLDL and chylomicrons particles that serves as the carrier of lipids (fat molecules), as well as cholesterol, in the water surrounding the cells within every tissue across the body. Though all the functional aspects of Apolipoprotein B within the LDL and other elements are considered to be rather uncertain, it serves as the key organizing protein of all other carriers of lipids. across LDL membranes, apolipoprotein B also serves as a ligand for LDL receptors in many cells across the body, meaning, it shows that lipid carriers that are set to cross into cells with Apolipoprotein B receptors, this is the way that lipids are transported within and into cells.
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Synonyms
APOB, APO-B, Apolipoprotein B.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
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Stability
Lyophilized APOB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution, APOB 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.
-
Solubility
It is recommended to reconstitute the lyophilized APOB in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1,
HIV-2, HCV, HBSAG, HBc.
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Background
Apolipoprotein-B Human: Unveiling the Key Player in Cholesterol Transport
Abstract:
Apolipoprotein-B (ApoB), a pivotal component of lipoproteins, plays a critical role in cholesterol metabolism and transportation. It is primarily synthesized in the liver and intestines, existing in two main isoforms: ApoB-100 and ApoB-48. This research paper aims to provide a comprehensive overview of ApoB human, emphasizing its physiological functions, regulatory mechanisms, and implications in cardiovascular diseases. By delving into the intricacies of ApoB, we can gain valuable insights into its significance as a therapeutic target and potential biomarker.
Introduction:
The prevalence of cardiovascular diseases necessitates a deeper understanding of the mechanisms governing cholesterol metabolism. ApoB, an integral component of lipoproteins, holds the key to unlocking vital insights into cholesterol transport and its association with atherosclerosis.
Structure and Function of Apolipoprotein-B:
ApoB exhibits a complex molecular structure, consisting of functional domains that enable its interaction with lipids and receptors. ApoB-100, the longer isoform, is primarily associated with low-density lipoprotein (LDL) particles, while ApoB-48 is present in chylomicrons and chylomicron remnants. These isoforms serve distinct roles in lipoprotein metabolism and cholesterol delivery to peripheral tissues.
Regulation of Apolipoprotein-B:
The synthesis and secretion of ApoB are tightly regulated processes influenced by various factors, including dietary and genetic factors. Transcriptional and post-transcriptional mechanisms govern the expression and processing of ApoB, ensuring its proper function in cholesterol transport.
Apolipoprotein-B and Cardiovascular Diseases:
Elevated levels of ApoB-containing lipoproteins, such as LDL, have been implicated in the development of atherosclerosis and cardiovascular diseases. The ratio of ApoB to ApoA-I, known as the ApoB/ApoA-I ratio, serves as a reliable marker for cardiovascular risk assessment, with higher ratios indicating increased risk.
Therapeutic Implications of Apolipoprotein-B:
Targeting ApoB presents a promising avenue for managing dyslipidemia and reducing cardiovascular risk. Strategies aimed at reducing ApoB production or enhancing its clearance have shown efficacy in clinical trials, underscoring the potential of ApoB as a therapeutic target.
Conclusion:
Apolipoprotein-B human serves as a cornerstone in cholesterol transport, playing a crucial role in lipoprotein metabolism and its implications for cardiovascular health. By unraveling the intricate interplay between ApoB, cholesterol metabolism, and atherosclerosis, we can pave the way for novel therapeutic interventions and improved risk assessment in cardiovascular diseases.
What is the molecular weight/Mw of APOB Protein?
APOB Protein has a total Mw of 550kDa.
What is the source or expression system of APOB Protein?
Human Plasma.
What is the Purity of APOB Protein?
APOB Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of APOB Protein?
The biological functionality of APOB Protein will be determined in the future.
What applications can APOB Protein be used in?
APOB Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APOB Protein?
The endotoxin level is minimal, APOB 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 :
APOH Human, sf9Description:
Apolipoprotein-H Human Recombinant, Sf9
Beta-2-glycoprotein 1, Beta-2-glycoprotein I, Apolipoprotein H, Apo-H, B2GPI, Beta(2)GPI, Activated protein C-binding protein, APC inhibitor, Anticardiolipin cofactor, APOH, B2G1, BG, B2GP-1, B2 Glycoprotein-I.
Product # :
PRO-388Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Apolipoprotein-H Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing 326 amino acids and having a molecular mass of 38,200 Dalton (excluding glycosylation), 45kDa total mass. APOH is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
APOH is supplied in 16mM HEPES buffer pH-7.2, 200mM NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Apolipoprotein H (APOH) attaches to numerous kinds of negatively charged substances for instance heparin, phospholipids, and dextran sulfate. APOH prevents activation of the intrinsic blood coagulation cascade by attaching to phospholipids on the surface of damaged cells. APOH expressed by the liver and secreted in the plasma.
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Synonyms
Beta-2-glycoprotein 1, Beta-2-glycoprotein I, Apolipoprotein H, Apo-H, B2GPI, Beta(2)GPI, Activated protein C-binding protein, APC inhibitor, Anticardiolipin cofactor, APOH, B2G1, BG, B2GP-1, B2 Glycoprotein-I.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 1RA Rat, HisDescription:
Interleukin-1 Receptor Antagonist Rat Recombinant, His Tag
Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, Il1rn, Il-1ra, Interleukin-1 Receptor Antagonist, IL-1ra, IL 1RA.
Product # :
CYT-899Price :
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Description
IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (27-178a.a.) and having a molecular mass of 19.8kDa.IL 1RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL 1RA protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
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Synonyms
Interleukin-1 receptor antagonist protein, IL-1RN, IL-1ra, IRAP, IL1 inhibitor, Il1rn, Il-1ra, Interleukin-1 Receptor Antagonist, IL-1ra, IL 1RA.
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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 MGSHPAGKRP CKMQAFRIWD TNQKTFYLRN NQLIAGYLQG PNTKLEEKID MVPIDFRNVF LGIHGGKLCL SCVKSGDDTK LQLEEVNITD LNKNKEEDKR FTFIRSETGP TTSFESLACP GWFLCTTLEA DHPVSLTNTP KEPCTVTKFY FQEDQ.
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 :
GDF11 Human, HisDescription:
Growth and Differentiation factor 11 Human Recombinant, His Tag
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
Product # :
CYT-887Price :
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Description
GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa. GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF11 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
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Synonyms
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
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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 MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
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Background
What is the molecular weight/Mw of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein has a total Mw of 14.8kDa.
What is the source or expression system of GDF11 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF11 HUMAN, HIS Protein?
The biological functionality of GDF11 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of GDF11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
What applications can GDF11 HUMAN, HIS Protein be used in?
GDF11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF11 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF11 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.
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Name :
IL5 Mouse, HEKDescription:
Interleukin-5 Mouse Recombinant, HEK
interleukin 5, Il, Il-5, B-cell growth factor II, EDF, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, TRFB cell differentiation factor I, T-cell replacing factor, TRF, B-cell differentiation factor I, IL5
Product # :
CYT-1194Price :
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Description
IL5 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 122 amino acids (21-133 a.a) and having a molecular mass of 14.2 kDa.IL5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IL5 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 3 ng/ml.
More Info
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Introduction
The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. IL5is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of IL5is reported to be related to asthma or hypereosinophilic syndromes. The receptor of IL5is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). IL5, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. IL5, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
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Synonyms
interleukin 5, Il, Il-5, B-cell growth factor II, EDF, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, TRFB cell differentiation factor I, T-cell replacing factor, TRF, B-cell differentiation factor I, IL5
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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
DGSMEIPMST VVKETLTQLS AHRALLTSNE TMRLPVPTHK NHQLCIGEIF QGLDILKNQT VRGGTVEMLF QNLSLIKKYI DRQKEKCGEE RRRTRQFLDY LQEFLGVMST EWAMEGHHHH HH
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 :
TNF a Rhesus MacaqueDescription:
Tumor Necrosis Factor-Alpha Rhesus Macaque Recombinant
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
Product # :
CYT-737Price :
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Shipped at Room temp
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Description
TNF-a Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.3kDa.The TNFA Rhesus Macaque is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg in the presence of actinomycin D.More Info
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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer. -
Synonyms
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha 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
VRSSSRTPSD KPVAHVVANP QAEGQLQWLN RRANALLANG VELTDNQLVV PSEGLYLIYS QVLFKGQGCP SNHVLLTHTI SRIAVSYQTK VNLLSAIKSP CQRETPEGAE AKPWYEPIYL GGVFQLEKGD RLSAEINLPD YLDFAESGQV YFGIIAL.
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 :
MIF Human His NDescription:
Macrophage Migration Inhibitory Factor Human, Recombinant His Tag N-Terminus
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
Product # :
CYT-431Price :
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Shipped with Ice Packs
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Description
MIF human Recombinant, fused to 40 a.a. His-tag at N-terminus, was cloned into an E. coli expression vector and was purified to apparent homogeneity by using conventional column chromatography techniques. Macrophage Inducing Factor Human Recombinant ( 1-115 a.a. ) is a single, non-glycosylated, polypeptide chain having a total amino acids of 155 and molecular mass of 17kDa.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Phenylpyruvate tautomerase, Glycosylation-inhibiting factor, GIF, MMIF, MIF.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Liquid MIF although stable 4°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC LHSIGKIGGA QNRSYSKLLC GLLAERLRIS PDRVYINYYD MNAANVGWNN STFA.
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 :
SAA EquineDescription:
Serum Amyloid A (APO-SAA) Equine Recombinant
Product # :
CYT-1222Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SAA Equine produced in E.coli is a single, non-glycosylated polypeptide chain (1-110 a.a) containing 120 a.a and having a molecular mass of 13,580 Dalton. SAA s fused with a 10 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SAA was lyophilized from 0.01M HCl (pH 2.0).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SAA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serum Amyloid A (APO-SAA) 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 SAA in 0.01M HCl (pH 2.0) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Elevated SAA levels serve as sensitive markers for various inflammatory disorders, including infections, autoimmune diseases, and cancer. SAA assays, often utilizing recombinant SAA proteins, are invaluable in clinical diagnostics, aiding in disease monitoring and treatment evaluation. Moreover, the targeted modulation of SAA activities presents novel therapeutic strategies, offering potential interventions in conditions characterized by excessive inflammation.
SAA Recombinant Protein, as a representative of the intricate SAA family, embodies the complexities of inflammation, immune regulation, and lipid metabolism. Its versatile roles in health and disease underscore its significance in biology and medicine. By unraveling the molecular intricacies of SAA, scientists pave the way for innovative diagnostic methods, therapeutic interventions, and a deeper understanding of the intricate interplay between inflammation and various physiological processes. This research not only illuminates the multifaceted nature of SAA but also holds the promise of transformative advancements in both clinical practice and scientific discovery.
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.