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543 results found for “midkine”
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Name :
PRKAR1ADescription:
cAMP-Dependent Protein Kinase A regulatory subunit I a Recombinant
cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, CAR, CNC, CNC1, PKR1, PPNAD1, PRKAR1, PRKAR1A, MGC17251, DKFZp779L0468.
Product # :
PKA-201Price :
Quantity :
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Shipped with Ice Packs
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Description
cAMP-dependent PKA is an ubiquitous serine/theonine protein kinase present in a variety of tissues (e.g. brain, skeletal muscle, heart). The intracellular cAMP level regulates cellular responses by altering the interaction between the catatytic C and regulatory R subunits of PKA. The inactive tetrameric PKA holoenzyme R2C2 is activated when cAMP binds to R2, which dissociates the tetramer to R2 cAMP 4 and two active catalytic subunits. Free Catalytic subunits of PKA can phosphorylate a wide variety of intracellular target proteins. In response to hormone- induced high cAMP levels, PKA phosphorylates glycogen synthetase (inhibition of the enzyme activity) and phosphorylase kinase to block glycogen synthesis. Different isoforms of catalytic and regulatory subunits suggest specific functions. The recombinant PKA regulatory subunit I a is a dimeric 90kDa protein.
Source
Escherichia Coli.
Formulation
PKA regulatory subunit I a is supplied in 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
cAMP-dependent protein kinase type I-alpha regulatory subunit, Tissue-specific extinguisher 1, TSE1, CAR, CNC, CNC1, PKR1, PPNAD1, PRKAR1, PRKAR1A, MGC17251, DKFZp779L0468.
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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. Avoid multiple freeze-thaw cycles.
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Unit Definition
Specifically inhibits PKA catalytic subunit (Ki about 0.1nM). Activity can be restored by adding cAMP (Kact about 100nM). The binding of the catalytic subunit is dependent on the presence of ATP and 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.
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Name :
CKS2 HumanDescription:
CDC28 Protein Kinase 2 Human Recombinant
CDC28, CKSHS2, CKS2, CDC28 Protein Kinase 2.
Product # :
PKA-258Price :
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Description
CKS2 Human Recombinant fused to T7-Tag produced in E.Coli is a single, non- glycosylated polypeptide chain containing 94 amino acids and having a molecular mass of 11 kDa.
Source
Escherichia Coli.
Formulation
The CKS2 protein solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CKS2 protein binds to the catalytic subunit of the cyclin dependent kinases and is necessary for their biological function. The CKS2 mRNA is expressed in various patterns through the cell cycle in HeLa cells, which shows spcific role for the encoded protein. CKS2 (CDC28) Protein kinase 2 binds to the catalytic subunit of cyclin-dependent kinases and has thus in involved in cell cycle regulation. CKS2 is required for the first metaphase/anaphase transition during the meiosis. An increase in expression of CKS2 protects the cells from apoptosis. CKS2 is essential during early embryogenesis and cell cycle progression in somatic cells.
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Synonyms
CDC28, CKSHS2, CKS2, CDC28 Protein Kinase 2.
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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
MASMTGGQQM GRGSHMAHKQ IYYSDKYFDE HYEYRHVMLP RELSKQVPKT HLMSEEEWRRLGVQQSLGWV HYMIHEPEPH ILLFRRPLPK DQQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Leptin N82K Human, PEGDescription:
Leptin N82K Human Recombinant, Pegylated
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1107Price :
Quantity :
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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.
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Name :
CKMB Human ActiveDescription:
Creatine Kinase MB Active Human Recombinant
CKMB, CK-MB
Product # :
CKI-200Price :
Quantity :
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Shipped at Room temp
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Description
CKMB Human Recombinant produced in E. coli is a noncovalently-linked heterodimer consists of CK-M and CK-B each containing 381 amino acids and having a total molecular mass of 85.7kDa (43.10 kDa and 42.64 kDa respectively). CKMB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris and 150mM NaCl, pH 8.0.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The specific activity ranges from 500-600 units/mg and was measured kinetically by the CK-NAC assay at 37°C.More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CKMB Active although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CKMB Active should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles. -
Solubility
It is recommended to reconstitute the lyophilized CKMB 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
CKM
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
CKB
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K.
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Background
CKMB is used in cardiovascular research as a biomarker for myocardial injury and to investigate the molecular mechanisms of cardiac muscle damage and repair.
CKMB is also used in Immunoassay development, Aptamer screening, Biosensor validation and Point-of-care diagnostic assay development
What is the molecular weight / Mw of CKMB Protein?
CKMB Protein is a non covalently heterodimer having a total Mw of 85.7ka
What is the source or expression system of CKMB Protein?
Escherichia Coli.
What is the Purity of CKMB Protein?
CKMB Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CKMB Protein?
The activity was determined kinetically by the CK-NAC assay at 37°C which ranges between 500-600 U/mg.
What is the amino acid sequence of CKMB Protein?
CKM
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
CKB
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K
What applications can CKMB Protein be used in?
CKMB Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CKMB Protein?
The endotoxin level is minimal, CKMB 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 :
HEV ORF3Description:
Hepatitis E Virus ORF3 Recombinant
Product # :
HEV-273Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The e.coli derived HEV protein is fused with beta-galactosidase at the N-Terminus and contains the HEV immunodominant ORF3 92-123 a.a.
Formulation
20mM Tris-HCl, pH-8, 10mM B-ME and 8M urea.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
Hepatitis E virus (HEV), the major etiologic agent of enterically transmitted non-A, non-B hepatitis worldwide, is a spherical, non-enveloped, single stranded RNA virus that is approximately 32 to 34 nm in diameter. HEV belongs to a genus of HEV-like viruses (unassigned genus). HEV has a single-stranded polyadenylated RNA genome of approximately 8 kb. Based on its physicochemical properties it is presumed to be a calici-like virus.
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Stability
HEV ORF3 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Specificity
Immunoreactive with sera HEV-infected individuals.
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Purification Method
HEV ORF3 protein was purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL31 Canine, HEKDescription:
Interleukin-31 Canine Recombinant, HEK
IL-31, Interleukin 31, IL31.
Product # :
CYT-1215Price :
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Description
IL31 Canine Recombinant is a single, glycosylated, polypeptide chain (24-159 a.a) containing a total of 136 amino acids, having a molecular mass of 25.2 kDa. IL31 is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IL31 solution (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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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. 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
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQ.
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Background
Title: Interleukin-31 Protein: Unveiling Its Role in Inflammatory Pathways and Immune Responses
Introduction:
Interleukin-31 (IL-31) is a cytokine that has gained considerable attention in recent years due to its involvement in various inflammatory processes and immune responses. Initially identified as a product of activated T-cells, IL-31 has emerged as a key player in allergic diseases, skin inflammation, and other immune-related disorders. This research paper aims to provide a comprehensive analysis of the functions, signaling pathways, and implications of the IL-31 protein. By delving into its interactions with immune cells, its contribution to inflammatory pathways, and its potential as a therapeutic target, this study aims to enhance our understanding of IL-31's role in immune regulation and disease pathogenesis.
Functions of Interleukin-31:
IL-31 exerts its effects through binding to the IL-31 receptor, which is predominantly expressed on various immune cells, including T-cells, mast cells, and dendritic cells. Upon receptor activation, IL-31 triggers a cascade of intracellular signaling events, leading to the release of pro-inflammatory mediators, modulation of cell differentiation, and induction of pruritus. Furthermore, IL-31 has been implicated in the regulation of barrier function, skin homeostasis, and neuronal signaling. Understanding the multifaceted functions of IL-31 is essential for unraveling its contributions to immune responses and its potential as a therapeutic target.
Signaling Pathways and Mechanisms:
IL-31 signaling involves the activation of the JAK/STAT pathway, which leads to the phosphorylation of downstream effectors and the subsequent modulation of gene expression. Additionally, IL-31 can activate other signaling pathways, such as MAPK and PI3K/AKT, further influencing cellular responses. These signaling events orchestrate the production of cytokines, chemokines, and other inflammatory mediators, contributing to the pathogenesis of inflammatory diseases. Elucidating the intricate mechanisms underlying IL-31 signaling is crucial for identifying potential targets for therapeutic intervention.
Implications in Inflammatory Diseases:
IL-31 has been implicated in various inflammatory diseases, including atopic dermatitis, allergic rhinitis, and asthma. Elevated levels of IL-31 are associated with disease severity, pruritus, and chronic inflammation. Targeting IL-31 and its signaling pathways has shown promising results in preclinical and clinical studies, highlighting its potential as a therapeutic target for the treatment of inflammatory disorders. Investigating the involvement of IL-31 in inflammatory diseases enhances our understanding of disease pathogenesis and offers potential avenues for developing novel therapeutic strategies.
Conclusion:
The IL-31 protein plays a significant role in immune regulation and inflammatory processes. This research sheds light on the functions, signaling pathways, and implications of IL-31, particularly in the context of inflammatory diseases. Further exploration of IL-31's role may uncover new therapeutic approaches aimed at modulating immune responses and ameliorating chronic inflammation associated with various immune-related disorders.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on IL-31 for a comprehensive list of references and sources.
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 :
Fibronectin HumanDescription:
Fibronectin Human
Product # :
PRO-448Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Fibronectin produced purified from Human Plasma having a Molecular Weight of 440kDa.
Source
Human Plasma.
Formulation
The Fibronectin was lyophilized from a non sterile 2mg/ml buffer of 10mM sodium phosphate, pH 7.5 and 0.15M NaCl.
Purity
≥ 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin plays a role in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion. Fibronectin consists in two main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the extracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin also takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Fibronectin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibronectin should be stored at 4°C between 2-7 days and for future use below -18°C.
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Solubility
We suggest reconstituting the 1mg Fibronectin with a chaotropic agent such as urea at room temperature at a concentration of 0.2mg/ml using sterile water. Let stand 1-2 hours. The recommended concentration is 4M-5M urea.
When using the protein as an attachment factor, wash the urea off after attaching the fibronectin to the growth surface (plate or dish).
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 :
KRT18 Human, HisDescription:
Cytokeratin 18 Human Recombinant , His Tag
Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.
Product # :
PRO-484Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KRT18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a calculated molecular mass of 52.42kDa.The KRT18 is fused to a His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KRT18 protein solution (0.8mg/ml) contains 20mM Tris pH 8, 5mM EDTA and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
KRT18 encodes the type I intermediate filament chain keratin 18. Keratin 18, together with its filament partner keratin 8, are perhaps the most commonly found members of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.
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Synonyms
Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.
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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 :
M CSF Rat HEKDescription:
Macrophage Colony Stimulating Factor Rat Recombinant HEK
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
Product # :
CYT-046Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
MCSF Rat Recombinant produced in HEK-293 cells is a secreted protein (amino acids Glu33-Arg254). M-CSF is disulfide-linked homodimer containing 2 x 222 a.a chains.
Source
HEK293
Formulation
The recombinant MCSF was lyophilized after extensive dialysis against PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of mouse M-NFS-60 cells.More Info
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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
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Synonyms
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 MCSF in sterile PBS not less than 100 µg/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.
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Name :
SELE Human, HEKDescription:
E-Selectin Human Recombinant, HEK
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
Product # :
PRO-1645Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SELE Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 543 amino acids (22-556). SELE is fused to an 8 amino acid His-tag at C-terminus is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
SELE was lyophilized from a 0.2 µM filtered solution of PBS and 4% Mannitol, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
E-selectin which is also called Endothelial leukocyte adhesion molecule 1, ELAM1, ELAM belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Eselectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.
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Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SELE although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELE 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 SELE in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
WSYNTSTEAMTYDEASAYCQQRYTHLVAIQNKEEIEYLNSILSYSPSYYWIGIRKVNNVW
VWVGTQKPLTEEAKNWAPGEPNNRQKDEDCVEIYIKREKDVGMWNDERCSKKKLALCYTA
ACTNTSCSGHGECVETINNYTCKCDPGFSGLKCEQIVNCTALESPEHGSLVCSHPLGNFSY
NSSCSISCDRGYLPSSMETMQCMSSGEWSAPIPACNVVECDAVTNPANGFVECFQNPGSFPW
NTTCTFDCEEGFELMGAQSLQCTSSGNWDNEKPTCKAVTCRAVRQPQNGSVRCSHSPAGEFT
FKSSCNFTCEEGFMLQGPAQVECTTQGQWTQQIPVCEAFQCTALSNPERGYMNCLPSASGSFR
YGSSCEFSCEQGFVLKGSKRLQCGPTGEWDNEKPTCEAVRCDAVHQPPKGLVRCAHSPIGEFTY
KSSCAFSCEEGFELHGSTQLECTSQGQWTEEVPSCQVVKCSSLAVPGKINMSCSGEPVFGTVCKF
ACPEGWTLNGSAARTCGATGHWSGLLPTCEAPTESNIPVDHHHHHH.
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 :
MBP E.Coli, HisDescription:
Maltose Binding Protein E.coli Recombinant, His Tag
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
Product # :
PRO-2322Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused. -
Synonyms
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.
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 :
Hemopexin Human, Sf9Description:
Hemopexin Human Recombinant, Sf9
Hemopexin, Beta-1B-Glycoprotein, HX, Beta-1B-glycoprotein.
Product # :
PRO-2544Price :
Quantity :
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Description
Hemopexin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 448 amino acids (24-462a.a.) and having a molecular mass of 50.4kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).Hemopexin is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Hemopexin protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Hemopexin (or haemopexin) is a plasma protein that binds heme with the highest affinity of any known protein. Hemopexin is generally expressed in liver, and belongs to acute phase reactants, the synthesis of which is induced after inflammation. Heme is potentially very toxic because of its ability to intercalate into lipid membrane and to generate hydroxyl radicals. Hemopexin’s function of scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin defends the body from the oxidative damage that free heme can cause. Additionally, hemopexin discharges its bound ligand for internalisation upon interacting with a specific receptor located on the surface of liver cells. This hemopexin function is in order to preserve the body's iron. Hemopexin’s levels in the serum are an indication of how much heme is present in the blood. Low Hemopexin levels show that there is a lot of it in the serum. For that reason, low hemopexin levels indicate that there has been consid
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Synonyms
Hemopexin, Beta-1B-Glycoprotein, HX, Beta-1B-glycoprotein.
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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
ADPTPLPPTS AHGNVAEGET KPDPDVTERC SDGWSFDATT LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA FRQGHNSVFL IKGDKVWVYP PEKKEKGYPK LLQDEFPGIP SPLDAAVECH RGECQAEGVL FFQGDREWFW DLATGTMKER SWPAVGNCSS ALRWLGRYYC FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN GTGHGNSTHH GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ WPQGPSAVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKRLEKEVG TPHGIILDSV DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ATWTELPWPH EKVDGALCME KSLGPNSCSA NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ PQNVTSLLGC THHHHHHH.
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 :
ACKA E.ColiDescription:
Acetate Kinase E.Coli Recombinant
Acetate kinase, Acetokinase, ackA, ack, ACKA, Acetate kinase A and propionate kinase 2.
Product # :
PKA-063Price :
Quantity :
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Shipped with Ice Packs
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Description
Recombinant ACKA produced in E.coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-400) and having a molecular mass of 45.7 kDa.The ACKA is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ACKA protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
E.Coli Acetate Kinase, also knowns as ACKA, catalyzes the formation of acetyl phosphate from acetate and ATP and also catalyzes the reverse reaction. ACKA takes part in synthesis of various ATP formed catabolically during anaerobic growth of the organism.
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Synonyms
Acetate kinase, Acetokinase, ackA, ack, ACKA, Acetate kinase A and propionate kinase 2.
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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. 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 MGSMSSKLVL VLNCGSSSLK FAIIDAVNGE EYLSGLAECF HLPEARIKWK MDGNKQEAAL GAGAAHSEAL NFIVNTILAQ KPELSAQLTA IGHRIVHGGE KYTSSVVIDE SVIQGIKDAA SFAPLHNPAH LIGIEEALKS FPQLKDKNVA VFDTAFHQTM PEESYLYALP YNLYKEHGIR RYGAHGTSHF YVTQEAAKML NKPVEELNII TCHLGNGGSV SAIRNGKCVD TSMGLTPLEG LVMGTRSGDI DPAIIFHLHD TLGMSVDAIN KLLTKESGLL GLTEVTSDCR YVEDNYATKE DAKRAMDVYC HRLAKYIGAY TALMDGRLDA VVFTGGIGEN AAMVRELSLG KLGVLGFEVD HERNLAARFG KSGFINKEGT RPAVVIPTNE ELVIAQDASR LTA.
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 :
IL8 Canine, HEKDescription:
Interleukin-8, HEK Canine Recombinant
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
Product # :
CHM-045Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL8 Canine, HEK Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 80 amino acids (28-101 a.a) and having a molecular mass of 9.4 kDa.IL8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IL8 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. IL8 is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
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Synonyms
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
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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
VSSELRCQCI KTHSTPFHPK YIKELRVIDS GPHCENSEII VKLFNGNEVC LDPKEKWVQK VVQIFLKKAE KQDPHHHHHH
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 :
MIP 4 HumanDescription:
Macrophage Inflammatory Protein-4 Human Recombinant (CCL18)
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
Product # :
CHM-322Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Macrophage Inflammatory Protein-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7813 Dalton. The MIP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP-4 protein is lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
Chemokine (C-C motif) ligand 18 (CCL18 / MIP-4) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). MIP-4 is approximately 60% identical in amino acid sequence to CCL3. MIP-4 is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIP-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized MIP-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.
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 :
Adiponectin Mouse, HEKDescription:
Adiponectin Mouse Recombinant, HEK
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-435Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Acrp30 Mouse Recombinant is fused with FLAG tag having a total Mw of 26kDa.
Source
HEK293 (Human embryonic kidney cell line).
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M PBS buffer,0.075M NaCl, pH7.4.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml. An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.
More Info
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Introduction
Adiponectin is an important negative regulator in hematopoiesis and immune systems. It may be involved in ending inflammatory responses through its inhibitory functions. Inhibits endothelial nf-kappa-b signaling through a camp-dependent pathway. Inhibits tnf-alpha- induced expression of endothelial adhesion molecules. Involved in the control of fat metabolism and insulin sensitivity.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Stability
Store lyophilized APM-1 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 reconstitute the lyophilized Acrp30 Mouse in sterile 18M-cm H2O at 0.5mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
Full-length adiponectin activates AMP-activated protein kinase in hepatocyte. Adiponectin also activates AMPK in HepG2 human hepatocytes at the concentration of 1.0 µg/ml. An in vitro gluconeogenesis assay which was performed in primary rat hepatocytes showed the murine adiponectin derived from mammalian cells can inhibit glucose production.
What is the amino acid sequence of ADIPONECTIN Protein?
EDDVTTTEEL APALVPPPKG TCAGWMAGIP GHPGHNGTPG RDGRDGTPGE KGEKGDAGLL GPKGETGDVG MTGAEGPRGF PGTPGRKGEP GEAAYMYRSA FSVGLETRVT VPNVPIRFTK IFYNQQNHYD GSTGKFYCNI PGLYYFSYHI TVYMKDVKVS LFKKDKAVLF TYDQYQEKNV DQASGSVLLH LEVGDQVWLQ VYGDGDHNGL YADNVNDSTF TGFLLYHDTN DYKDDDDK.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
MMP 1 Human, HEKDescription:
Matrix Metalloproteinase-1 Human Recombinant, HEK
Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.
Product # :
ENZ-099Price :
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- sds-page
Description
MMP-1 Human Recombinant produced in HEK293 cells is a proform of the Human MMP1 (Met1-Asn469) and fused with a ployhistide tag at the C-terminus, having an Mw of 52kDa. MMP-1 is purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
The MMP-1 is supplied as a 0.2µm filtered solution in MES, NaCl, Glycerol and Brij35.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The activity was measured by its ability to cleave fluorogenic peptide substrate, Mca-KPLGL-Dpa-AR-NH2, The specific activity is > 400 pmoles/min/µg.
Recombinant Human MMP-1 protein pro form needs to be activated with p-aminophenylmercuric acetate (APMA).
Activation Protocol:
1. Dilute MMP1 to 50µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
2. Activate MMP1 by adding APMA to a final concentration of 1mM. (Sigma, Catalog # A9563) and 100mM stock in DMSO.
3. Incubate at 37°C for 2 hours.sds-page
More Info
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Introduction
MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.
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Synonyms
Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.
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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.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 :
AKR1C3 Human, HisDescription:
Aldo-Keto Reductase Family 1 Member C3 Human Recombinant, His Tag
DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.
Product # :
ENZ-406Price :
Quantity :
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Description
AKR1C3 Human Recombinant fused to 20 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 39 kDa. The AKR1C3 is fused to a 20 amino acid His tag purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1C3 solution contains 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: approximately < 0.1 units/mg.
Enzymatic activity was confirmed by measuring the amount of enzyme catalyzing the oxidation of 1 micromole NADPH per minute at 25C. Specific activity was expressed as units/mg protein.More Info
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Introduction
AKR1C3 is part of the aldo/keto reductase superfamily, which has at least 40 identified proteins. AKR1C3 catalyzes the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. AKR1C3 displays overlapping but distinct substrate specificity. AKR1C3 catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. AKR1C3 is involved in the pathogenesis of allergic diseases such as asthma. AKR1C3 controls cell growth and/or differentiation. AKR1C3 takes part in adrenal testosterone production. AKR1C3 expression is affected by metabolic disease, and its levels are considerably reduced in response to diet-induced weight loss and correlate with leptin levels.
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Synonyms
DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.
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Physical Appearance
Sterile Filtered clear 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 MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKPGLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD RNLHYFNSDS FASHPNYPYS DEY.
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 :
Noggin HumanDescription:
Noggin Human Recombinant
SYM1, SYNS1, NOG.
Product # :
CYT-475Price :
Quantity :
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Shipped at Room temp
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Description
Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.
More Info
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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
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Synonyms
SYM1, SYNS1, NOG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
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Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC. -
Background
Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.
Abstract:
Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.
Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.
This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.
Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
- Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.
Molecular Characteristics of Noggin :
- This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.
Inhibition of BMP Signaling by Noggin:
- Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.
Physiological Functions of Noggin:
- Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.
Therapeutic Implications of Noggin:
- The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.
Clinical Studies and Translational Research:
- This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.
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 :
SKA1 HumanDescription:
Spindle And Kinetochore Associated Complex Subunit 1 Human Recombinant
Spindle and kinetochore-associated protein 1, SKA1, C18orf24, Spindle And Kinetochore Associated Complex Subunit 1.
Product # :
PRO-1896Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SKA1 Human Recombinant produced in E. coli is a single polypeptide chain containing 278 amino acids (1-255) and having a molecular mass of 31.9 kDa.SKA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SKA1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Spindle And Kinetochore Associated Complex Subunit 1 (SKA1) is a part of the kinetochore-microtubule interface which associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. SKA1 is necessary for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint.
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Synonyms
Spindle and kinetochore-associated protein 1, SKA1, C18orf24, Spindle And Kinetochore Associated Complex Subunit 1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASSDLE QLCSHVNEKI GNIKKTLSLR NCGQEPTLKT VLNKIGDEII VINELLNKLE LEIQYQEQTN NSLKELCESL EEDYKDIEHL KENVPSHLPQ VTVTQSCVKG SDLDPEEPIK VEEPEPVKKP PKEQRSIKEM PFITCDEFNG VPSYMKSRLT YNQINDVIKE INKAVISKYK ILHQPKKSMN SVTRNLYHRF IDEETKDTKG RYFIVEADIK EFTTLKADKK FHVLLNILRH CRRLSEVRGG GLTRYVIT.
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 :
NTRK1 RatDescription:
Neurotrophic Receptor Tyrosine Kinase 1 Rat Recombinant
TRKA, TRK-A, NTRK-1.
Product # :
PKA-133Price :
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Shipped with Ice Packs
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Description
NTRK1 Rat Recombinant produced in HEK is a single, non-glycosylated polypeptide chain containing 623 amino acids (35-418 a.a) and having a molecular mass of 69 kDa. NTRK1 is fused to a 239 amino acid human IgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NTRK1 protein solution (1mg/ml) in Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to inhibit NGF-induced proliferation assay using TF1 human erythroleukemic cells in the presence of 0.5ng/ml of rat NGF. The ED50 range ≤ 5 ng/ml.
More Info
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Introduction
NTRK1 plays a role in the development and survival of nerve cells (neurons), specifically those that transmit dataregarding senses such as touch, pain and temperatureie. sensory neurons. NTRK1 protein is located on surface cells, mainly such as sensory neurons. NTRK1 acts as a kinase enzyme that alters the activity of different proteins by adding anoxygen cluster and phosphorus atoms at precise positions ie. phosphorylation. NTRK1 activated by nerve growth factor beta which binds to it and signals the NTRK1 protein to phosphorylate itself. Post autophosphorylation, the activated NTRK1 protein phosphorylates other proteins which is required for cell growth and survival.
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Synonyms
TRKA, TRK-A, NTRK-1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
NTRK1 although stable at 4°C for 1 week, should be stored 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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Amino Acid Sequence
SCRETCCPVG PSGLRCTRAG TLNTLRGLRG AGNLTELYVE NQRDLQRLEF EDLQGLGELR SLTIVKSGLR FVAPDAFHFT PRLSHLNLSS NALESLSWKT VQGLSLQDLT LSGNPLHCSC ALLWLQRWEQ EDLCGVYTQK LQGSGSGDQF LPLGHNNSCG VPSVKIQMPN DSVEVGDDVF LQCQVEGQAL QQADWILTEL EGTATMKKSG DLPSLGLTLV NVTSDLNKKN VTCWAENDVG RAEVSVQVSV SFPASVHLGK AVEQHHWCIP FSVDGQPAPS LRWFFNGSVL NETSFIFTQF LESALTNETM RHGCLRLNQP THVNNGNYTL LAANPYGQAA ASIMAAFMDN PFEFNPEDPI PVSFSPVDTN STSRDPVEKK DETP LEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HEV ORF2 (403-461 a.a.)Description:
Hepatitis E Virus ORF2 (403-461 a.a.) Recombinant
Product # :
HEV-272Price :
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Shipped with Ice Packs
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Description
The e.coli derived HEV protein is fused with beta-galactosidase at the N-Terminus and contains the HEV immunodominant regions from ORF2 403-461 a.a.
Formulation
20mM Tris-HCl pH-8, 8M urea and 10mM B-ME.
Purity
HEV ORF2 Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
Hepatitis E virus (HEV), the major etiologic agent of enterically transmitted non-A, non-B hepatitis worldwide, is a spherical, non-enveloped, single stranded RNA virus that is approximately 32 to 34 nm in diameter. HEV belongs to a genus of HEV-like viruses (unassigned genus). HEV has a single-stranded polyadenylated RNA genome of approximately 8 kb. Based on its physicochemical properties it is presumed to be a calici-like virus.
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Stability
HEV ORF2 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HEV ORF2 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HEV with minimal specificity problems.
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Specificity
Immunoreactive with sera HEV-infected individuals.
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Purification Method
HEV ORF2 was purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Leptin qA Human, PEGDescription:
Leptin Quadruple Antagonist Pegylated Human Recombinant
Product # :
CYT-1251Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DCTN2 (1-401) HumanDescription:
Dynactin 2 (1-401 a.a.) Human Recombinant
DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.
Product # :
PRO-1776Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (1-401 a.a) and having a molecular mass of 46.6kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.
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Synonyms
DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.
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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 MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAEE LTSTSVEHII VNPNAAYDKF KDKRVGTKGL DFSDRIGKTK RTGYESGEYE MLGEGLGVKE TPQQKYQRLL HEVQELTTEV EKIKTTVKES ATEEKLTPVL LAKQLAALKQ QLVASHLEKL LGPDAAINLT DPDGALAKRL LLQLEATKNS KGGSGGKTTG TPPDSSLVTY ELHSRPEQDK FSQAAKVAEL EKRLTELETA VRCDQDAQNP LSAGLQGACL METVELLQAK VSALDLAVLD QVEARLQSVL GKVNEIAKHK ASVEDADTQS KVHQLYETIQ RWSPIASTLP ELVQRLVTIK QLHEQAMQFG QLLTHLDTTQ QMIANSLKDN TTLLTQVQTT MRENLATVEG NFASIDERMK KLGK.
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.