Search: 1000 results found for "Anti Human Cytokine"

Description:

Interleukin-13 Variant Human Recombinant

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

Product # :

CYT-682

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Shipped at Room temp

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Description

Interleukin-13 Variant Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids, with a substitution of Q for R at position 112 compared with the wild type IL-13, having a molecular mass of 12.5 kDa. The IL-13 Variant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.2, containing 5% trehalose.

Purity

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

Biological Activity

The ED50 was determined by the dose dependent prolifiration of TF-1 cells and was found to be < 1ng/ml, corresponding to a specific activity of >1,000,000 units/mg. This analog has also been shown to exhibit increased in vivo activity compared to wild type IL-13.

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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
Interleukin-13, NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-13 Variant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 Variant 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 Variant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPGPVPPSTA LRELIEELVN ITQNQKAPLC NGSMVWSINL TAGMYCAALE SLINVSGCSA IEKTQRMLSG FCPHKVSAGQ FSSLHVRDTK IEVAQFVKDL LLHLKKLFRE GQFN.
Background
What is the molecular weight/Mw of IL13 VARIANT HUMAN Protein?
IL13 VARIANT HUMAN Protein has a total Mw of 12.5kDa.

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

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

What is the Biological Activity of IL13 VARIANT HUMAN Protein?
The ED50 was determined by the dose dependent prolifiration of TF-1 cells and was found to be < 1ng/ml, corresponding to a specific activity of >1,000,000 units/mg. This analog has also been shown to exhibit increased in vivo activity compared to wild type IL-13.

What is the amino acid sequence of IL13 VARIANT HUMAN Protein?
SPGPVPPSTA LRELIEELVN ITQNQKAPLC NGSMVWSINL TAGMYCAALE SLINVSGCSA IEKTQRMLSG FCPHKVSAGQ FSSLHVRDTK IEVAQFVKDL LLHLKKLFRE GQFN.

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

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

Who supplies recombinant IL13 VARIANT HUMAN 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 VARIANT HUMAN?
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:

Epstein Barr Virus Induced 3 Human Recombinant, His Tag

Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.

Product # :

CYT-668

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Shipped with Ice Packs

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Description

EBI3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 209 amino acids fragment (21-229) having a molecular weight of 34kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The EBI3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EBI3 protein is supplied in 1xPBS, 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
Synonyms
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
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 EBI3 Protein?
EBI3 Protein has a total Mw of 34kDa.

What is the source or expression system of EBI3 Protein?
Escherichia Coli.

What is the Purity of EBI3 Protein?
EBI3 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of EBI3 Protein?
The biological functionality of EBI3 Protein will be determined in the future.

What is the amino acid sequence of EBI3 Protein?
EBI3 Protein is composed from 209 amino acids.

What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 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 12 Receptor Beta 1 Human Recombinant

Interleukin 12 Receptor Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R.

Product # :

CYT-862

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Shipping Method :

Shipped with Ice Packs

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Description

IL12RB1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 568 amino acids (1-545 a.a) and having a molecular mass of 62.6kDa. IL12RB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL12RB1 protein solution (0.25mg/ml) containing 20mM TRIS 8.0 buffer and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
IL-12 is a heterodimeric cytokine that stimulates the production of IFN gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.
Synonyms
Interleukin 12 Receptor Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R.
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 MGSMEPLVTW VVPLLFLFLL SRQGAACRTS ECCFQDPPYP DADSGSASGP RDLRCYRISS DRYECSWQYE GPTAGVSHFL RCCLSSGRCC YFAAGSATRL QFSDQAGVSV LYTVTLWVES WARNQTEKSP EVTLQLYNSV KYEPPLGDIK VSKLAGQLRM EWETPDNQVG AEVQFRHRTP SSPWKLGDCG PQDDDTESCL CPLEMNVAQE FQLRRRQLGS QGSSWSKWSS PVCVPPENPP QPQVRFSVEQ LGQDGRRRLT LKEQPTQLEL PEGCQGLAPG TEVTYRLQLH MLSCPCKAKA TRTLHLGKMP YLSGAAYNVA VISSNQFGPG LNQTWHIPAD THTEPVALNI SVGTNGTTMY WPARAQSMTY CIEWQPVGQD GGLATCSLTA PQDPDPAGMA TYSWSRESGA MGQEKCYYIT IFASAHPEKL TLWSTVLSTY HFGGNASAAG TPHHVSVKNH SLDSVSVDWA PSLLSTCPGV LKEYVVRCRD EDSKQVSEHP VQPTETQVTL SGLRAGVAYT VQVRADTAWL RGVWSQPQRF SIEVQVSD.
Background
What is the molecular weight/Mw of IL12RB1 HUMAN Protein?
IL12RB1 HUMAN Protein has a total Mw of 62.6kDa.

What is the source or expression system of IL12RB1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL12RB1 HUMAN Protein?
IL12RB1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12RB1 HUMAN Protein?
The biological functionality of IL12RB1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL12RB1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMEPLVTW VVPLLFLFLL SRQGAACRTS ECCFQDPPYP DADSGSASGP RDLRCYRISS DRYECSWQYE GPTAGVSHFL RCCLSSGRCC YFAAGSATRL QFSDQAGVSV LYTVTLWVES WARNQTEKSP EVTLQLYNSV KYEPPLGDIK VSKLAGQLRM EWETPDNQVG AEVQFRHRTP SSPWKLGDCG PQDDDTESCL CPLEMNVAQE FQLRRRQLGS QGSSWSKWSS PVCVPPENPP QPQVRFSVEQ LGQDGRRRLT LKEQPTQLEL PEGCQGLAPG TEVTYRLQLH MLSCPCKAKA TRTLHLGKMP YLSGAAYNVA VISSNQFGPG LNQTWHIPAD THTEPVALNI SVGTNGTTMY WPARAQSMTY CIEWQPVGQD GGLATCSLTA PQDPDPAGMA TYSWSRESGA MGQEKCYYIT IFASAHPEKL TLWSTVLSTY HFGGNASAAG TPHHVSVKNH SLDSVSVDWA PSLLSTCPGV LKEYVVRCRD EDSKQVSEHP VQPTETQVTL SGLRAGVAYT VQVRADTAWL RGVWSQPQRF SIEVQVSD.
What applications can IL12RB1 HUMAN Protein be used in?
IL12RB1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12RB1 HUMAN Protein?
The endotoxin level is minimal, IL12RB1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12RB1 HUMAN 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 IL12RB1 HUMAN?
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-7 Human Recombinant, sf9

Interleukin 7, IL-7, Interleukin-7.

Product # :

CYT-975

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 161 amino acids (26-177 a.a.) and having a molecular mass of 18.4kDa. IL7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL7 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.
Synonyms
Interleukin 7, IL-7, Interleukin-7.
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
ADPDCDIEGK DGKQYESVLM VSIDQLLDSM KEIGSNCLNN EFNFFKRHIC DANKEGMFLF RAARKLRQFL KMNSTGDFDL HLLKVSEGTT ILLNCTGQVK GRKPAALGEA QPTKSLEENK SLKEQKKLND LCFLKRLLQE IKTCWNKILM GTKEHHHHHH H
Background
What is the molecular weight/Mw of IL7 HUMAN, SF9 Protein?
IL7 HUMAN, SF9 Protein has a total Mw of 18.4kDa.

What is the source or expression system of IL7 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL7 HUMAN, SF9 Protein?
IL7 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL7 HUMAN, SF9 Protein?
The biological functionality of IL7 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of IL7 HUMAN, SF9 Protein?
ADPDCDIEGK DGKQYESVLM VSIDQLLDSM KEIGSNCLNN EFNFFKRHIC DANKEGMFLF RAARKLRQFL KMNSTGDFDL HLLKVSEGTT ILLNCTGQVK GRKPAALGEA QPTKSLEENK SLKEQKKLND LCFLKRLLQE IKTCWNKILM GTKEHHHHHH H.

What applications can IL7 HUMAN, SF9 Protein be used in?
IL7 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL7 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL7 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL7 HUMAN, SF9 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 IL7 HUMAN, SF9?
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:

I-TAC Human Recombinant (CXCL11), His Tag

Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.

Product # :

CHM-232

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

I-TAC (CXCL11) Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 94 amino acids (22-94) and having a molecular mass of 10.6kDa.I-TAC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The I-TAC solution (1mg/ml) contains 10mM sodium citrate(pH 3.5), 20% glycerol and 2mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Chemokine (C-X-C motif) ligand 11 (CXCL11) is a small cytokine belonging to the CXC chemokine family that is also called Interferon-inducible T-cell alpha chemoattractant (I-TAC) and Interferon-gamma-inducible protein 9 (IP-9). It is highly expressed in peripheral blood leukocytes, pancreas and liver, with moderate levels in thymus, spleen and lung and low expression levels were in small intestine, placenta and prostate. Gene expression of CXCL11 is strongly induced by IFN-g and IFN-b, and weakly induced by IFN-a. This chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10. CXCL11 is chemotactic for activated T cells. Its gene is located on human chromosome 4 along with many other members of the CXC chemokine family.
Synonyms
Small inducible cytokine B11, CXCL11, Interferon-inducible T-cell alpha chemoattractant, I-TAC, Interferon-gamma-inducible protein 9, IP-9, H174, Beta-R1, chemokine (C-X-C motif) ligand 11, IP9, b-R1, SCYB11, SCYB9B, MGC102770.
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 MFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF.
Background
What is the molecular weight/Mw of CXCL11 HUMAN, HIS Protein?
CXCL11 HUMAN, HIS Protein has a total Mw of 10.6kDa.

What is the source or expression system of CXCL11 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL11 HUMAN, HIS Protein?
CXCL11 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL11 HUMAN, HIS Protein?
The biological functionality of CXCL11 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF.

What applications can CXCL11 HUMAN, HIS Protein be used in?
CXCL11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL11 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL11 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL11 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 CXCL11 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-17A (75-155 a.a) Human Recombinant

IL-17A, Interleukin 17A, CTLA8, IL17.

Product # :

CYT-1236

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

The IL17A Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The IL17A His-Tagged Fusion Protein, produced in E. coli, is a 14kDa protein containing 81 amino acid residues of the IL17A Human, 75-155 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Synonyms
IL-17A, Interleukin 17A, CTLA8, IL17.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized IL17A 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.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
LHRNE DPERYPSVIW EAKCRHLGCI NADGNVDYHM NSVPIQQEILVLRREPPHCP NSFRLEKILV SVGCTCVTPI VHHVA
Background
IL17 is a proinflammatory cytokine produced by activated T cells. IL-17A takes an important part in immune responses, particularly in host defense against infections and in the pathogenesis of various autoimmune diseases. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 stimulates the expression of IL6 and cyclooxygenase-2 and enhances the production of nitric oxide.

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 Human Recombinant

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

Product # :

CYT-211

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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biological activity
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Description

Interleukin-4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 15kDa. The IL-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

Purity

Greater than 98% 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 TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5x106 IU/mg.

More Info

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 IL-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.
Solubility
It is recommended to reconstitute the lyophilized IL-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.
Background
Everything You Should Know About IL-4 Human Recombinant
Interleukin-4 (IL-4) is an important type-2 cytokine with multiple effects on numerous cells and tissues in the body. As such, it's crucial for the immune system's maintenance and function.
Recent advancements have led to the development of interleukin-4 (rhIL-4) human recombinant in laboratories. As a result, experts have started studying its potential uses and therapeutic applications.
If you're interested in learning more about IL-4 human recombinant, check out the information below!
How Does Interleukin-4 (IL-4) Work?
Interleukin-4 (IL-4) acts as a signaling molecule, specifically a protein. It communicates with various immune cells by binding to specific receptors on their surface.
This process triggers responses against common threats, such as allergens, contaminants, and infections.
IL-4 is produced by T helper 2 (Th2) cells (a type of white blood cells), mast cells, eosinophils, and basophils.
What Interleukin-4 (IL-4) Does
As mentioned, this type-2 cytokine has multiple effects on various cells and tissues, so it fulfills several functions. Below are the most important ones:
- Th2 cell differentiation: IL-4 promotes the differentiation of T cells, triggering the response of Th2 cells, which fight parasites and regulate allergic responses.
- B cell activation and antibody production: IL-4 stimulates B cells, helping them proliferate and produce antibodies, particularly immunoglobulin E (IgE), which is involved in allergic reactions.
- Inflammation reduction: IL-4 can promote inflammation to address threats, such as allergens or parasites, and suppress it when necessary, depending on the context.
- Tissue repair and remodeling: IL-4 is key for tissue repair and remodeling processes, such as wound healing and fibrosis.
What Is IL-4 Human Recombinant?
IL-4 human recombinant is a version produced in a laboratory using DNA technology. The cytokine is inserted into a host organism, commonly E. Coli bacteria, for mass production.
This method allows experts to obtain pure and contaminant-free rhIL-4 with uniform biological activity and in large quantities.
What Can IL-4 Human Recombinant Be Used For?
Since this cytokine plays a key role in different processes, it may have multiple therapeutic applications for numerous diseases. These are the most common:
- Allergic diseases, such as asthma, rhinitis, and eczema
- Autoimmune diseases, such as rheumatoid arthritis and multiple sclerosis
- Infectious diseases, including those caused by parasites and viruses
- Cancer, as research suggests IL-4 could enhance the immune system's ability to fight cancer cells
Final Thoughts
The future of IL-4 human recombinant seems promising. This laboratory-produced version of an essential type-2 cytokine may be key to developing innovative therapies. However, more research is needed on potential applications to determine if it's safe and effectiv.
What is the molecular weight/Mw of IL 4 HUMAN Protein?
IL 4 HUMAN Protein has a total Mw of 15kDa.

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

What is the Purity of IL 4 HUMAN Protein?
IL 4 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.2 ng/ml, corresponding to a Specific Activity of 5x106 IU/mg.

What is the amino acid sequence of IL 4 HUMAN Protein?
HKCDITLQE IIKTLNSLTE QKTLCTELTV TDIFAASKNT TEKETFCRAA TVLRQFYSHH EKDTRCLGAT AQQFHRHKQL IRFLKRLDRN LWGLAGLNSC PVKEANQSTL ENFLERLKTI MREKYSKCSS.

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

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

Who supplies recombinant IL 4 HUMAN 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 HUMAN?
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 0.594 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-4 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:

Vaspin Human Recombinant, His Tag

Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

Product # :

CYT-459

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.
Synonyms
Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Liquid Vaspin although stable at 10°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.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.

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:

Adiponectin glycosylated Human Recombinant, HMW Rich

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-764

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.

Source

HEK293.

Formulation

Acrp30 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl, pH 7.5 and 1mM CaCl2.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Acrp30 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24.6 kDa.

What is the source or expression system of ADIPONECTIN Protein?
HEK293.

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

What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.

What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.

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.

Description:

Resistin Mutant Human Recombinant

Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

Product # :

CYT-585

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

9.9 kDa protein containing 93 amino acid residues, produced in E.coli. Mutant-Resistin has had a Cysteine residue mutated to prevent dimerization and possibly acts as an antagonist.

Source

Escherichia Coli.

Formulation

Recombinant Human Resistin was lyophilized from a concentrated (1mg/ml) solution containing 0.1% TFA.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrophobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.
Synonyms
Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add 0.2 ml of deionized water and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP.

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:

IFN-Alpha 2a Human Recombinant

Leukocyte IFN, B cell IFN, Type I IFN, IFNA2, IFN-a 2a, Interferon-alpha-2a.

Product # :

CYT-204

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IFN Alpha Human 2a Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19241 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine.The Interferon-alpha-2a gene was obtained from human leukocytes.The IFNA2A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized without additives.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.

More Info

Introduction
IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNA2, IFN-a 2a, Interferon-alpha-2a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFNA-2A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2a 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 Interferon-alpha-2a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE.
N-terminal methionine has been completely removed enzymatically.
Background
What is the molecular weight/Mw of IFN A 2A HUMAN Protein?
IFN A 2A HUMAN Protein has a total Mw of 19.2kDa.

What is the source or expression system of IFN A 2A HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN A 2A HUMAN Protein?
IFN A 2A HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN A 2A HUMAN Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.

What is the amino acid sequence of IFN A 2A HUMAN Protein?
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE.
N-terminal methionine has been completely removed enzymatically.

What applications can IFN A 2A HUMAN Protein be used in?
IFN A 2A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN A 2A HUMAN Protein?
The endotoxin level is minimal, IFN A 2A HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.924 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 IFN-a 2a 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:

Interferon-alpha 2c Human Recombinant

Interferon alpha-2, IFN-alpha-2, Interferon alpha-A, LeIF A, IFNA2, IFNA2A, IFNA2B, IFNA2C.

Product # :

CYT-1117

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interferon-alpha 2c Recombinant Human produced in yeast is a single, glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 19.3kDa. The IFNA2C is purified by proprietary chromatographic techniques.

Source

Saccharomyces cerevisiae.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4 and 0.02 % Tween-20.

Purity

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

Biological Activity

The activity is determined by the cytopathic effect inhibition assay.

More Info

Introduction
IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
Interferon alpha-2, IFN-alpha-2, Interferon alpha-A, LeIF A, IFNA2, IFNA2A, IFNA2B, IFNA2C.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFNA2C although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interferon-alpha 2c 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 Interferon-alpha 2c in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRRDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.
Background
What is the molecular weight/Mw of IFNA2C HUMAN Protein?
IFNA2C HUMAN Protein has a total Mw of 19.3kDa.

What is the source or expression system of IFNA2C HUMAN Protein?
Saccharomyces cerevisiae.

What is the Purity of IFNA2C HUMAN Protein?
IFNA2C HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNA2C HUMAN Protein?
The activity is determined by the cytopathic effect inhibition assay.

What is the amino acid sequence of IFNA2C HUMAN Protein?
CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRRDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.

What applications can IFNA2C HUMAN Protein be used in?
IFNA2C HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNA2C HUMAN Protein?
The endotoxin level is minimal, IFNA2C HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Interleukin-24 Human Recombinant

C49A, FISP, MDA7, ST16, IL-24, IL10B, Mob-5, MDA-7, Suppression of tumorigenicity 16 protein, Melanoma differentiation-associated gene 7 protein.

Product # :

CYT-515

Price :

Quantity :

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Shipped at Room temp

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Description

Interleukin 24 human recombinant produced in yeast is a single, glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18 kDa. As a result of glycosylation, the protein migrates at 19.5 kDa on SDS-PAGE.

Source

Sacharomyces cerevisiae.

Formulation

Lyophilized from a 0.2µm filtered solution in PBS with BSA as a carrier.

Purity

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

Biological Activity

Measured by its ability to bind to the cell receptor of Capan-1 cells line resulted in Stat-3 activation. The ED₅₀ for this effect is typically 1.0 ng/ml, corresponding to a Specific Activity of 1x10⁶ units/mg.

More Info

Introduction
IL24 is a member of the IL10 family of cytokines. It was identified as a gene induced during terminal differentiation in melanoma cells. IL-10B encoded can induce apoptosis selectively in various cancer cells. Overexpression IL-24 leads to elevated expression of several GADD family genes, which correlates with the induction of apoptosis. The phosphorylation of mitogen-activated protein kinase 14 (MAPK7/P38), and heat shock 27kDa protein 1 (HSPB2/HSP27) are found to be induced by this gene in melanoma cells, but not in normal immortal melanocytes. Alternatively spliced transcript variants encoding distinct isoforms have been reported. The glycosylation is essential for activity of IL-24. Functionally, IL-24 has diverse activities. At low concentrations, it induces type I proinflammatory cytokines such as IFN-g, IL-1b, IL-12 and TNF-a. At high concentration, it is a strong inducer of apoptosis in tumor cells, but not normal cells. mda-7/IL-24 is being hailed as a ‘magic bullet’ for cancer gene therapy.
Synonyms
C49A, FISP, MDA7, ST16, IL-24, IL10B, Mob-5, MDA-7, Suppression of tumorigenicity 16 protein, Melanoma differentiation-associated gene 7 protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MDA7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MDA-7 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-24 in sterile 18MΩ-cm H2O 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.

Description:

Interleukin-1 receptor-like 1 Human Recombinant

Interleukin-1 receptor-like 1, Protein ST2, IL1RL1, DER4, ST2, T1, ST2L, ST2V, FIT-1, MGC32623.

Product # :

CYT-671

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL1RL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 310 amino acids fragment (19-328) corresponding to the soluble IL1RL1 coding sequence, having a molecular weight of 39.5kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL1RL1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL1RL1 protein solution is supplied in 25mM Sodium Acetate pH 4.8 and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.
A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.
Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells.
Synonyms
Interleukin-1 receptor-like 1, Protein ST2, IL1RL1, DER4, ST2, T1, ST2L, ST2V, FIT-1, MGC32623.
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 IL1RL1 HUMAN Protein?
IL1RL1 HUMAN Protein has a total Mw of 39.5kDa.

What is the source or expression system of IL1RL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL1RL1 HUMAN Protein?
IL1RL1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1RL1 HUMAN Protein?
The biological functionality of IL1RL1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL1RL1 HUMAN Protein?
IL1RL1 HUMAN Protein is composed from 310 amino acids.

What applications can IL1RL1 HUMAN Protein be used in?
IL1RL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1RL1 HUMAN Protein?
The endotoxin level is minimal, IL1RL1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1RL1 HUMAN 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 IL1RL1 HUMAN ?
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 Human Recombinant, Sf9

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

Product # :

CYT-1092

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL22 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (34-179 a.a.) fused to a 6 aa His Tag at C-terminus containing a total of 155 amino acids and having a molecular mass of 17.8kDa. IL22 is purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL22 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by its ability to induce IL-10 secretion using COLO 205 human colorectal adenocarcinoma cell is ≤ 1.2 ng/ml.

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 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
ADPAPISSHC RLDKSNFQQP YITNRTFMLA KEASLADNNT DVRLIGEKLF HGVSMSERCY LMKQVLNFTL EEVLFPQSDR FQPYMQEVVP FLARLSNRLS TCHIEGDDLH IQRNVQKLKD TVKKLGESGE IKAIGELDLL FMSLRNACIH HHHHH.

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-21 Human Recombinant

Za11, IL-21.

Product # :

CYT-408

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IL21 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a total molecular mass of 15.4kDa. The IL-21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from PBS, pH 7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to proliferate activated B cells.

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Introduction
IL-21 is produced by CD4+ T cells in response to antigenic stimulation. Its action enhances antigen-specific responses of immune cells. The biological effects of IL-21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation (in conjuction) with IL-4 of IgG production, and induction of apoptotic effects in naive B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the gamma chain (°C) found in other cytokine receptors including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.
Synonyms
Za11, IL-21.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-21 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL21 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 -21 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQDRHMIRMR QLIDIVDQLK NYVNDLVPEF LPAPEDVETN CEWSAFSCFQ KAQLKSANTG NNERIINVSI KKLKRKPPST NAGRRQKHRL TCPSCDSYEK KPPKEFLERF KSLLQKMIHQ HLSSRTHGSE DS.

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 Human Recombinant, Yeast

Interleukin-2, T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.

Product # :

CYT-797

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-2 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 134 amino acids and having a molecular mass of 14 kDa. The IL-2 is purified by proprietary chromatographic techniques.

Source

Pichia pastoris.

Formulation

The protein was lyophilized from a 0.2µm filtered solution in 20mM sodium phosphate buffer pH 7.0 in absence of any carrier protein.

Purity

Greater than 98% as determined by SDS-PAGE.

Biological Activity

The biological activity is determined by the dose dependent proliferation of mouse CTLL–2 cells. Optimal concentration for individual application should be determined by a dose response assay. ED50 range = 0.08–0.5ng/ml

More Info

Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
Synonyms
Interleukin-2, T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Interleukin-2 should be stored at 4C between 2-7 days and for future use below -18C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
A P T S S S T K K T Q L Q L E H L L L D L Q M I L N G I N N Y K N P K L T R M L T F K F Y M P K K A T E L K H L Q C L E E E L K P L E E V L N L A Q S K N F H L R P R D L I S N I N V I V L E L K G S E T T F M C E Y A D E T A T I V E F L N R W I T F C Q S I I S T L T.
Background
What is the molecular weight/Mw of IL 2 HUMAN, YEAST Protein?
IL 2 HUMAN, YEAST Protein has a total Mw of 14kDa.

What is the source or expression system of IL 2 HUMAN, YEAST Protein?
Pichia pastoris.

What is the Purity of IL 2 HUMAN, YEAST Protein?
IL 2 HUMAN, YEAST Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 HUMAN, YEAST Protein?
The biological activity is determined by the dose dependent proliferation of mouse CTLL–2 cells. Optimal concentration for individual application should be determined by a dose response assay. ED50 range = 0.08–0.5ng/ml

What is the amino acid sequence of IL 2 HUMAN, YEAST Protein?
A P T S S S T K K T Q L Q L E H L L L D L Q M I L N G I N N Y K N P K L T R M L T F K F Y M P K K A T E L K H L Q C L E E E L K P L E E V L N L A Q S K N F H L R P R D L I S N I N V I V L E L K G S E T T F M C E Y A D E T A T I V E F L N R W I T F C Q S I I S T L T.

What applications can IL 2 HUMAN, YEAST Protein be used in?
IL 2 HUMAN, YEAST Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 2 HUMAN, YEAST Protein?
The endotoxin level is minimal, IL 2 HUMAN, YEAST Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 2 HUMAN, YEAST 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 2 HUMAN, YEAST?
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:

IFN-Alpha 2b Human Recombinant

IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

Product # :

CYT-205

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

IFN-a 2b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids and having a molecular mass of 19400 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine. The IFN-alpha 2b gene was obtained from human leukocytes. The IFN-a 2b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a (1 mg/ml) solution in containing 2.3 mg Sodium phosphate dibasic and 0.55 mg sodium phosphate monobasic buffer.

Purity

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

Biological Activity

The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

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Introduction
IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN alpha 2b 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 IFN-alpha 2b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
Background
IFN-alpha forms are produced by monocytes/macrophages, lymphoblastoid cells, fibroblasts, and a number of different cell types following induction by viruses, nucleic acids, glucocorticoid hormones, and low-molecular weight substances (n-butyrate, 5-bromodeoxy uridine). At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end. Disulfide bonds are formed between cysteines at positions 1/98 and 29/138. The disulfide bond 29/138 is essential for biological activity while the 1/98 bond can be reduces without affecting biological activity. All IFN-alpha forms contain a potential glycosylation site but most subtypes are not glycosylated. In contrast to IFN-gamma IFN-alpha proteins are stable at pH2.
There are at least 23 different IFN-alpha genes. They have a length of 1-2 kb and are clustered on human chromosome 9p22. It is not known whether all these genes are expressed following stimulation of the cells. In some cell systems expression of some subtypes (IFN-alpha-1, IFN-alpha-2, IFN-alpha-4) is stronger than those of others. IFN-alpha genes do not contain intron sequences found in many other eukaryotic genes (see also: gene expression). Based upon the structures two types of IFN-alpha genes, designated class 1 and II, are distinguished. They encode proteins of 156-166 and172 amino acids, respectively. Deletions covering 9p22 are observed frequently in cells of lymphoblastoid leukemias. It is not known to date whether this is of significance with respect to IFN expression.
The gene encoding the IFN-alpha receptor maps to human chromosome 21q22.1. IFN-alpha and IFN-beta are thought to bind to the same IFN binding subunit which is expressed in 100-5000 copies in IFN-alpha sensitive and -resistant cells and is associated with other as yet unidentified proteins. The IFN-omega (Omega IFN) also binds to the IFN-alpha/IFN-beta receptor. Another receptor expressed on B-lymphocytes is identical with CD21. This receptor also binds Epstein-Barr virus through its gp350/220 coat protein.Signal transduction mechanisms elicited after binding of IFN-alpha to its receptors involves tyrosine phosphorylation (see also: PTK; protein tyrosine kinase) of various non-receptor tyrosine kinases belonging to the Janus kinases. Soluble forms of the IFN-alpha receptor, corresponding to truncated forms of the extracellular domain of the cell surface IFN-alpha receptor, have been found in human serum and in normal human urine.
All known subtypes of IFN-alpha show the same antiviral antiparasitic, antiproliferative activities in suitable bioassays although they may differ in relative activities. Human IFN-alpha is also a potent antiviral substance in murine, porcine, and bovine cell systems. Human IFN-alpha is less active in rodent cells. Site-directed mutagenesis techniques have been used to create some variants of certain subtypes (IFN-alpha-2) that display approximately 100-fold enhanced antiviral activities in mouse cells.
What is the molecular weight/Mw of IFN A 2B HUMAN Protein?
IFN A 2B HUMAN Protein has a total Mw of 19.4kDa.

What is the source or expression system of IFN A 2B HUMAN Protein?
Escherichia Coli.

What is the Purity of IFN A 2B HUMAN Protein?
IFN A 2B HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN A 2B HUMAN Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

What is the amino acid sequence of IFN A 2B HUMAN Protein?
MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
What applications can IFN A 2B HUMAN Protein be used in?
IFN A 2B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN A 2B HUMAN Protein?
The endotoxin level is minimal, IFN A 2B HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.924 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 IFN alpha 2b 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-2 Human Recombinant

T-cell growth factor (TCGF), Lymphokine, IL-2.

Product # :

CYT-209

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15.4kDa. The IL-2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a 0.2μm filtered concentrated solution (1.0mg/ml) in PBS, pH 5.0.

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 murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x10⁷IU/mg.

More Info

Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
Synonyms
T-cell growth factor (TCGF), Lymphokine, IL-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 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-2 in sterile distilled water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.
Background
IL 2 HUMAN: A Vital Tool for Advancing Immunotherapy Research
IL 2 HUMAN refers to the human form of Interleukin-2, a critical cytokine in the immune system. This protein is crucial for the growth and activity of T and B lymphocytes, the cells responsible for the body's immune defense against infections.
By promoting the growth of these cells, IL 2 plays a vital role in maintaining and activating the immune response.
Production and Characteristics
Typically, IL 2 is produced through recombinant DNA technology using E. coli bacteria. This method allows for creating large quantities of pure and functional IL 2 protein.
The product appears as a sterile, white lyophilized powder that is non-glycosylated and consists of 133 amino acids with a molecular mass of approximately 15.4 kDa.
Reconstituting IL-2 Human for Laboratory Use
To dissolve the lyophilized IL-2 effectively, it should be reconstituted with sterile distilled water to achieve a minimum 100µg/ml concentration. This makes the protein readily usable for further experimental procedures.
Moreover, the concentration allows for easy adjustment in solubility and ensures optimal conditions for the protein's activity in various research setups. Proper dissolution and storage are crucial to maintain the protein's functionality and stability.
Storage and Stability
The stability of IL 2 is dependent on its storage conditions. When lyophilized, it can remain stable at room temperature for up to three weeks, but for long-term storage, it should be kept desiccated below -18°C.
Once reconstituted, IL 2 should be used within a week if kept at 4°C, or it can be stored at below -18°C for future use. It's important to avoid freeze-thaw cycles, which can degrade the protein.
Purity and Biological Activity
IL 2 HUMAN's purity is generally greater than 97%, confirmed by reverse-phase high-performance liquid chromatography (RP-HPLC) and SDS-PAGE analyses.
Its biological activity is evaluated by its ability to stimulate the proliferation of murine CTLL-2 cells, with an effective dose (ED50) typically less than 0.1 ng/ml. This indicates a very high specific activity, making it highly potent and effective in research settings.
Applications in Research
IL 2 is used extensively in research, particularly in studies focusing on the immune system, autoimmune diseases, and cancer. Furthermore, its role in T-cell growth and function makes it invaluable for developing new therapeutic strategies and understanding immune response mechanisms.
Important Considerations
It is important to remember that IL 2, like all cytokines used in research, is intended for laboratory use only. This protein is not suitable for drug, food, or cosmetic applications. Proper handling and usage instructions must be followed to ensure safety and efficacy in research environments.
Essentially, IL 2 HUMAN is a vital tool in immunological research, offering insights into the complex workings of the immune system and providing avenues for potential therapeutic developments. The careful production, handling, and storage of IL 2 are crucial for its effective use in laboratory settings.
What is the molecular weight/Mw of IL 2 HUMAN Protein?
IL 2 HUMAN Protein has a total Mw of 15.4kDa.

What is the source or expression system of IL 2 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL 2 HUMAN Protein?
IL 2 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 HUMAN Protein?
The ED50 as determined by the dose-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x107IU/mg.

What is the amino acid sequence of IL 2 HUMAN Protein?
APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.

What applications can IL 2 HUMAN Protein be used in?
IL 2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 2 HUMAN Protein?
The endotoxin level is minimal, IL 2 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 2 HUMAN 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 2 HUMAN?
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 34 Human Recombinant, His Tag

Interleukin 34, C16orf77, MGC34647, IL34.

Product # :

CYT-042

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL34 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (21-242 a.a) and having a molecular mass of 29.6kDa. IL34 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The IL34 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
Interleukin 34 (IL34) is a cytokine that promotes the differentiation and viability of monocytes and macrophages through the colony-stimulating factor-1 receptor and is a part of a group of cytokines called interleukins. IL34 increases growth or survival of immune cells known as monocytes. IL34 protein obtains its activity by binding the Colony stimulating factor 1 receptor. Interleukin 34 has also a potential part in viral infection, the adaptive immune response and bone marrow cell proliferation. Furthermore, IL34 plays an important role in innate immunity and in inflammatory processes.
Synonyms
Interleukin 34, C16orf77, MGC34647, IL34.
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 KDRWGSHMNE PLEMWPLTQN EECTVTGFLR DKLQYRSRLQ YMKHYFPINY KISVPYEGVF RIANVTRLQR AQVSERELRY LWVLVSLSAT ESVQDVLLEG HPSWKYLQEV QTLLLNVQQG LTDVEVSPKV ESVLSLLNAP GPNLKLVRPK ALLDNCFRVM ELLYCSCCKQ SSVLNWQDCE VPSPQSCSPE PSLQYAATQL YPPPPWSPSS PPHSTGSVRP VRAQGEGLLP.

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-17 Human Recombinant

CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.

Product # :

CYT-250

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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sds-page
Citations

Description

Interleukin-17A Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 264 amino acids (2 chains of 132 aa) and having a molecular mass of 31kDa. The IL-17 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Sterile filtered lyophilized (freeze-dried) powder, with 20mM Citrate, 0.1M NaCl, pH4.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependent induction of IL-6 in Hs68 cell line was found to be approximately 2ng/ml corresponding to a Specific Activity of 500,000IU/mg.

sds-page

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Introduction
IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.
Synonyms
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin 17A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.13 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-17 as a Reference Standard.

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

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.

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
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-1 Receptor Like-1 Human Recombinant, Sf9 Active

Interleukin 1 Receptor Like 1, Homolog Of Mouse Growth Stimulation-Expressed, DER4, ST2, T1, Interleukin 1 Receptor-Related Protein, Interleukin-1 Receptor-Like 1, Growth Stimulation-Expressed, Protein ST2, FIT-1, IL33R, ST2L, ST2V, Interleukin-1 receptor-like 1.

Product # :

CYT-1052

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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formulation
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SDS-PAGE
Citations

Description

IL1RL1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 318 amino acids (19-328a.a.) and having a molecular mass of 36.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL1RL1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL1RL1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is less or equal to 10ng/ml with IL-33.

SDS-PAGE

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Introduction
The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells.
Synonyms
Interleukin 1 Receptor Like 1, Homolog Of Mouse Growth Stimulation-Expressed, DER4, ST2, T1, Interleukin 1 Receptor-Related Protein, Interleukin-1 Receptor-Like 1, Growth Stimulation-Expressed, Protein ST2, FIT-1, IL33R, ST2L, ST2V, Interleukin-1 receptor-like 1.
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
KFSKQSWGLE NEALIVRCPR QGKPSYTVDW YYSQTNKSIP TQERNRVFAS GQLLKFLPAA VADSGIYTCI VRSPTFNRTG YANVTIYKKQ SDCNVPDYLM YSTVSGSEKN SKIYCPTIDL YNWTAPLEWF KNCQALQGSR YRAHKSFLVI DNVMTEDAGD YTCKFIHNEN GANYSVTATR SFTVKDEQGF SLFPVIGAPA QNEIKEVEIG KNANLTCSAC FGKGTQFLAA VLWQLNGTKI TDFGEPRIQQ EEGQNQSFSN GLACLDMVLR IADVKEEDLL LQYDCLALNL HGLRRHTVRL SRKNPIDHHS LEHHHHHH.
Background
What is the molecular weight/Mw of IL1RL1 HUMAN, SF9 ACTIVE Protein?
IL1RL1 HUMAN, SF9 ACTIVE Protein has a total Mw of 36kDa.

What is the source or expression system of IL1RL1 HUMAN, SF9 ACTIVE Protein?
Sf9, Baculovirus cells.

What is the Purity of IL1RL1 HUMAN, SF9 ACTIVE Protein?
IL1RL1 HUMAN, SF9 ACTIVE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1RL1 HUMAN, SF9 ACTIVE Protein?
Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is less or equal to 10ng/ml with IL-33.

What is the amino acid sequence of IL1RL1 HUMAN, SF9 ACTIVE Protein?
KFSKQSWGLE NEALIVRCPR QGKPSYTVDW YYSQTNKSIP TQERNRVFAS GQLLKFLPAA VADSGIYTCI VRSPTFNRTG YANVTIYKKQ SDCNVPDYLM YSTVSGSEKN SKIYCPTIDL YNWTAPLEWF KNCQALQGSR YRAHKSFLVI DNVMTEDAGD YTCKFIHNEN GANYSVTATR SFTVKDEQGF SLFPVIGAPA QNEIKEVEIG KNANLTCSAC FGKGTQFLAA VLWQLNGTKI TDFGEPRIQQ EEGQNQSFSN GLACLDMVLR IADVKEEDLL LQYDCLALNL HGLRRHTVRL SRKNPIDHHS LEHHHHHH.

What applications can IL1RL1 HUMAN, SF9 ACTIVE Protein be used in?
IL1RL1 HUMAN, SF9 ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1RL1 HUMAN, SF9 ACTIVE Protein?
The endotoxin level is minimal, IL1RL1 HUMAN, SF9 ACTIVE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1RL1 HUMAN, SF9 ACTIVE 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 IL1RL1 HUMAN, SF9 ACTIVE?
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:

Tumor Necrosis Factor Receptor 13B Human Recombinant

CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

Product # :

CYT-819

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
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biological activity
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Description

TACI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 18.0kDa.

Source

Escherichia Coli.

Formulation

TACI protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

Fully biologically active when compared to standard. The biological activity is determined by its ability to block human BAFF induced T2B cell survival using a concentration range of 1.0-3.0 µg/ml corresponding to a specific activity of 334-1000 IU/mg.

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Introduction
TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
Synonyms
CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TACI although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TACI 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 TACI in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC KTICNHQSQR TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC AYFCENKLRS PVNLPPELRR QRSGEVENNS DNSGRYQGLE HRGSEASPAL PGLKLSADQV

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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