Search: 1000 results found for "interleukin 8 (cxcl8)"

Description:

GRO-Beta Mouse Recombinant (CXCL2)

Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

Product # :

CHM-338

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Shipped at Room temp

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Description

GRO-Beta Mouse Recombinant also caled mouse MIP-2 produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7849 Dalton. The CXCL2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The Biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 10⁵-10⁶units/mg.

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Introduction
Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.
Synonyms
Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CXCL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 GRO-beta Mouse in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVVASELRCQ CLKTLPRVDF KNIQSLSVTP PGPHCAQTEV IATLKGGQKV CLDPEAPLVQ KIIQKILNKG KAN.
Background
What is the molecular weight/Mw of CXCL2 MOUSE Protein?
CXCL2 MOUSE Protein has a total Mw of 7.84kDa.

What is the source or expression system of CXCL2 MOUSE Protein?
Escherichia Coli.

What is the Purity of CXCL2 MOUSE Protein?
CXCL2 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL2 MOUSE Protein?
The Biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 105-106units/mg.

What is the amino acid sequence of CXCL2 MOUSE Protein?
AVVASELRCQ CLKTLPRVDF KNIQSLSVTP PGPHCAQTEV IATLKGGQKV CLDPEAPLVQ KIIQKILNKG KAN.

What applications can CXCL2 MOUSE Protein be used in?
CXCL2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL2 MOUSE Protein?
The endotoxin level is minimal, CXCL2 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL2 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL2 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.015 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of GRO-b as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-1 alpha Human Recombinant, His Tag

Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

Product # :

CYT-479

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Shipped with Ice Packs

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Description

IL-1A Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids fragment (113-271) with an amino-terminal hexahistidine tag and having a total molecular mass of 22.5kDa. The Interleukin-1 alpha His-tag is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-1 alpha His-tag protein is supplied in 1x PBS and 50% glycerol.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced by inflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
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. Please avoid freeze thaw cycles.
Background
What is the molecular weight/Mw of IL1A HUMAN, HIS Protein?
IL1A HUMAN, HIS Protein has a total Mw of 22.5kDa.

What is the source or expression system of IL1A HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL1A HUMAN, HIS Protein?
IL1A HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A HUMAN, HIS Protein?
The biological functionality of IL1A HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL1A HUMAN, HIS Protein?
IL1A HUMAN, HIS Protein is composed from 159 amino acids.

What applications can IL1A HUMAN, HIS Protein be used in?
IL1A HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A HUMAN, HIS Protein?
The endotoxin level is minimal, IL1A 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.

Description:

Interleukin-17E Mouse Recombinant

IL-25, IL-17E, IL17E, IL25, Interleukin-25.

Product # :

CYT-641

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Shipped at Room temp

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Description

Recombinant mouse IL-17E is a non-glycosylated, disulfide-linked homodimer, containing 2x145 amino acid chains, with a total molecular weight of 35.5 kDa. The Mouse IL-17E is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL17E was lyophilized from a concentrated (1mg/ml) solution containing no additives.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity is determined by the dose-dependent production of IL-8 by human PBMCs and is 322-488ng/ml.

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Introduction
IL-25 also called IL-17E cytokine has a sequence similarity with IL17.
IL-17E indluces NF-kappaB activation, and stimulates the production of IL-8. IL17E and IL17B are ligands for the cytokine receptor IL17BR. IL-25 is a proinflammatory cytokine favoring Th2-type immune response. The upregulation of costimulation-induced IL-17E receptors and release of cytokines and chemokines from IL-17E treated costimulated Th cells are differentially regulated by intracellular JNK, p38 MAPK and NF-kappaB activity. Blocking Iinterleukin-25 prevents airway hyperresponsiveness, a critical feature of clinical asthma. IL25 produced by innate effector eosinophils and basophils increase the allergic inflammation by enhancing the maintenance and functions of TSLP-DC activated adaptive Th2 memory cells. Over expression of IL-25 up-regulates gene expression of Th2 cytokines and induces growth retardation, jaundice, and multiorgan inflammation in a transgenic mouse model. IL-25 contributes to the induction and maintenance of eosinophilic inflammation by acting on lung fibroblasts which supports the fact that IL-17E is an important factor in asthma pathophysiology. IL-17E operates by amplifying TH2 cell-mediated allergic airway inflammation but doesn’t induce allergic inflammation in vivo.
Synonyms
IL-25, IL-17E, IL17E, IL25, Interleukin-25.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Murine IL17E although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17E 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 Mouse IL17E in sterile 10mM HCl at a concentration not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VSLRIQEGCSHLPSCCPSKEQEPPEEWLKWSSASVS
PPEPLSHTHHAESCRASKDGPLNSRAISPWSYELDRD
LNRVPQDLYHARCLCPHCVSLQTGSHMDPLGNSVPL
YHNQTVFYRRPCHGEEGTHRRYCLERRLYRVSLACV
CVRPRVMA.

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.

Description:

Interleukin-13 Rat Recombinant

NC300, ALRH, BHR1, P600, IL-13.

Product # :

CYT-391

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Quantity :

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Shipped at Room temp

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Description

Interleukin-13 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 113 amino acids and having a molecular mass of 12.7 kDa.The IL-13 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

ED₅₀ range = 2-6 ng/mL as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.

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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.
Synonyms
NC300, ALRH, BHR1, P600, IL-13.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of IL13 RAT Protein?
IL13 RAT Protein has a total Mw of 12.7kDa.

What is the source or expression system of IL13 RAT Protein?
Escherichia Coli.

What is the Purity of IL13 RAT Protein?
IL13 RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13 RAT Protein?
ED50 range = 2-6 ng/mL as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.

What is the amino acid sequence of IL13 RAT Protein?
IL13 RAT Protein is composed from 113 amino acids.

What applications can IL13 RAT Protein be used in?
IL13 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13 RAT Protein?
The endotoxin level is minimal, IL13 RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13 RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL13 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-13 as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-6 Mouse Recombinant

IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.

Product # :

CYT-350

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-6 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids and having a molecular mass of 21709 Dalton. The IL-6 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 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependant stimulation of the proliferation of IL-6-dependent murine 7TD1 cells is < 0.02 ng/ml, corresponding to a specific activity of > 50,000,000 units/mg.

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Introduction
Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.
Synonyms
IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 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 Mouse Il-6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQT.
Background
Research Paper on Interleukin-6 Mouse Recombinant
Abstract:
Interleukin-6 (IL-6) Mouse Recombinant stands at the forefront of immunological exploration, unraveling the intricacies of immune modulation. This research paper delves into its molecular attributes and implications within the realm of immunological studies. By examining its functions, synonyms like DIF, TNFA, and TNFSF2, and potential applications, we gain insights into its pivotal role in shaping immune responses.
Introduction:
IL-6 Mouse Recombinant has emerged as a linchpin in immunological research. This paper seeks to comprehensively elucidate its molecular characteristics and the impact it bears on immune mechanisms.
Molecular Architecture and Insights:
Delving into the molecular makeup of IL-6 Mouse Recombinant, we unveil its crucial role in immune signaling. Its interactions and functions contribute significantly to orchestrating immune responses.
Navigating Immune Dynamics:
The well-established influence of IL-6 on immune cell activation and inflammation is a cornerstone. IL-6 Mouse Recombinant allows for a more intricate exploration of these immune processes, augmenting our understanding of cytokine-mediated functions.
Synonyms and Network Connections:
Understanding the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2, amplifies our grasp of immune signaling networks. IL-6 Mouse Recombinant aids in unraveling the complexity of these interconnected pathways.
Potential Applications in Research and Beyond:
Beyond the confines of research, IL-6 Mouse Recombinant holds promise in deciphering immune-related diseases. Its significance extends to potential therapeutic interventions and diagnostic applications.
Clinical Implications and Future Prospects:
The clinical relevance of IL-6 Mouse Recombinant is underscored by its role in diseases characterized by altered IL-6 signaling. Unearthing its therapeutic potential paves the way for innovative strategies in disease management.
Conclusion:
Within the realm of immunology, IL-6 Mouse Recombinant assumes a pivotal role. Its molecular insights, fundamental functions, and potential applications position it as a cornerstone in advancing our comprehension of immune regulation.
What is the molecular weight/Mw of IL6 MOUSE Protein?
IL6 MOUSE Protein has a total Mw of 21.7kDa.

What is the source or expression system of IL6 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL6 MOUSE Protein?
IL6 MOUSE Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6 MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of IL-6-dependent murine 7TD1 cells is < 0.02 ng/ml, corresponding to a specific activity of > 50,000,000 units/mg.

What is the amino acid sequence of IL6 MOUSE Protein?
FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQT.

What applications can IL6 MOUSE Protein be used in?
IL6 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL6 MOUSE Protein?
The endotoxin level is minimal, IL6 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL6 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL6 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Interleukin-13 Rhesus Macaque Recombinant

NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.

Product # :

CYT-175

Price :

Quantity :

Shipping Method :

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

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.
Synonyms
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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.
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.
Amino Acid Sequence
SPSPVPRSTA LKELIEELVN ITQNQKAPLC NGSMVWSINL TAGVYCAALE SLINVSGCSA IEKTQRMLNG FCPHKVSAGQ FSSLRVRDTK IEVAQFVKDL LVHLKKLFRE GRFN
Background
What is the molecular weight/Mw of IL13 RHESUS MACAQUE Protein?
IL13 RHESUS MACAQUE Protein has a total Mw of 12.6kDa.

What is the source or expression system of IL13 RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of IL13 RHESUS MACAQUE Protein?
IL13 RHESUS MACAQUE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13 RHESUS MACAQUE Protein?
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.

What is the amino acid sequence of IL13 RHESUS MACAQUE Protein?
SPSPVPRSTA LKELIEELVN ITQNQKAPLC NGSMVWSINL TAGVYCAALE SLINVSGCSA IEKTQRMLNG FCPHKVSAGQ FSSLRVRDTK IEVAQFVKDL LVHLKKLFRE GRFN.

What applications can IL13 RHESUS MACAQUE Protein be used in?
IL13 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13 RHESUS MACAQUE Protein?
The endotoxin level is minimal, IL13 RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13 RHESUS MACAQUE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL13 RHESUS MACAQUE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Interleukin-1 alpha Rat Recombinant

Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

Product # :

CYT-381

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

Interleukin-1A Rat Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17703 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Tris-HCl, pH=8.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.

More Info

Introduction
Interleukin-1 alpha is a proinflammatory cytokine produced by a wide variety of cell types, including macrophages, osteoblasts, monocytes and hepatocytes. Circulating levels of are normally low and only rise after stimulation by agents such as those produced byinflammation, infection or microbial endotoxins. IL-1 alpha possesses a wide variety of biological activities and exerts its effects by binding to specific cell surface receptors.
Synonyms
Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A 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 Interleukin 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-His-Ser-Phe.
Background
What is the molecular weight/Mw of IL1A RAT Protein?
IL1A RAT Protein has a total Mw of 17.7kDa.

What is the source or expression system of IL1A RAT Protein?
Escherichia Coli.

What is the Purity of IL1A RAT Protein?
IL1A RAT Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A RAT Protein?
The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.005 ng/ml, corresponding to a Specific Activity of 200,000,000IU/mg.

What is the amino acid sequence of IL1A RAT Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-His-Ser-Phe.

What applications can IL1A RAT Protein be used in?
IL1A RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A RAT Protein?
The endotoxin level is minimal, IL1A RAT Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-18 Mouse Recombinant, His Tag

Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin, Il18.

Product # :

CYT-634

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Interleukin-18 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (36-192 a.a.) and having a molecular mass of 20.4 kDa. The Mouse IL-18 is fused to a 20 amino acids His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse IL-18 protein solution contains 20mM Tris-HCl pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.
Synonyms
Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin, Il18.
Physical Appearance
Sterile Filtered colorless liquid formulation.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNFGRLHCTT AVIRNINDQV LFVDKRQPVF EDMTDIDQSA SEPQTRLIIY MYKDSEVRGL AVTLSVKDSK MSTLSCKNKI ISFEEMDPPE NIDDIQSDLI FFQKRVPGHN KMEFESSLYE GHFLACQKED DAFKLILKKK DENGDKSVMF TLTNLHQS.

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.

Description:

Interleukin-16 Rhesus Macaque Recombinant

IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.

Product # :

CYT-153

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL 16 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of 12.5kDa.The IL 16 Rhesus Macaque is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2?m filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

Fully biologically active when compared to standard. Determined by its ability to chemoattract human CD4+ T-Lymphocytes using a concentration range of 50.0-100.0ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

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Introduction
IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4.
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-16 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 IL-16 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SAASASAASD VSVESSAEAT VYTVTLEKMS AGLGFSLEGG KGSLHGDKPL TINRIFKGAA SEQSETIQPG DEILQLAGTA MQGLTRFEAW NIIKALPDGP VTIVIRRKSL QPKETTAAAD S
Background
What is the molecular weight/Mw of IL16 RHESUS MACAQUE Protein?
IL16 RHESUS MACAQUE Protein has a total Mw of 12.5kDa.

What is the source or expression system of IL16 RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of IL16 RHESUS MACAQUE Protein?
IL16 RHESUS MACAQUE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL16 RHESUS MACAQUE Protein?
Fully biologically active when compared to standard. Determined by its ability to chemoattract human CD4+ T-Lymphocytes using a concentration range of 50.0-100.0ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

What is the amino acid sequence of IL16 RHESUS MACAQUE Protein?
SAASASAASD VSVESSAEAT VYTVTLEKMS AGLGFSLEGG KGSLHGDKPL TINRIFKGAA SEQSETIQPG DEILQLAGTA MQGLTRFEAW NIIKALPDGP VTIVIRRKSL QPKETTAAAD S.

What applications can IL16 RHESUS MACAQUE Protein be used in?
IL16 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL16 RHESUS MACAQUE Protein?
The endotoxin level is minimal, IL16 RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL16 RHESUS MACAQUE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL16 RHESUS MACAQUE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Interleukin-28A Mouse Recombinant

IFN-lambda-2, Interleukin-28A, IL-28A, Ifnl2, Il28a, EG330496.

Product # :

CYT-741

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Recombinant Mouse Interleukin-28A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids and having a total molecular mass of 19.7kDa.The IL-28A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse IL-28A is lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 and 5% trehalose.

Purity

Greater than 95% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by an anti-viral assay using human HepG2 cells infected with encephalomyocarditis(EMC) virus is less than 3 ng/ml, corresponding to a specific activity of > 3.3 × 10⁵ IU/mg.

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Introduction
IL-28A is distantly related to the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
Synonyms
IFN-lambda-2, Interleukin-28A, IL-28A, Ifnl2, Il28a, EG330496.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-Lambda 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 2 Recombinant 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 IL-28A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DPVPRATRLP VEAKDCHIAQ FKSLSPKELQ AFKKAKDAIE KRLLEKDMRC SSHLISRAWD LKQLQVQERP KALQAEVALT LKVWENMTDS ALATILGQPL HTLSHIHSQL QTCTQLQATA EPKPPSRRLS RWLHRLQEAQ SKETPGCLED SVTSNLFRLL TRDLKCVASG DQCV.

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.

Description:

Interleukin-32 alpha Human Recombinant

NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.

Product # :

CYT-584

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 131 amino acids and having a molecular mass of 14.9 kDa.

Source

Escherichia Coli.

Formulation

IL-32 was lyophilized from a concentrated (1mg/ml) solution in water containing 50mM sodium Phosphate buffer pH=7.5.

Purity

Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Human IL-32 alpha activity is measured via the dose-dependent induction of TNF-alpha in the human THP-1 monocytic cell line.

More Info

Introduction
IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function.
Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine, which is particularly stimulated by mycobacteria through a caspase-1- and IL-18-dependent production of IFNgamma.
IL-32 is associated with TNF-a, IL-1beta, and IL-18. IL32 is involved in human rheumatoid arthritis and is a novel target in autoimmune diseases.
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL32 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL32 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 IL-32 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MCFPKVLSDD MKKLKARMHQ AIERFYDKMQ NAESGRGQVM SSLAELEDDF KEGYLETVAA YYEEQHPELT PLLEKERDGL RCRGNRSPVP DVEDPATEEP GESFCDKSYG APRGDKEELT PQKCSEPQSS K.

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.

Description:

Interleukin-3 Human Recombinant, His Tag

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

CYT-482

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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SDS-PAGE
Citations

Description

Interleukin-3 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 154 amino acids fragment (20-152) and having a total molecular mass of 17.3kDa and fused with a 20 aa N-terminal His tag. The IL3 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-3 His (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH 8.0), 0.2mM PMSF and 10% glycerol.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

Biological Activity

The ED50 for this effect is <0.53ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.

SDS-PAGE

More Info

Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells. IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPMTQTTSL KTSWVNCSNM IDEIITHLKQ PPLPLLDFNN LNGEDQDILM ENNLRRPNLE AFNRAVKSLQ NASAIESILK NLLPCLPLAT AAPTRHPIHI KDGDWNEFRR KLTFYLKTLE NAQAQQTTLS LAIF.
Background
What is the molecular weight/Mw of IL3 HUMAN, HIS Protein?
IL3 HUMAN, HIS Protein has a total Mw of 17.3kDa.

What is the source or expression system of IL3 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL3 HUMAN, HIS Protein?
IL3 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL3 HUMAN, HIS Protein?
The ED50 for this effect is <0.53ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.

What is the amino acid sequence of IL3 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MAPMTQTTSL KTSWVNCSNM IDEIITHLKQ PPLPLLDFNN LNGEDQDILM ENNLRRPNLE AFNRAVKSLQ NASAIESILK NLLPCLPLAT AAPTRHPIHI KDGDWNEFRR KLTFYLKTLE NAQAQQTTLS LAIF.

What applications can IL3 HUMAN, HIS Protein be used in?
IL3 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL3 HUMAN, HIS Protein?
The endotoxin level is minimal, IL3 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL3 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL3 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Interleukin-13 109 a.a. Rat Recombinant

NC300, ALRH, BHR1, P600, IL-13.

Product # :

CYT-182

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-13 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids and having a molecular mass of 11.9 kDa. The IL-13 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized in PBS, pH7.4.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

ED₅₀ range = 40ng/ml, corresponding to a specific activity of > 25,000IU/mg as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.

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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.
Synonyms
NC300, ALRH, BHR1, P600, IL-13.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VRRSTSPPVA LRELIEELSN ITQDQKTSLC NSSIVWSVDI TAGGFCAALE SLTNISSCNA IHRTQRILNG LCNQKASDVA SSPPDTKIEV AQFISKLLNY SKQLFRYGH.
Background
What is the molecular weight/Mw of IL13 RAT 109 A.A. Protein?
IL13 RAT 109 A.A. Protein has a total Mw of 11.9kDa.

What is the source or expression system of IL13 RAT 109 A.A. Protein?
Escherichia Coli.

What is the Purity of IL13 RAT 109 A.A. Protein?
IL13 RAT 109 A.A. Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13 RAT 109 A.A. Protein?
ED50 range = 40ng/ml, corresponding to a specific activity of > 25,000IU/mg as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.
What is the amino acid sequence of IL13 RAT 109 A.A. Protein?
VRRSTSPPVA LRELIEELSN ITQDQKTSLC NSSIVWSVDI TAGGFCAALE SLTNISSCNA IHRTQRILNG LCNQKASDVA SSPPDTKIEV AQFISKLLNY SKQLFRYGH.

What applications can IL13 RAT 109 A.A. Protein be used in?
IL13 RAT 109 A.A. Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13 RAT 109 A.A. Protein?
The endotoxin level is minimal, IL13 RAT 109 A.A. Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13 RAT 109 A.A. that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL13 RAT 109 A.A.?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-13 as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-36 Beta 153 a.a Human Recombinant

Interleukin 36 beta, interleukin 1 family member 8 (eta), Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily e, IL1H2, MGC126880, MGC126882.

Product # :

CYT-180

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL36B 153 a.a. Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 153 amino acids (5-157a.a.) and having a molecular mass of 17.2kDa.The IL36B 153 a.a. Human is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE and HPLC analyses.

Biological Activity

Fully biologically active when compared to standard. The ED50 as measured by its ability to induce IL-8 secretion in human preadipocytes is less than 10ng/ml, corresponding to a specific activity of 10IU/mg.

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Introduction
Human IL-36b belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36 beta is known to be actively secreted. Cells expressing IL-36 beta include resting and activated monocytes and B cells. The receptor for IL-36 beta is a blend of IL-1 Rrp2 and IL-1 RAcP. Recombinant IL-36 beta stimulates processes involving NF-kB and MAPK in an IL-1 Rrp2-dependent manner.
Synonyms
Interleukin 36 beta, interleukin 1 family member 8 (eta), Interleukin-1 homolog 2, IL1F8 (Canonical product IL-1F8a), IL-1F8 (FIL1-eta), Interleukin-1 Superfamily e, IL1H2, MGC126880, MGC126882.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL36B 153 a.a. Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36B 153 a.a. Human 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 IL36B 153 a.a. Human in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
REAAPKSYAI RDSRQMVWVL SGNSLIAAPL SRSIKPVTLH LIACRDTEFS DKEKGNMVYL GIKGKDLCLF CAEIQGKPTL QLKEKNIMDL YVEKKAQKPF LFFHNKEGST SVFQSVSYPG WFIATSTTSG QPIFLTKERG ITNNTNFYLD SVE

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.

Description:

Interleukin-17F Mouse Recombinant

Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.

Product # :

CYT-642

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL17F Mouse Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 266 amino acids and having a molecular mass of 29.8 kDa. The Mouse IL-17F is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL17F was lyophilized from a concentrated (1mg/ml) solution containing no additives.

Purity

Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM-CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Murine IL17F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17F 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 Mouse IL17F in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RKNPKAGVPALQKAGNCPPLEDNTVRVDIRIFNQNQGISVPREFQNRSSSP
WDYNITRDPHRFPSEIAEAQCRHSGCINAQGQEDSTMNSVAIQQEILVLRR
EPQGCSNSFRLEKMLLKVGCTCVKPIVHQAA.

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.

Description:

Interleukin-2 Receptor (CD25), Rat Anti-Mouse

CD25, IL2R, TCGFR, IL-2RA, sIL-2RA, TAC antigen, sIL-2R, IDDM10, p55.

Product # :

ANT-103

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
IL2-Ra is one of the three constituent subunits of the IL2 receptor. IL-2Ra is released into the serum after increased cellular expression such as increased activation of B and T cells. Clinical manifestations of IL2-Ra elevation include autoimmune conditions and some leukemias and lymphomas.
Synonyms
CD25, IL2R, TCGFR, IL-2RA, sIL-2RA, TAC antigen, sIL-2R, IDDM10, p55.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Con A-activated T cells.
Ig Subclass
Rat IgG1.
Clone
NYRmIL-2R.
Titer
1:1,000 dilution will block T cell proliferation induced by specific Ag or concanavaline A. 10µl will stain 106 IL-R positive cells for FACS analysis.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Rat Anti Mouse Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Ion exchange.

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.

Description:

Interleukin-3 Rat Recombinant

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

CYT-383

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
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Description

Interleukin-3 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids and having a molecular mass of 16.3kDa. The IL-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-3 Rat was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of the proliferation of thymidine uptake by murine MC-9 cells is < 10 ng/ml, corresponding to a specific activity of >1.0 x 10⁵ units/mg.

More Info

Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells.
IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 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 Interleukin 3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MISDRGSDAH HLLRTLDCRT IALEILVKLP YPQVSGLNNS DDKANLRNST LRRVNLDEFL KSQEEFDSQD TTDIKSKLQK LKCCIPAAAS DSVLPGVYNK DLDDFKKKLR FYVIHLKDLQ PVSVSRPPQP TSSSDNFRPM TVEC.
Background
What is the molecular weight/Mw of IL 3 RAT Protein?
IL 3 RAT Protein has a total Mw of 16.3kDa.

What is the source or expression system of IL 3 RAT Protein?
Escherichia Coli.

What is the Purity of IL 3 RAT Protein?
IL 3 RAT Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 RAT Protein?
The ED50 as determined by the dose-dependent stimulation of the proliferation of thymidine uptake by murine MC-9 cells is < 10 ng/ml, corresponding to a specific activity of >1.0 x 105 units/mg.

What is the amino acid sequence of IL 3 RAT Protein?
MISDRGSDAH HLLRTLDCRT IALEILVKLP YPQVSGLNNS DDKANLRNST LRRVNLDEFL KSQEEFDSQD TTDIKSKLQK LKCCIPAAAS DSVLPGVYNK DLDDFKKKLR FYVIHLKDLQ PVSVSRPPQP TSSSDNFRPM TVEC.

What applications can IL 3 RAT Protein be used in?
IL 3 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 3 RAT Protein?
The endotoxin level is minimal, IL 3 RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 3 RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 3 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Interleukin-33 Rat Recombinant, His Tag

Interleukin-33, IL-33.

Product # :

CYT-906

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
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Description

IL 33 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (109-264 a.a) and having a molecular mass of 19.8kDa. IL 33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 33 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
nterleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
Synonyms
Interleukin-33, IL-33.
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
MGSSHHHHHH SSGLVPRGSH MGSSIQGTSL LTESCALSTY NDQSVSFVLE NGCYVINVED CGKNQEKDKV LLRYYESSFP AQSGDGVDGK KLMVNMSPIK DTDIWLNAND KDYSVELQKG DVSPPDQAFF VLHKKSSDFV SFECKNLPGT YIGVKDNQLA LVEENDESCN NIMFKLSKM.

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.

Description:

Interleukin-4 Mouse Recombinant

BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.

Product # :

CYT-282

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

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source
formulation
purity
biological activity
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Description

Interleukin-4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids and having a molecular mass of 13500 Dalton. The IL-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm concentrated (1mg/ml) solution in PBS pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependant induction of HT-2 cell proliferation is less than 2 ng/ml corresponding to a Specific Activity of 500,000IU/mg.

More Info

Introduction
Interleukin-4 is a pleiotropic cytokine produced primarily by activated T lymphocytes, basophils and mast cells. Multiple immune response-modulating functions are performed by IL-4 on a variety of cell types and it has an important role in the regulator of isotype switching, induction of IgE production in B lymphocytes and differentiation of precursor T helper cells. IL-4 binds to both membrane-bound and secreted soluble IL-4 receptors.
Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 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 Interleukin 4 in sterile 10mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MHIHGCDKNH LREIIGILNE VTGEGTPCTE MDVPNVLTAT KNTTESELVC RASKVLRIFY LKHGKTPCLK KNSSVLMELQ RLFRAFRCLD SSISCTMNES KSTSLKDFLE SLKSIMQMDY S.
Background
What is the molecular weight/Mw of IL 4 MOUSE Protein?
IL 4 MOUSE Protein has a total Mw of 13.5kDa.

What is the source or expression system of IL 4 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL 4 MOUSE Protein?
IL 4 MOUSE Protein is >96% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 MOUSE Protein?
The ED50 as determined by the dose-dependant induction of HT-2 cell proliferation is less than 2 ng/ml corresponding to a Specific Activity of 500,000IU/mg.

What is the amino acid sequence of IL 4 MOUSE Protein?
MHIHGCDKNH LREIIGILNE VTGEGTPCTE MDVPNVLTAT KNTTESELVC RASKVLRIFY LKHGKTPCLK KNSSVLMELQ RLFRAFRCLD SSISCTMNES KSTSLKDFLE SLKSIMQMDY S.

What applications can IL 4 MOUSE Protein be used in?
IL 4 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 4 MOUSE Protein?
The endotoxin level is minimal, IL 4 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 4 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 4 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Interleukin-15 Mouse Recombinant

IL-15, MGC9721, Interleukin-15, Il15, AI503618.

Product # :

CYT-647

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
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Description

Interleukin-15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (49-162 a.a.) and having a molecular mass of 17.6 kDa. The IL-15 is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The mouse IL-15 protein solution contains PBS, 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 CTLL2 mouse cytotoxic T cells. The ED50 for this effect is < 1 ng/ml, corresponding to a specific activity of 1,000,000IU/mg.

More Info

Introduction
The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.
Synonyms
IL-15, MGC9721, Interleukin-15, Il15, AI503618.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMNW IDVRYDLEKI ESLIQSIHID TTLYTDSDFH PSCKVTAMNC FLLELQVILH
EYSNMTLNET VRNVLYLANS TLSSNKNVAE SGCKECEELE EKTFTEFLQS FIRIVQMFIN TS.
Background
What is the molecular weight/Mw of IL15 MOUSE Protein?
IL15 MOUSE Protein has a total Mw of 17.6kDa.

What is the source or expression system of IL15 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL15 MOUSE Protein?
IL15 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL15 MOUSE Protein?
Measured in a cell proliferation assay using CTLL2 mouse cytotoxic T cells. The ED50 for this effect is < 1 ng/ml, corresponding to a specific activity of 1,000,000IU/mg.

What is the amino acid sequence of IL15 MOUSE Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMNW IDVRYDLEKI ESLIQSIHID TTLYTDSDFH PSCKVTAMNC FLLELQVILH
EYSNMTLNET VRNVLYLANS TLSSNKNVAE SGCKECEELE EKTFTEFLQS FIRIVQMFIN TS.

What applications can IL15 MOUSE Protein be used in?
IL15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL15 MOUSE Protein?
The endotoxin level is minimal, IL15 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL15 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL15 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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.

Description:

Interleukin-22 Mouse Recombinant

IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

Product # :

CYT-539

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids and having a molecular mass of 16.7 kDa. The Murine IL-22 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from 1X PBS.

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 its ability to induce IL-10 secretion in Colo205 cells is less than 0.5ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.

More Info

Introduction
Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10R? (previously known as CRF2-4), belonging to the class II cytokine receptor family.
Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 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 Interleukin -22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Pro-Val-Asn.

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.

Description:

Interleukin-1 beta Human Recombinant, His Tag

Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

Product # :

CYT-480

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

Interleukin-1 beta His-Tag Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 153 amino acids fragment (117-269) and having a total molecular mass of 21.88 kDa fused with an amino-terminal hexahistidine tag. The IL-1b His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-1b His tag protein solution is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-1b is a potent pro-inflammatory cytokine produced by a wide variety of cell types including monocytes and macrophages. It displays a broad range of biological activity including activation of B and T cells in response to inflammation and the activation of endothelial cells.
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
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. Please avoid freeze thaw cycles.
Amino Acid Sequence
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV
QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME
KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS
Background
What is the molecular weight/Mw of IL1B HUMAN, HIS Protein?
IL1B HUMAN, HIS Protein has a total Mw of 21.88kDa.

What is the source or expression system of IL1B HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL1B HUMAN, HIS Protein?
IL1B HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B HUMAN, HIS Protein?
The biological functionality of IL1B HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL1B HUMAN, HIS Protein?
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV
QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME
KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS.

What applications can IL1B HUMAN, HIS Protein be used in?
IL1B HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1B HUMAN, HIS Protein?
The endotoxin level is minimal, IL1B 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.

Description:

Interleukin-35 Human Recombinant

Product # :

CYT-842

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Description

IL35 Human Recombinant produced in HEK 293 cells is comprised of a p35 subunit from IL-12 (Accession # p29459) and a EBI3 (Accession # q14213) subunit from IL-27. IL35 is a heterodimeric polypeptide chain containing 406 amino acids, with a predicted molecular weight of 45.8 kDa.

Source

HEK 293 cells.

Formulation

Lyophilized from a concentrated solution containing 10mM Na2PO4 pH 7.5 and 30mM NaCl.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

More Info

Introduction
Interleukin-35 is a glycosylated, disulfide-linked, heterodimeric protein comprised of the p35 subunit of IL-12 (IL-12 alpha) and the beta subunit of IL-27 (EBI3). IL35 is expressed by regulatory T-cells (Tregs), macrophages and some trophoblast and dendritic cells. IL-35 is produced in response to inflammation and generally serves as an inflammation suppressor. Interleukin-35 curbs inflammation by applying multiple activities, including the stimulation of regulatory T-cells and the inhibition of Th17 cells.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL35 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL35 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 IL35 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EBI3 subunit:RKGPPAALTL PRVQCRASRY PIAVDCSWTL PPAPNSTSPV SFIATYRLGM AARGHSWPCL QQTPTSTSCT ITDVQLFSMA PYVLNVTAVH PWGSSSSFVP FITEHIIKPD PPEGVRLSPL AERQLQVQWE PPGSWPFPEI FSLKYWIRYK RQGAARFHRV GPIEATSFIL RAVRPRARYY VQVAAQDLTD YGELSDWSLP ATATMSLGKp35 subunit:RNLPVATPDP GMFPCLHHSQ NLLRAVSNML QKARQTLEFY PCTSEEIDHE DITKDKTSTV EACLPLELTK NESCLNSRET SFITNGSCLA SRKTSFMMAL CLSSIYEDLK MYQVEFKTMN AKLLMDPKRQ IFLDQNMLAV IDELMQALNF NSETVPQKSS LEEPDFYKTK IKLCILLHAF RIRAVTIDRV MSYLNAS

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.

Description:

Monocyte Chemotactic Protein-1 Human Recombinant (CCL2), His Tag

Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

Product # :

CHM-246

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
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purity
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SDS-PAGE
Citations

Description

MCP-1 Human Recombinant also known as Monocyte Chemotactic and Activating Factor (MCAF) produced in E.Coli is a non-glycosylated, Polypeptide chain containing 97 amino acids (24-99) and having a molecular mass of 10.9 kDa. The MCP-1 is fused to 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The His Tag MCP-1 protein (1mg/ml) solution contains 20mM Tris-HCL pH-8.0, 1mM DTT and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQPDAINAPV TCCYNFTNRK ISVQRLASYR RITSSKCPKE AVIFKTIVAK EICADPKQKW VQDSMDHLDK QTQTPKT.
Background
What is the molecular weight/Mw of CCL2 HUMAN, HIS Protein?
CCL2 HUMAN, HIS Protein has a total Mw of 10.9kDa.

What is the source or expression system of CCL2 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CCL2 HUMAN, HIS Protein?
CCL2 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 HUMAN, HIS Protein?
The biological functionality of CCL2 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL2 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQPDAINAPV TCCYNFTNRK ISVQRLASYR RITSSKCPKE AVIFKTIVAK EICADPKQKW VQDSMDHLDK QTQTPKT.

What applications can CCL2 HUMAN, HIS Protein be used in?
CCL2 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL2 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL2 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL2 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL2 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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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Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info