Search: 1000 results found for "Interleukin"

Description:

Interleukin-4 Induced-1 Human Recombinant

IL-4I1, IL4I1, IL4-I1, IL4I-1

Product # :

CYT-1209

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Description

IL4R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (26-232 a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 215 amino acids and having a molecular mass of 24.7kDa.IL4R shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL4I1 protein solution (0.25mg/ml) contains 25mM MES pH-5.5, 40% glycerol and 100mM NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

> 300 pmol/min/ug, defined as the amount of enzyme that oxidize 3-phenylpyruvate pH-7 at 25C.

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Introduction
IL4I1 is a secreted L-amino acid oxidase protein that mainly catabolizes L-phenylalanine. IL4I1 eexpression is induced by the IL4 in B cells.IL4I1 is expressed in dendritic cells & macrophagesIL4I1 takes part in the immune system since it is expressed in tumor-associated macrophages and suppresses T-cell responses. IL4I1 plays a role in the binding of flavin adenine dinucleotide cofactor.
Synonyms
IL-4I1, IL4I1, IL4-I1, IL4I-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
ADL QDWKAER SQDPFEKCMQ DPDYEQLLKV VTWGLNRTLK PQRVIVVGAG VAGLVAAKVL SDAGHKVTIL EADNRIGGRI FTYRDQNTGW IGELGAMRMP SSHRILHKLC QGLGLNLTKF TQYDKNTWTE VHEVKLRNYV VEKVPEKLGY ALRPQEKGHS PEDIYQMALN QALKDLKALG CRKAMKKFER HTLLEYLLGE GNLSRPAVQL LGDVMSEDGF FYLSFAEALR AHSCLSDRLQ YSRIVGGWDL LPRALLSSLS GLVLLNAPVV AMTQGPHDVH VQIETSPPAR NLKVLKADVV LLTASGPAVK RITFSPPLPR HMQEALRRLH YVPATKVFLS FRRPFWREEH IEGGHSNTDR PSRMIFYPPP REGALLLASY TWSDAAAAFA GLSREEALRL ALDDVAALHG PVVRQLWDGT GVVKRWAEDQ HSQGGFVVQP PALWQTEKDD WTVPYGRIYF AGEHTAYPHG WVETAVKSAL RAAIKINSRK GPASDTASPE GHASDMEGQG HVHGVASSPS HDLAKEEGSH PPVQGQLSLQNTTHTRTSH H HHHHHH
Background
What is the molecular weight/Mw of IL 4 I1 HUMAN Protein?
IL 4 I1 HUMAN Protein has a total Mw of 24.7kDa.

What is the source or expression system of IL 4 I1 HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 4 I1 HUMAN Protein?
IL 4 I1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 I1 HUMAN Protein?
> 300 pmol/min/ug, defined as the amount of enzyme that oxidize 3-phenylpyruvate pH-7 at 25C.

What is the amino acid sequence of IL 4 I1 HUMAN Protein?
ADL QDWKAER SQDPFEKCMQ DPDYEQLLKV VTWGLNRTLK PQRVIVVGAG VAGLVAAKVL SDAGHKVTIL EADNRIGGRI FTYRDQNTGW IGELGAMRMP SSHRILHKLC QGLGLNLTKF TQYDKNTWTE VHEVKLRNYV VEKVPEKLGY ALRPQEKGHS PEDIYQMALN QALKDLKALG CRKAMKKFER HTLLEYLLGE GNLSRPAVQL LGDVMSEDGF FYLSFAEALR AHSCLSDRLQ YSRIVGGWDL LPRALLSSLS GLVLLNAPVV AMTQGPHDVH VQIETSPPAR NLKVLKADVV LLTASGPAVK RITFSPPLPR HMQEALRRLH YVPATKVFLS FRRPFWREEH IEGGHSNTDR PSRMIFYPPP REGALLLASY TWSDAAAAFA GLSREEALRL ALDDVAALHG PVVRQLWDGT GVVKRWAEDQ HSQGGFVVQP PALWQTEKDD WTVPYGRIYF AGEHTAYPHG WVETAVKSAL RAAIKINSRK GPASDTASPE GHASDMEGQG HVHGVASSPS HDLAKEEGSH PPVQGQLSLQNTTHTRTSH H HHHHHH.

What applications can IL 4 I1 HUMAN Protein be used in?
IL 4 I1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 4 I1 HUMAN Protein?
The endotoxin level is minimal, IL 4 I1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 4 I1 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 I1 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-1 Receptor Antagonist Human Recombinant, His Tag

IRAP, IL1F3, IL1RA; IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

Product # :

CYT-481

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Shipped with Ice Packs

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Description

IL1Ra Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 152 amino acids fragment (26-177) and having a total molecular mass of 21.63kDa with an amino-terminal hexahistidine tag. The IL-1Ra His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-1Ra His-tag protein is supplied in 20mM Tris HCl (pH 8) and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
IL-1Ra is the natural antagonist of the pro-inflammatory cytokines Interleukin-1? and Interleukin-1?. IL-1Ra is produced by a variety of cells including monocytes, macrophages, neutrophils and fibroblasts in response to the binding of various pro-inflammatory cytokines.
Synonyms
IRAP, IL1F3, IL1RA; IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
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 IL 1RA HUMAN, HIS Protein?
IL 1RA HUMAN, HIS Protein has a total Mw of 21.63kDa.

What is the source or expression system of IL 1RA HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL 1RA HUMAN, HIS Protein?
IL 1RA HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 1RA HUMAN, HIS Protein?
The biological functionality of IL 1RA HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL 1RA HUMAN, HIS Protein?
IL 1RA HUMAN, HIS Protein is composed from 152 amino acids.

What applications can IL 1RA HUMAN, HIS Protein be used in?
IL 1RA HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 1RA HUMAN, HIS Protein?
The endotoxin level is minimal, IL 1RA HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 1RA 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 IL 1RA 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-21 Receptor Human Recombinant

Interleukin 21 Receptor, Novel Interleukin Receptor, IL-21 Receptor, NILR, Interleukin-21 Receptor, CD360 Antigen, IL-21R, CD360.

Product # :

CYT-911

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Description

IL21R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (20-232 a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 221 amino acids and having a molecular mass of 25.6kDa.IL21R shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL21R protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Interleukin-21 receptor, also known as IL21R is a member of the type I cytokine receptors family. IL21R forms a heterodimeric receptor complex with the common gamma-chain, a receptor subunit which is also shared by the receptors for interleukin 2, 4, 7, 9, and 15. Furthermore, IL21 receptor transduces the growth promoting signal of IL21, and is significant for the proliferation as well as differentiation of T cells, B cells, and natural killer (NK) cells. The ligand binding of IL21 receptor leads to the activation of numerous downstream signaling molecules, including JAK1, JAK3, STAT1, as well as STAT3.
Synonyms
Interleukin 21 Receptor, Novel Interleukin Receptor, IL-21 Receptor, NILR, Interleukin-21 Receptor, CD360 Antigen, IL-21R, CD360.
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
CPDLVCYTDY LQTVICILEM WNLHPSTLTL TWQDQYEELK DEATSCSLHR SAHNATHATY TCHMDVFHFM ADDIFSVNIT DQSGNYSQEC GSFLLAESIK PAPPFNVTVT FSGQYNISWR SDYEDPAFYM LKGKLQYELQ YRNRGDPWAV SPRRKLISVD SRSVSLLPLE FRKDSSYELQ VRAGPMPGSS YQGTWSEWSD PVIFQTQSEE LKEVEHHHHH H

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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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.

More Info

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.

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 Receptor Subunit Alpha Human Recombinant

Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.

Product # :

CYT-1049

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Shipped with Ice Packs

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sds-page
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Description

IL3RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (20-305 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 295 amino acids and having a molecular mass of 34.1kDa.IL3RA is purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL3RA protein solution (0.25mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

More Info

Introduction
IL3RA, also known as Interleukin 3 Receptor Subunit Alpha, is a single-pass type 1 membrane protein which is a member of the type 1 cytokine receptor family as well as type 5 subfamily. IL3RA is a pleiotropic cytokine which is produced mainly by activated T cells or mast cells. Moreover, the specific alpha subunit of the interleukin 3 receptor is strongly expressed in a variety of leukemic blasts as well as leukemic stem cells and appears to be a great target for the therapy of leukemias.
Synonyms
Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.
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
ADLKEDPNPP ITNLRMKAKA QQLTWDLNRN VTDIECVKDA DYSMPAVNNS YCQFGAISLC EVTNYTVRVA NPPFSTWILF PENSGKPWAG AENLTCWIHD VDFLSCSWAV GPGAPADVQY DLYLNVANRR QQYECLHYKT DAQGTRIGCR FDDISRLSSG SQSSHILVRG RSAAFGIPCT
DKFVVFSQIE ILTPPNMTAK CNKTHSFMHW KMRSHFNRKF RYELQIQKRM QPVITEQVRD RTSFQLLNPG TYTVQIRARE RVYEFLSAWS TPQRFECDQE EGANTRAWRH HHHHH.
Background
What is the molecular weight/Mw of IL 3 RA HUMAN Protein?
IL 3 RA HUMAN Protein has a total Mw of 34.1kDa.

What is the source or expression system of IL 3 RA HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 3 RA HUMAN Protein?
IL 3 RA HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 RA HUMAN Protein?
The biological functionality of IL 3 RA HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL 3 RA HUMAN Protein?
ADLKEDPNPP ITNLRMKAKA QQLTWDLNRN VTDIECVKDA DYSMPAVNNS YCQFGAISLC EVTNYTVRVA NPPFSTWILF PENSGKPWAG AENLTCWIHD VDFLSCSWAV GPGAPADVQY DLYLNVANRR QQYECLHYKT DAQGTRIGCR FDDISRLSSG SQSSHILVRG RSAAFGIPCT
DKFVVFSQIE ILTPPNMTAK CNKTHSFMHW KMRSHFNRKF RYELQIQKRM QPVITEQVRD RTSFQLLNPG TYTVQIRARE RVYEFLSAWS TPQRFECDQE EGANTRAWRH HHHHH.

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

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

Who supplies recombinant IL 3 RA 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 3 RA 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-28A Human Recombinant, His Tag

Interleukin-28A, IL-28A, IFN-Lambda 2, Interferon-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.

Product # :

CYT-813

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Description

IL 28A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (26-200 a.a.) and having a molecular mass of 22.1kDa. IL 28A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 28A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
IL-28A is distantly related to type I interferons and 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
Interleukin-28A, IL-28A, IFN-Lambda 2, Interferon-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
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 MGSVPVARLH GALPDARGCH IAQFKSLSPQ ELQAFKRAKD ALEESLLLKD CRCHSRLFPR TWDLRQLQVR ERPMALEAEL ALTLKVLEAT ADTDPALVDV LDQPLHTLHH ILSQFRACIQ PQPTAGPRTR GRLHHWLYRL QEAPKKESPG CLEASVTFNL FRLLTRDLNC VASGDLCV .

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 p35 Human Recombinant

NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.

Product # :

CYT-487

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Interleukin-12 p35 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 197 amino acids fragment (57-253) with an amino-terminal hexahistidine tag. The IL-12 p35 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-12 p35 His-Tag is supplied in 1xPBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
Synonyms
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
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 source or expression system of IL12P35 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL12P35 HUMAN Protein?
IL12P35 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12P35 HUMAN Protein?
The biological functionality of IL12P35 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL12P35 HUMAN Protein?
IL12P35 HUMAN Protein is composed from 197 amino acids.

What applications can IL12P35 HUMAN Protein be used in?
IL12P35 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12P35 HUMAN Protein?
The endotoxin level is minimal, IL12P35 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12P35 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 IL12P35 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-19 Human Recombinant

Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19.

Product # :

CYT-363

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-19 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids and having a molecular mass of 17913 Dalton. The IL-19 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 10mM sodium citrate pH-5.

Purity

Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity is determined by it's ability to activate STAT following receptor-ligand interaction.

More Info

Introduction
IL19 is a cytokine that belongs to the IL10 cytokine subfamily. IL-19 is found to be preferentially expressed in monocytes. It can bind the IL20 receptor complex and lead to the activation of the signal transducer and activator of transcription 3 (STAT3). A similar cytokine in mouse is reported to up-regulate the expression of IL6 and TNF-alpha and induce apoptosis, which suggests a role of this cytokine in inflammatory responses. Alternatively spliced transcript variants encoding the distinct isoforms have been described.
Synonyms
Melanoma differentiation association like protein, MDA1, NG.1, ZMDA1, IL-10C, IL-19.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-19 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL19 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 -19 in sterile 18MΩ-cm H2O at a concentration of 0.5mg/ml or less.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Leu-Arg-Arg-Cys.

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-36 Alpha 158 a.a. Human Recombinant

Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.

Product # :

CYT-179

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Description

IL36A 158 a.a. Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 17.7kDa.The IL36A 158 a.a. Human is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2?m filtered concentrated solution in 2xPBS, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

Biological Activity

Fully biologically active when compared to standard. The specific activity determined by its ability in a functional ELISA. Immobilized rHuIL-36? at 1 ?g/mL can bind recombinant human IL-1 Rrp2 Fc Chimera with a range of 0.15-5?g/ml corresponding to a specific activity of 200,000-6,666,667IU/mg.

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Introduction
Human IL-36a belongs to the IL-1 family which 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-36a is an 18-22kDa, 158aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential from N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
Human IL-36a (aa 6-158) shares 57-68% aa sequence homology with mouse, rabbit, equine and bovine IL-36a and 27-57% aa sequence homology with other new IL-1 family members. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine.
Synonyms
Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL36A 158 a.a. Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36A 158 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 IL36A 158 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
MEKALKIDTP QQGSIQDINH RVWVLQDQTL IAVPRKDRMS PVTIALISCR HVETLEKDRG NPIYLGLNGL NLCLMCAKVG DQPTLQLKEK DIMDLYNQPE PVKSFLFYHS QSGRNSTFES VAFPGWFIAV SSEGGCPLIL TQELGKANTT DFGLTMLF

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 , His Tag

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-648

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Description

Interleukin-32 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-131 a.a.) and having a molecular mass of 19.1 kDa. The IL-32 is fused to a 37 amino acid His Tag at N-terminus and purified by conventional chromatography.

Source

Escherichia Coli.

Formulation

The IL-32 His Tag protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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 interferon gamma.
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 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 KDRWGSHMCF PKVLSDDMKK LKARMHQAIE RFYDKMQNAE SGRGQVMSSL AELEDDFKEGYLETVAAYYE EQHPELTPLL EKERDGLRCR GNRSPVPDVE DPATEEPGES FCDKSYGAPR GDKEELTPQK CSEPQSSK.

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 Alpha Mouse Recombinant

Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.

Product # :

CYT-162

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Description

IL36A Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 21.0kDa.The IL36A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA to bind recombinant mouse IL-1 Rrp2.

More Info

Introduction
Murine IL-36a 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. Murine IL-36a is a 160 amino acid intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
Mouse to human, full length IL-36a/IL-1F6 shares 54% aa sequence homology. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine.
Synonyms
Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL36A Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36A 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 IL36A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MNKEKELRAA SPSLRHVQDL SSRVWILQNN ILTAVPRKEQ TVPVTITLLP CQYLDTLETN RGDPTYMGVQ RPMSCLFCTK DGEQPVLQLG EGNIMEMYNK KEPVKASLFY HKKSGTTSTF ESAAFPGWFI AVCSKGSCPL ILTQELGEIF ITDFEMIVVH

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 A/F Heterodimer Mouse Recombinant

IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.

Product # :

CYT-640

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Description

Interleukin-17 A/F Mouse Recombinant produced in E.Coli is a heterodimeric, non-glycosylated polypeptide comprised of IL17A monomeric subunit & and IL17F monomeric subunit containing a total of 266 amino acids and having a total molecular mass of 29.8kDa. The IL-17 A/F is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing no additives.

Purity

Greater than 97.0% as determined by SDS-PAGE.

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Introduction
Human IL-17A/F is a 40kDa glycoprotein which is secreted as a disulfide-linked heterodimer. IL-17A/F consists of two proteins of the IL-17 family, IL-17A and IL17F. Proteins of the 6 homodimeric IL17 family show a cysteine knot motif that contains two disulfide-bonds. Human IL17A is produced as a 155 a.a precursor that includes a 23 amino acids signal sequence and a 132 amino acid chain that includes an N-linked glycosylation site. Human IL17F is produced as a 153 amino acid precursor with a 20 amino acid signal sequence and a 133 amino acid region. Similar to IL17A, IL17F also has an N-linked glycosylation site. Both proteins (IL17A & IL17F) share 50% amino acid sequence identity. Human IL17A & IL17F show approximately 60% homology in their amino acid sequence to mouse IL-17A and IL-17F. Interleukin-17A/F and IL17A, IL17F homodimers are manufactured by activted CD4+ T cells, called Th17. IL-23 causes Th17 lymphocytes to manufacture IL-17A/F. IL17RA and IL17RC form a heterodimer for the binding of IL17A and IL17F. IL-17A/F binds IL-17RA. Interleukin-17A/F induces chemokine production and airway neutrophilia with intermediate potency between IL17A (most potent) and IL17F (least potent).
Synonyms
IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Mouse IL17 A/F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse IL17 A/F 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 IL17 A/F 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
EPQGCSNSFRLEKMLLKVGCTCVKPIVHQAAAAIIPQSSACPNTEAKDFLQ
NVKVNLKVFNSLGAKVSSRRPSDYLNRSTSPWTLHRNEDPDRYPSVIWE
AQCRHQRCVNAEGKLDHHMNSVLIQQEILVLKREPESCPFTFRVEKMLV
GVGCTCVASIVRQAA.

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

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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.

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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-6 Human Recombinant, Sf9

BSF2, HGF, HSF, IFNB2, IL-6.

Product # :

CYT-1150

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Description

IL6 Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 189 amino acids (30-212aa) and having a molecular mass of 21.6kDa.(Migrates at 18-28kDa on SDS-PAGE under reducing conditions).IL6 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL6 protein (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50, determined by cell proliferation assay using TF-1 human erythroleukemic cell, is 0.2 - 0.8 ng/ml .

SDS-PAGE

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Introduction
Interleukin-6 or Il-6 is a cytokine with a large assortment of biological functions. IL-6 it has a crucial part in the last differentiation of b-cells into ig-secreting cells. This cytokine also induces myeloma and plasmacytoma growth. Interleukin-6 induces nerve cells differentiation, among hepatocytes it induces acute phase reactants.
Synonyms
BSF2, HGF, HSF, IFNB2, IL-6.
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
VPPGEDSKDV AAPHRQPLTS SERIDKQIRY ILDGISALRK ETCNKSNMCE SSKEALAENN
LNLPKMAEKD GCFQSGFNEE TCLVKIITGL LEFEVYLEYL QNRFESSEEQ ARAVQMSTKV
LIQFLQKKAK NLDAITTPDP TTNASLLTKL QAQNQWLQDM TTHLILRSFK EFLQSSLRAL RQMHHHHHH.
Background
Production and Applications of Human Recombinant Interleukin-6 in Sf9 Cells
Abstract:
Interleukin-6 (IL-6) holds a central role in immune regulation, inflammation, and hematopoiesis. The production of Human Recombinant IL-6 using the Sf9 insect cell system presents a versatile approach for investigating its biological functions and potential therapeutic applications. This paper outlines the methodology of producing Human Recombinant IL-6 in Sf9 cells and explores its significance in immunological research and clinical studies.
Introduction:
IL-6 is a multifunctional cytokine pivotal in various physiological processes, making it a target of intensive research. The expression of Human Recombinant IL-6 facilitates investigations into its intricate mechanisms and offers potential avenues for therapeutic development. The Sf9 cell system, harnessed from Spodoptera frugiperda, enables efficient recombinant protein expression through baculovirus vectors.
Methods:
Production of Human Recombinant IL-6 involves cloning the human IL-6 gene into a baculovirus transfer vector, which is co-transfected with linearized baculovirus DNA into Sf9 cells. The resultant recombinant baculovirus generates and secretes IL-6 into the culture medium. Purification methods, such as chromatography, ensure the protein's quality and functionality.
Applications:
Human Recombinant IL-6 from Sf9 cells has broad applications. It serves as a critical tool for investigating IL-6's roles in immune responses, inflammation, and hematopoiesis. Additionally, it plays a crucial role in the development of therapies targeting IL-6-associated disorders like autoimmune diseases, chronic inflammatory conditions, and cancer.
Sf9 Expression Advantages:
The Sf9 system offers notable advantages, including post-translational modifications and protein folding, necessary for IL-6's biological activity. Sf9 cells provide a platform for generating properly folded and functional recombinant IL-6, reflecting its native structure and function.
Challenges and Future Prospects:
While Sf9-based expression of Human Recombinant IL-6 offers significant advantages, optimization of expression conditions and scale-up strategies remain challenges. Furthermore, the therapeutic potential of Human Recombinant IL-6 requires in-depth preclinical and clinical investigations.
Conclusion:
The production of Human Recombinant IL-6 in Sf9 cells through baculovirus expression offers a powerful tool to comprehend IL-6's multifaceted roles in health and disease. This technology is poised to expand our knowledge of IL-6-related conditions and catalyze the development of precision therapeutic interventions.
What is the molecular weight/Mw of IL 6 HUMAN, SF9 Protein?
IL 6 HUMAN, SF9 Protein has a total Mw of 21.6kDa.

What is the source or expression system of IL 6 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 6 HUMAN, SF9 Protein?
IL 6 HUMAN, SF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 6 HUMAN, SF9 Protein?
The ED50, determined by cell proliferation assay using TF-1 human erythroleukemic cell, is 0.2 - 0.8 ng/ml .

What is the amino acid sequence of IL 6 HUMAN, SF9 Protein?
VPPGEDSKDV AAPHRQPLTS SERIDKQIRY ILDGISALRK ETCNKSNMCE SSKEALAENN
LNLPKMAEKD GCFQSGFNEE TCLVKIITGL LEFEVYLEYL QNRFESSEEQ ARAVQMSTKV
LIQFLQKKAK NLDAITTPDP TTNASLLTKL QAQNQWLQDM TTHLILRSFK EFLQSSLRAL RQMHHHHHH.

What applications can IL 6 HUMAN, SF9 Protein be used in?
IL 6 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 6 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL 6 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 6 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 IL 6 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:

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.

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 Type I Human Recombinant

Interleukin-1 receptor type 1, IL1R1, Interleukin-1 receptor type 1, IL-1R-1, IL-1RT-1,IL-1RT1, CD121 antigen-like family member A, Interleukin-1 receptor alpha, IL-1R-alpha, Interleukin-1 receptor type I, p80, CD121a, Interleukin-1 receptor type 1, membrane form, mIL-1R1, mIL-1RI, Interleukin-1 receptor type 1, soluble form, sIL-1R1, sIL-1RI, IL1R, IL1RA, IL1RT1, IL1R1, IL1R1, CD121A, D2S1473.

Product # :

CYT-923

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SDS-PAGE
Citations

Description

IL1R1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 324 amino acids (21-336a.a.) and having a molecular mass of 37.4kDa(Migrates at 40-57kDa on SDS-PAGE under reducing conditions).IL1R1 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL1R1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Interleukin-1 receptor type 1 (IL1R1) associates with the co-receptor IL1RAP to form the high affinity interleukin-1 receptor complex, which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. IL1R1 is a central mediator involved in numerous cytokine induced immune and inflammatory responses.
Synonyms
Interleukin-1 receptor type 1, IL1R1, Interleukin-1 receptor type 1, IL-1R-1, IL-1RT-1,IL-1RT1, CD121 antigen-like family member A, Interleukin-1 receptor alpha, IL-1R-alpha, Interleukin-1 receptor type I, p80, CD121a, Interleukin-1 receptor type 1, membrane form, mIL-1R1, mIL-1RI, Interleukin-1 receptor type 1, soluble form, sIL-1R1, sIL-1RI, IL1R, IL1RA, IL1RT1, IL1R1, IL1R1, CD121A, D2S1473.
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
DKCKEREEKI ILVSSANEID VRPCPLNPNE HKGTITWYKD DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN SSYCLRIKIS AKFVENEPNL CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN ENNELPKLQW YKDCKPLLLD NIHFSGVKDR LIVMNVAEKH RGNYTCHASY TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL GSQIQLICNV TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKLEHH HHHH.
Background
What is the molecular weight/Mw of IL1R1 HUMAN Protein?
IL1R1 HUMAN Protein has a total Mw of 37.4kDa.

What is the source or expression system of IL1R1 HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL1R1 HUMAN Protein?
IL1R1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1R1 HUMAN Protein?
The biological functionality of IL1R1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL1R1 HUMAN Protein?
DKCKEREEKI ILVSSANEID VRPCPLNPNE HKGTITWYKD DSKTPVSTEQ ASRIHQHKEK LWFVPAKVED SGHYYCVVRN SSYCLRIKIS AKFVENEPNL CYNAQAIFKQ KLPVAGDGGL VCPYMEFFKN ENNELPKLQW YKDCKPLLLD NIHFSGVKDR LIVMNVAEKH RGNYTCHASY TYLGKQYPIT RVIEFITLEE NKPTRPVIVS PANETMEVDL GSQIQLICNV TGQLSDIAYW KWNGSVIDED DPVLGEDYYS VENPANKRRS TLITVLNISE IESRFYKHPF TCFAKNTHGI DAAYIQLIYP VTNFQKLEHH HHHH.
What applications can IL1R1 HUMAN Protein be used in?
IL1R1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1R1 HUMAN Protein?
The endotoxin level is minimal, IL1R1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1R1 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 IL1R1 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-31 Canine Recombinant, HEK

IL-31, Interleukin 31, IL31.

Product # :

CYT-1215

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Description

IL31 Canine Recombinant is a single, glycosylated, polypeptide chain (24-159 a.a) containing a total of 136 amino acids, having a molecular mass of 25.2 kDa. IL31 is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The IL31 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Synonyms
IL-31, Interleukin 31, IL31.
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
SHMAPTHQLP PSDVRKIILE LQPLSRGLLE DYQKKETGVP ESNRTLLLCL TSDSQPPRLN SSAILPYFRA IRPLSDKNII DKIIEQLDKL KFQHEPETEI SVPADTFECK SFILTILQQF SACLESVFKS LNSGPQ.
Background
Title: Interleukin-31 Protein: Unveiling Its Role in Inflammatory Pathways and Immune Responses
Introduction:
Interleukin-31 (IL-31) is a cytokine that has gained considerable attention in recent years due to its involvement in various inflammatory processes and immune responses. Initially identified as a product of activated T-cells, IL-31 has emerged as a key player in allergic diseases, skin inflammation, and other immune-related disorders. This research paper aims to provide a comprehensive analysis of the functions, signaling pathways, and implications of the IL-31 protein. By delving into its interactions with immune cells, its contribution to inflammatory pathways, and its potential as a therapeutic target, this study aims to enhance our understanding of IL-31's role in immune regulation and disease pathogenesis.
Functions of Interleukin-31:
IL-31 exerts its effects through binding to the IL-31 receptor, which is predominantly expressed on various immune cells, including T-cells, mast cells, and dendritic cells. Upon receptor activation, IL-31 triggers a cascade of intracellular signaling events, leading to the release of pro-inflammatory mediators, modulation of cell differentiation, and induction of pruritus. Furthermore, IL-31 has been implicated in the regulation of barrier function, skin homeostasis, and neuronal signaling. Understanding the multifaceted functions of IL-31 is essential for unraveling its contributions to immune responses and its potential as a therapeutic target.
Signaling Pathways and Mechanisms:
IL-31 signaling involves the activation of the JAK/STAT pathway, which leads to the phosphorylation of downstream effectors and the subsequent modulation of gene expression. Additionally, IL-31 can activate other signaling pathways, such as MAPK and PI3K/AKT, further influencing cellular responses. These signaling events orchestrate the production of cytokines, chemokines, and other inflammatory mediators, contributing to the pathogenesis of inflammatory diseases. Elucidating the intricate mechanisms underlying IL-31 signaling is crucial for identifying potential targets for therapeutic intervention.
Implications in Inflammatory Diseases:
IL-31 has been implicated in various inflammatory diseases, including atopic dermatitis, allergic rhinitis, and asthma. Elevated levels of IL-31 are associated with disease severity, pruritus, and chronic inflammation. Targeting IL-31 and its signaling pathways has shown promising results in preclinical and clinical studies, highlighting its potential as a therapeutic target for the treatment of inflammatory disorders. Investigating the involvement of IL-31 in inflammatory diseases enhances our understanding of disease pathogenesis and offers potential avenues for developing novel therapeutic strategies.
Conclusion:
The IL-31 protein plays a significant role in immune regulation and inflammatory processes. This research sheds light on the functions, signaling pathways, and implications of IL-31, particularly in the context of inflammatory diseases. Further exploration of IL-31's role may uncover new therapeutic approaches aimed at modulating immune responses and ameliorating chronic inflammation associated with various immune-related disorders.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on IL-31 for a comprehensive list of references and sources.

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

Description:

Interleukin-17 Rat Recombinant

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

Product # :

CYT-542

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Description

Interleukin-17A Rat Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain having a molecular mass of 30 kDa. The IL-17A Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 10mM NaCitrate, pH-3.0.

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 dose-dependent induction of IL-6 by mouse NIH 3T3 fibroblasts is 0.44-0.66ng/ml.

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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, Interleukin-17A.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin Rat 17A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat 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 Rat 17A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAVLIPQSSV CPNAEANNFL QNVKVNLKVL NSLSSKASSR RPSDYLNRST SPWTLSRNED PDRYPSVIWE AQCRHQRCVN AEGKLDHHMN SVLIQQEILV LKREPEKCPF TFRVEKMLVG VGCTCVSSIV RHAS.

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, His Tag

Interleukin-1 alpha, IL-1 alpha.

Product # :

CYT-913

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Description

IL 1 alpha Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (115-270 a.a) and having a molecular mass of 20.2kDa. IL 1 alpha is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL 1 alpha protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The biological activity was Rat IL1 alpha was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 20 pg/ml.

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Introduction
IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
Synonyms
Interleukin-1 alpha, IL-1 alpha.
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 MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD RIHLKAASLN DLQLEVKFDM YAYSSGGDDS KYPVTLKVSN TQLFVSAQGE DKPVLLKEIP ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.
Background
What is the molecular weight/Mw of IL1A RAT, HIS Protein?
IL1A RAT, HIS Protein has a total Mw of 20.2kDa.

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

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

What is the Biological Activity of IL1A RAT, HIS Protein?
The biological activity was Rat IL1 alpha was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell. The ED50 for this effect is less or equal to 20 pg/ml.

What is the amino acid sequence of IL1A RAT, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD RIHLKAASLN DLQLEVKFDM YAYSSGGDDS KYPVTLKVSN TQLFVSAQGE DKPVLLKEIP ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.

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

What is the endotoxin level for IL1A RAT, HIS Protein?
The endotoxin level is minimal, IL1A RAT, 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-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

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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-1 Alpha Rhesus Macaque 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-790

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Shipped at Room temp

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Description

Recombinant IL 1 alpha Rhesus Macaque produced in E.coli cells is a non-glycosylated, homodimeric protein containing 159 amino acid chain and having a molecular mass of 18.1kDa. The IL 1 alpha is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The IL 1 alpha 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 a cell proliferation assay using murine D10S cells is less than 10 pg/ml, corresponding to a specific activity of > 1.0×10⁸IU/mg.

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Introduction
IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
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 IL 1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1 alpha 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 1 alpha Recombinant in sterile distilled H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SAPFSFLSNM TYHFIRIIKH EFILNDTLNQ TIIRANDQHL TAAAIHNLDE AVKFDMGAYT SSKDDTKVPV ILRISKTQLY VSAQDEDQPV LLKEMPEINK TITGSETNFL FFWETHGTKN YFISVAHPNL FIATKHDNWV CLAKGLPSIT DFQILENQA
Background
What is the molecular weight/Mw of IL1A RHESUS MACAQUE Protein?
IL1A RHESUS MACAQUE Protein has a total Mw of 18.1kDa.

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

What is the Purity of IL1A RHESUS MACAQUE Protein?
IL1A RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A RHESUS MACAQUE Protein?
The ED50 as determined by a cell proliferation assay using murine D10S cells is less than 10 pg/ml, corresponding to a specific activity of > 1.0×108IU/mg.

What is the amino acid sequence of IL1A RHESUS MACAQUE Protein?
SAPFSFLSNM TYHFIRIIKH EFILNDTLNQ TIIRANDQHL TAAAIHNLDE AVKFDMGAYT SSKDDTKVPV ILRISKTQLY VSAQDEDQPV LLKEMPEINK TITGSETNFL FFWETHGTKN YFISVAHPNL FIATKHDNWV CLAKGLPSIT DFQILENQA

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

What is the endotoxin level for IL1A RHESUS MACAQUE Protein?
The endotoxin level is minimal, IL1A RHESUS MACAQUE 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-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

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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:

Interleukin-6 Rat Recombinant

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

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CYT-388

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Description

Interleukin-6 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids and having a molecular mass of 21732 Dalton. The IL6 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from 0.02% TFA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ is less than 0.01 ng/ml as determined by dose-dependent stimulation of mouse 7TD1 cells.

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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 Interleukin-6 with 10mM HCl at a concentration of 0.1 mg/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-Phe-Pro-Thr-Ser.
Background
Research Paper on Interleukin-6 Rat Recombinant
Abstract:
Exploring Interleukin-6 Rat Recombinant: This research paper provides an extensive description of Interleukin-6 (IL-6) Rat Recombinant, a vital cytokine in immunological studies. We delve into its molecular properties, significance in immune responses, and its synonyms, including DIF, TNFA, and TNFSF2. Join us as we uncover the potential applications of IL-6 Rat Recombinant in advancing our understanding of immune regulation.
Introduction:
Unraveling IL-6 Rat Recombinant: This paper introduces IL-6 Rat Recombinant, a valuable tool for investigating immune responses. As researchers, we are intrigued by its diverse functions and potential therapeutic implications.
An Extensive Description of IL-6 Rat Recombinant:
We present a comprehensive overview of IL-6 Rat Recombinant, focusing on its structural characteristics and involvement in immune signaling. This recombinant cytokine allows us to explore the complexities of IL-6 biology and its impact on immune system homeostasis.
Significance in Immune Responses:
Marvel at IL-6's pivotal role in orchestrating immune responses! As a crucial mediator between immune cells, IL-6 plays a critical role in regulating inflammation and immune cell activation. It also contributes to tissue repair and antibody production.
Interactions and Synonyms:
Learn about the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2. Understanding these synonyms enhances our comprehension of the interconnected cytokine network, contributing to a broader understanding of immune signaling.
Potential Applications in Immunological Research:
Explore the diverse applications of IL-6 Rat Recombinant in immunological research. From deciphering cellular responses to developing potential therapeutics, this recombinant cytokine serves as an indispensable tool for advancing our knowledge of the immune system. Researchers use it for in vitro studies, functional assays, and investigating disease pathogenesis.
Novel Insights and Therapeutic Implications:
Gain novel insights into the therapeutic implications of IL-6 Rat Recombinant. Understanding its role in disease pathogenesis may lead to the development of targeted therapies for various immune-related disorders. Clinical trials targeting IL-6 have shown promise in treating certain inflammatory conditions.
Conclusion:
Concluding our exploration of IL-6 Rat Recombinant, we recognize its significance in immunological research. The extensive description of this recombinant cytokine broadens our understanding of IL-6 biology and its potential applications in various fields. By utilizing this powerful tool, we strive to make significant advancements in immunology research for improved health outcomes.
What is the molecular weight/Mw of IL6 RAT Protein?
IL6 RAT Protein has a total Mw of 21.7kDa.

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

What is the Purity of IL6 RAT Protein?
IL6 RAT Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL6 RAT Protein?
The ED50 is less than 0.01 ng/ml as determined by dose-dependent stimulation of mouse 7TD1 cells.

What is the amino acid sequence of IL6 RAT Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Phe-Pro-Thr-Ser.

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

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

Who supplies recombinant IL6 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 IL6 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 0.55 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-6 as a Reference Standard.

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

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