Search: 1000 results found for "Anti Human Cytokine"

Description:

Interleukin-7 Human Recombinant, His Tag

Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

Product # :

CYT-485

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Description

IL-7 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 21.97 kDa with an amino-terminal hexahistidine tag. The IL-7 His-Tag protein is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin -7 His is supplied in 1x PBS and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Interleukin-7 is a potent lymphoid cell growth factor produced primarily by stromal cells.
IL-7 has been shown to support the proliferation and differentiation of pre B- and early T cells as well as displaying a biological effect on cells of NK and myeloid lineages.
Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
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 IL7 HUMAN, HIS Protein?
IL7 HUMAN, HIS Protein has a total Mw of 21.97kDa.

What is the source or expression system of IL7 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL7 HUMAN, HIS Protein?
IL7 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of IL7 HUMAN, HIS Protein?
IL7 HUMAN, HIS Protein is composed from 152 amino acids.

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

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

Who supplies recombinant IL7 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 IL7 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-28A Human Recombinant

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

Product # :

CYT-602

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Shipped at Room temp

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Description

IL-28A human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 19.6 kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2 μm filtered solution containing no additives.

Purity

Greater than 85% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
IL-28A is distantly related to type I IFNs 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, IFN-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-Lambda 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 2 Recombinant should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-28A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPVAR LHGALPDARG CHIAQFKSLS PQELQAFKRAKDALEESLLL KDCRCHSRLF PRTWDLRQLQ VRERPMALEA ELALTLKVLE ATADTDPALV DVLDQPLHTL HHILSQFRAC IQPQPTAGPR TRGRLHHWLY RLQEAPKKES PGCLEASVTFNLFRLLTRDL NCVASGDLCV.

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

Description:

Interleukin 17F Human Recombinant, sf9

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

Product # :

CYT-1017

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Description

IL17F produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids (31-163 a.a.) and having a molecular mass of 16kDa (Molecular size on SDS-PAGE will appear at approximately 18-28 kDa). IL17F is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL17F protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
IL-17F having an accession number of Q96PD4 is a cytokine that shares sequence similarity with IL17. IL-17F is expressed by activated T cells, and has been shown to stimulate the production of several other cytokines, including IL6, IL8, and CSF2/GM_CSF. IL-17F inhibits the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. IL-17F induces stromal cells to produce proinflammatory and hematopoietic cytokines. Intestinal IL17F gene expression is increased in active CD.
IL-17A & IL-17F alleles influence the susceptibility to and pathophysiological features of ulcerative colitis independently. IL-17F and MIF gene polymorphisms are significantly associated with the development of functional dyspepsia.
The initiation of IL-17F/IL-17R signaling pathway requires the receptor ubiquitination by TRAF6. IL-17F induces expression of IFN-gamma-inducible protein 10 (IP-10) by activating Raf1-mitogen-activated protein kinase 1/2-extracellular-regulated kinase 1/2-p90 ribosomal S6 kinase-cyclic AMP response element-binding protein signaling pathway.
Synonyms
Cytokine ML-1, IL-17F, Interleukin-17F precursor, IL17F, ML1, ML-1.
Physical Appearance
Sterile Filtered 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
ADPRKIPKVG HTFFQKPESC PPVPGGSMKL DIGIINENQR VSMSRNIESR STSPWNYTVT WDPNRYPSEV VQAQCRNLGC INAQGKEDIS MNSVPIQQET LVVRRKHQGC SVSFQLEKVL VTVGCTCVTP VIHHVQHHHH HH.

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

Description:

Tumor Necrosis Factor-Alpha Human Recombinant

TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

Product # :

CYT-223

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Description

Tumor Necrosis Factor-a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (157 a.a. of the mature human TNF-alpha and an N-terminal methionine) and having a molecular mass of 17.5kDa. The TNF-alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNF-a Human was lyophilized from a concentrated 1mg/ml solution containing 20mM PB, pH-7.2, and 100mM NaCl.

Purity

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

Biological Activity

The Specific Activity is >5.0×10⁷ IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, INS resistance, and cancer.
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA E AKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL.
Background
TNF Alpha Human: An Overview of Its Role and Importance in Immunology
TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.
This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.
Production and Properties
Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.
Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.
Solubility and Usage
The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.
This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.
Storage and Stability
For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.
Biological Role and Implications
TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.
Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.
Mechanism of Action
TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.
Research and Clinical Importance
Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.
Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.
In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune diseases.

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 Induced-1 Human Recombinant

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

Product # :

CYT-1209

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Shipped with Ice Packs

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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:

Eotaxin-2, Mouse Anti Human

C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

Product # :

ANT-127

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Quantity :

Shipping Method :

Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
Eotaxin-2, also called MPIF2 & Ck?6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3.
Synonyms
C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human Eotaxin-2.
Ig Subclass
Mouse IgG.
Clone
NYRhEOT2.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.4 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion exchange.

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

Description:

Interleukin-2 Human Recombinant, His Tag

T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2, IL2.

Product # :

CYT-666

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Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 133 amino acids fragment (21-153) having a molecular weight of 20kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL-2 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-2 His-Tag protein is supplied in 20mM Tris-HCl pH-8 and 50% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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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), Interleukin-2, Lymphokine, IL-2, IL2.
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 2 HUMAN, HIS Protein?
IL 2 HUMAN, HIS Protein has a total Mw of 20kDa.

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

What is the Purity of IL 2 HUMAN, HIS Protein?
IL 2 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 2 HUMAN, HIS Protein?
The biological functionality of IL 2 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL 2 HUMAN, HIS Protein?
T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2, IL2.

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

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

Who supplies recombinant IL 2 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 2 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-9 Human Recombinant, Sf9

Interleukin 9, T-Cell Growth Factor P40,Homolog Of Mouse T Cell And Mast Cell Growth Factor 40, P40 T-Cell And Mast Cell Growth Factor, P40 Cytokine, Cytokine P40, IL-9, Interleukin-9, HP40, P40.

Product # :

CYT-866

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL-9 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-144 a.a.) including an 18 aa signal peptide (1-18 aa) and fused to a 6 aa His Tag at C-terminus containing a total of 150 amino acids and having a molecular mass of 14.5kDa.IL9 shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL-9 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IL-9 is a factor which is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
Synonyms
Interleukin 9, T-Cell Growth Factor P40,Homolog Of Mouse T Cell And Mast Cell Growth Factor 40, P40 T-Cell And Mast Cell Growth Factor, P40 Cytokine, Cytokine P40, IL-9, Interleukin-9, HP40, P40.
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
MLLAMVLTSA LLLCSVAGQG CPTLAGILDI NFLINKMQED PASKCHCSAN VTSCLCLGIP SDNCTRPCFS ERLSQMTNTT MQTRYPLIFS RVKKSVEVLK NNKCPYFSCE QPCNQTTAGN ALTFLKSLLE IFQKEKMRGM RGKIHHHHHH.
Background
What is the molecular weight/Mw of IL9 HUMAN, SF9 Protein?
IL9 HUMAN, SF9 Protein has a total Mw of 23kDa.

What is the source or expression system of IL9 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL9 HUMAN, SF9 Protein?
IL9 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL9 HUMAN, SF9 Protein?
The biological functionality of IL9 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of IL9 HUMAN, SF9 Protein?
MLLAMVLTSA LLLCSVAGQG CPTLAGILDI NFLINKMQED PASKCHCSAN VTSCLCLGIP SDNCTRPCFS ERLSQMTNTT MQTRYPLIFS RVKKSVEVLK NNKCPYFSCE QPCNQTTAGN ALTFLKSLLE IFQKEKMRGM RGKIHHHHHH.

What applications can IL9 HUMAN, SF9 Protein be used in?
IL9 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL9 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL9 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL9 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 IL9 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-36 Receptor Antagonist Human Recombinant

Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).

Product # :

CYT-009

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Description

IL1F5 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17kDa.The IL1F5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL1F5 was lyophilized after extensive dialysis against 20mM Phosphate buffer, pH7.4.

Purity

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

Biological Activity

As measured by its binding ability in a functional ELISA, immobilized IL1F5 at 1 µg/ml (100 µl/well) can bind rHuIL-1 Rrp2/Fc Chimera with a linear range of 0.15- 5 µg/ml.

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Introduction
Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.
Synonyms
Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL1F5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F5 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 quick spin followed by reconstitution of IL1F5 in PBS to a concentration no less than 100 µg/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-Val-Leu-Ser-Gly.

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:

Flt3 Ligand Human Recombinant

Fms-Related Tyrosine Kinase 3 Ligand, Flt3 Ligand, Flt-3 Ligand, SL Cytokine.

Product # :

CYT-331

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Description

Flt3-Ligand Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.6kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with no additives.

Purity

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

Biological Activity

The ED₅₀ as calculated by the dose-dependent stimulation of the proliferation of human AML5 cells is less than 1.0 ng/ml, corresponding to a Specific Activity of 1.0×10⁶ IU/mg.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-Related Tyrosine Kinase 3 Ligand, Flt3 Ligand, Flt-3 Ligand, SL Cytokine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA.
Background

What is the molecular weight/Mw of FLT3 LIGAND HUMAN Protein?
FLT3 LIGAND HUMAN Protein has a total Mw of 17.6kDa.

What is the source or expression system of FLT3 LIGAND HUMAN Protein?
Escherichia Coli.

What is the Purity of FLT3 LIGAND HUMAN Protein?
FLT3 LIGAND HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3 LIGAND HUMAN Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of human AML5 cells is less than 1.0 ng/ml, corresponding to a Specific Activity of 1.0×106 IU/mg.

What is the amino acid sequence of FLT3 LIGAND HUMAN Protein?
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA.

What applications can FLT3 LIGAND HUMAN Protein be used in?
FLT3 LIGAND HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3 LIGAND HUMAN Protein?
The endotoxin level is minimal, FLT3 LIGAND 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:

Eotaxin-1, Mouse Anti-Human

Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

Product # :

ANT-126

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophilsby inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligandinclude CCR2, CCR3and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human Eotaxin-1.
Ig Subclass
Mouse IgG1.
Clone
YNRhEOT1.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
Purification Method
Ion exchange.

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

Description:

Interleukin 9 Human Recombinant, Sf9, Active

Interleukin 9, Protein Il9, Il9, HP40, Cytokine P40, T-cell growth factor P40

Product # :

CYT-1143

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Shipped with Ice Packs

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Description

IL-9 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 132 amino acids (19-144 aa) and having a molecular mass of 14.9kDa.IL-9 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL-9 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 85.0% as determined by SDS-PAGE.

Biological Activity

Determined by cell proliferation assay using MO7e human megakaryocytic leukemic cells. ED50 range for this effect is ≤ 0.3 ng/ml.

SDS-PAGE

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Introduction
Interleukin-9 is a protein that acts as one of the regulators of hematopoiesis. IL-9 is an enhancer of cells and megakaryoblastic leukemic cells’ growth. Among this protein’s producers we can find cells like mast cells, Treg, NKT cells, Th17, Th2, ILC2, and Th9 cells in various amounts. Th9 are the primary CD4 cells (T cells) that IL-9 is produced in.
Synonyms
Interleukin 9, Protein Il9, Il9, HP40, Cytokine P40, T-cell growth factor P40
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
QGCPTLAGIL DINFLINKMQ EDPASKCHCS ANVTSCLCLG IPSDNCTRPC FSERLSQMTN
TTMQTRYPLI FSRVKKSVEV LKNNKCPYFS CEQPCNQTTA GNALTFLKSL LEIFQKEKMR GMRGKIHHHH HH
Background
What is the molecular weight/Mw of IL9 HUMAN, SF9 ACTIVE Protein?
IL9 HUMAN, SF9 ACTIVE Protein has a total Mw of 14.9kDa.

What is the source or expression system of IL9 HUMAN, SF9 ACTIVE Protein?
Sf9, Baculovirus cells.

What is the Purity of IL9 HUMAN, SF9 ACTIVE Protein?
IL9 HUMAN, SF9 ACTIVE Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL9 HUMAN, SF9 ACTIVE Protein?
Determined by cell proliferation assay using MO7e human megakaryocytic leukemic cells. ED50 range for this effect is ≤ 0.3 ng/ml.

What is the amino acid sequence of IL9 HUMAN, SF9 ACTIVE Protein?
QGCPTLAGIL DINFLINKMQ EDPASKCHCS ANVTSCLCLG IPSDNCTRPC FSERLSQMTN
TTMQTRYPLI FSRVKKSVEV LKNNKCPYFS CEQPCNQTTA GNALTFLKSL LEIFQKEKMR GMRGKIHHHH HH.

What applications can IL9 HUMAN, SF9 ACTIVE Protein be used in?
IL9 HUMAN, SF9 ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL9 HUMAN, SF9 ACTIVE Protein?
The endotoxin level is minimal, IL9 HUMAN, SF9 ACTIVE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL9 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 IL9 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:

Allograft Inflammatory Factor 1 Human Recombinant

AIF-1, Allograft inflammatory factor 1, Em:AF129756.17, G1, IBA1, Ionized calcium-binding adapter molecule 1, IRT-1, Protein G1, AIF1.

Product # :

CYT-697

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Shipped with Ice Packs

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Description

AIF1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147a.a.) and having a molecular mass of 18.9kDa. AIF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E. Coli.

Formulation

The AIF1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
2mM DTT, 200mM NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS PAGE.

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Introduction
Human AIF1 protein shares 98% homology/identity with that of rat. AIF1 is expressed in macrophages and neutrophils. The expression of AIF1 transcripts is upregulated by IFN-g in rat macrophages. AIF1 is expressed selectively in human macrophage-like cell lines, and in a subset of CD68(+) macrophages in the interstitial and perivascular spaces of human heart allografts. In quiescent cultured human vascular smooth muscle cells synthesis of AIF1 is induced by IFN-g, IL1b, and conditioned medium of T-cells. Overexpression of AIF1 in human VSMCs results in enhanced growth of these cells. AIF1 is expressed during apoptosis rat mammary gland and ventral prostate tissues. Allograft Inflammatory Factor 1 is expressed by several tumor-associated activated macrophages and microglial cells in rat and human gliomas. There is an evident relationship of AIF1-expressing activated macrophages and microglial cells with tumor malignancy in humans.
Synonyms
AIF-1, Allograft inflammatory factor 1, Em:AF129756.17, G1, IBA1, Ionized calcium-binding adapter molecule 1, IRT-1, Protein G1, AIF1.
Stability
Store AIF1 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 MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP.
Background
Allograft Inflammatory Factor 1 Human Recombinant: Uncovering its Role in Immune Responses and Therapeutic Prospects
1. Abstract
This paper explores the Allograft Inflammatory Factor 1 Human Recombinant (AIF-1), a cytoplasmic, IFN-gamma-inducible calcium-binding protein involved in inflammation and immunity. We review the structure, biological roles, and involvement of AIF-1 in disease pathology. The therapeutic potential of AIF-1 in immune-related disorders is also explored.
2. Introduction
AIF-1, also known as IBA1, plays an important role in immune responses. It is associated with various immune cells, particularly macrophages, and has been implicated in numerous inflammatory and immune-related diseases. Understanding the function of AIF-1 could aid the development of novel therapeutic strategies.
3. Structure and Signaling of AIF-1
AIF-1 is a small 17 kDa protein with an EF-hand calcium-binding motif. Although the precise mechanism by which AIF-1 exerts its functions is not entirely clear, it is known to regulate the activation, migration, and proliferation of macrophages, key cells involved in immune responses.
4. Biological Functions of AIF-1
AIF-1 has been shown to play key roles in macrophage activation and function, which are central to inflammation and immunity. It is also implicated in cell survival, proliferation, and differentiation.
5. AIF-1 in Disease Pathology
AIF-1 has been associated with a range of inflammatory and immune-related diseases, including rheumatoid arthritis, atherosclerosis, and multiple sclerosis. It is also implicated in several cancers, further underscoring its broad physiological and pathological relevance.
6. Therapeutic Potential of AIF-1
Given its pivotal role in immune responses, AIF-1 presents an intriguing target for therapeutic interventions in immune-related diseases. Modulating the activity of AIF-1 could potentially alleviate pathological inflammation and autoimmunity.
7. Conclusion and Future Perspectives
Our knowledge of AIF-1 and its functions has significantly improved in recent years, but much remains to be discovered. Further research into AIF-1's exact molecular mechanisms and roles in disease will undoubtedly contribute to the development of novel therapeutic strategies.
What is the molecular weight/Mw of AIF1 Protein?
AIF1 Protein has a total Mw of 18.9kDa.

What is the source or expression system of AIF1 Protein?
Escherichia Coli.

What is the Purity of AIF1 Protein?
AIF1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of AIF1 Protein?
The biological functionality of AIF1 Protein will be determined in the future.

What is the amino acid sequence of AIF1 Protein?
MGSSHHHHHH SSGLVPRGSH MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP.

What applications can AIF1 Protein be used in?
AIF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for AIF1 Protein?
The endotoxin level is minimal, AIF1 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:

Macrophage Inflammatory-3 Beta CCL19, Mouse Anti-Human

Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433.

Product # :

ANT-213

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Quantity :

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Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
Chemokine (C-C motif) ligand 19 (CCL19) is a small cytokine belonging to the CC chemokine family that is also known as EBI1 ligand chemokine (ELC) and macrophage inflammatory protein-3-beta (MIP-3-beta). CCL19 is expressed abundantly in thymus and lymph nodes, with moderate levels in trachea and colonand low levels in stomach, small intestine, lung, kidney and spleen. The gene for CCL19 is located on human chromosome 9. This chemokine elicits its effects on its target cells by binding to the chemokine receptor chemokine receptor CCR7. It attracts certain cells of the immune system, including dendritic cellsand antigen-engaged B cells.
Synonyms
Small inducible cytokine A19, CCL19, Macrophage inflammatory protein 3 beta, MIP-3- beta, EBI1-ligand chemokine, ELC, Beta chemokine exodus-3, CK beta-11, chemokine (C-C motif) ligand 19, CKb11, MIP3B, MIP-3b, SCYA19, MGC34433.
Solubility
Reconstitute with 0.5ml of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human MIP-3b.
Ig Subclass
Mouse IgG1.
Clone
YNR-HMIP3b.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.4 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Type
Mouse Anti Human Monoclonal.
Storage Procedures
Lyophilized: store at 4 C. After reconstitution, if not intended for use within a month, aliquot and store at 20 C.
Purification Method
Protein A.

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 17B Human Recombinant

Interleukin-17B, IL-17B, Cytokine Zcyto7, Interleukin-20, Neuronal interleukin-17-related factor, IL20, NIRF, ZCYTO7.

Product # :

CYT-771

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Quantity :

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Shipped at Room temp

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Description

Interleukin-17B Human Recombinant produced in E.Coli is a homodimeric, non-disulfide-linked polypeptide chain containing a total of 322 amino acids (2 chains of 161aa) and having a molecular mass of 36.5kDa. The IL-17B is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-17B was Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4, 0.05% Tween-20 and 3%Trehalose.

Purity

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

Biological Activity

The ED50 as determined by inducing IL-8 secretion of human HepG2 cells is less than 1.0µg/ml, corresponding to a specific activity of > 1000 IU/mg.

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Introduction
IL-17 family members are glycoproteins secreted as dimers which induce local cytokine production and recruit granulocytes to sites of inflammation. The IL-17 family is comprised of at least six pro-inflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 is induced by IL-15 and IL-23, mostly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL17B Diseases associated with IL17B include spondyloarthropathy, and neuronitis, and among its related super-pathways are Mucin expression in CF via IL-6, IL-17 signaling pathways and STAT3 Pathway.
Synonyms
Interleukin-17B, IL-17B, Cytokine Zcyto7, Interleukin-20, Neuronal interleukin-17-related factor, IL20, NIRF, ZCYTO7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin 17B although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution IL17B should be stored at 4C between 2-7 days and for future use below -18C. 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 17B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQPRSPKSKR KGQGRPGPLA PGPHQVPLDL VSRMKPYARM EEYERNIEEM VAQLRNSSEL AQRKCEVNLQ LWMSNKRSLS PWGYSINHDP SRIPVDLPEA RCLCLGCVNP FTMQEDRSMV SVPVFSQVPV RRRLCPPPPR TGPCRQRAVM ETIAVGCTCI F.

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

Description:

Interleukin-2 Receptor Gamma Human Recombinant

Interleukin 2 Receptor Gamma, IL-2 Receptor Subunit Gamma, IL-2R Subunit Gamma, CD132 Antigen, SCIDX1, IL-2RG, GammaC, SCIDX, IMD4, P64, Cytokine Receptor Common Subunit Gamma, Common Cytokine Receptor Gamma Chain, Interleukin-2 Receptor Subunit Gamma, Combined Immunodeficiency X-Linked, Severe Combined Immunodeficiency, CD132, CIDX, IL2RG.

Product # :

CYT-471

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Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL2RG Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 246 amino acids (23-262 a.a.) and having a molecular mass of 29kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).IL2RG is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL2RG protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 80.0% by SDS-PAGE.

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Introduction
Interleukin-2 Receptor Gamma (IL2RG) is a cytokine receptor sub-unit which is common to the receptor complexes for at least six different interleukin receptors. IL2RG is located on the surface of immature blood-forming cells in bone marrow. One end of the IL2RG protein resides outside of the cell where it binds to cytokines and the other end of the IL2RG protein resides in the interior of the cell where it transmits signals to the cell's nucleus. IL2RG teams up with other proteins to direct blood-forming cells to form lymphocytes. In addition, IL2RG directs the growth and maturation of lymphocyte subtypes, which kill viruses, make antibodies, and help regulate the entire immune system.
Synonyms
Interleukin 2 Receptor Gamma, IL-2 Receptor Subunit Gamma, IL-2R Subunit Gamma, CD132 Antigen, SCIDX1, IL-2RG, GammaC, SCIDX, IMD4, P64, Cytokine Receptor Common Subunit Gamma, Common Cytokine Receptor Gamma Chain, Interleukin-2 Receptor Subunit Gamma, Combined Immunodeficiency X-Linked, Severe Combined Immunodeficiency, CD132, CIDX, IL2RG.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
LNTTILTPNG NEDTTADFFL TTMPTDSLSV STLPLPEVQC FVFNVEYMNC TWNSSSEPQP TNLTLHYWYK NSDNDKVQKC SHYLFSEEIT SGCQLQKKEI HLYQTFVVQL QDPREPRRQA TQMLKLQNLV IPWAPENLTL HKLSESQLEL NWNNRFLNHC LEHLVQYRTD WDHSWTEQSV DYRHKFSLPS VDGQKRYTFR VRSRFNPLCG SAQHWSEWSH PIHWGSNTSK ENPFLFALEA HHHHHH.
Background
What is the molecular weight/Mw of IL2 RG HUMAN Protein?
IL2 RG HUMAN Protein has a total Mw of 29kDa.

What is the source or expression system of IL2 RG HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL2 RG HUMAN Protein?
IL2 RG HUMAN Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of IL2 RG HUMAN Protein?
The biological functionality of IL2 RG HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL2 RG HUMAN Protein?
LNTTILTPNG NEDTTADFFL TTMPTDSLSV STLPLPEVQC FVFNVEYMNC TWNSSSEPQP TNLTLHYWYK NSDNDKVQKC SHYLFSEEIT SGCQLQKKEI HLYQTFVVQL QDPREPRRQA TQMLKLQNLV IPWAPENLTL HKLSESQLEL NWNNRFLNHC LEHLVQYRTD WDHSWTEQSV DYRHKFSLPS VDGQKRYTFR VRSRFNPLCG SAQHWSEWSH PIHWGSNTSK ENPFLFALEA HHHHHH.

What applications can IL2 RG HUMAN Protein be used in?
IL2 RG HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL2 RG HUMAN Protein?
The endotoxin level is minimal, IL2 RG HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL2 RG 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 IL2 RG 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

Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

Product # :

CYT-254

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Description

Interleukin-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 17.4 kDa. The IL-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 1x PBS pH-7.4.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependant stimulation of murine 2E8 cells is < 0.5ng/ml, corresponding to a Specific Activity of 2,000,000 IU/mg.

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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
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 -7 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DCDIEGKDG KQYESVLMVS IDQLLDSMKE IGSNCLNNEF NFFKRHICDA NKEGMFLFRA ARKLRQFLKM NSTGDFDLHL LKVSEGTTIL LNCTGQVKGR KPAALGEAQP TKSLEENKSL KEQKKLNDLC FLKRLLQEIK TCWNKILMGT KEH.
Background
What is the molecular weight/Mw of IL7 HUMAN Protein?
IL7 HUMAN Protein has a total Mw of 17.4kDa.

What is the source or expression system of IL7 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL7 HUMAN Protein?
IL7 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL7 HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of murine 2E8 cells is < 0.5ng/ml, corresponding to a Specific Activity of 2,000,000 IU/mg.

What is the amino acid sequence of IL7 HUMAN Protein?
DCDIEGKDG KQYESVLMVS IDQLLDSMKE IGSNCLNNEF NFFKRHICDA NKEGMFLFRA ARKLRQFLKM NSTGDFDLHL LKVSEGTTIL LNCTGQVKGR KPAALGEAQP TKSLEENKSL KEQKKLNDLC FLKRLLQEIK TCWNKILMGT KEH.

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

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

Who supplies recombinant IL7 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 IL7 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-13 Human Recombinant

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

Product # :

CYT-446

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Description

Interleukin-13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids and having a molecular mass of 12 kDa. The IL-13 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized with 1xPBS pH-7.2 & 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 x 10⁶units/mg.

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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
NC30, ALRH, BHR1, P600, IL-13, MGC116786, MGC116788, MGC116789.
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
GPVPPSTALRELIEELVNITQNQKAPLCNGSMVWSINLTAGMYCAALESLINVS
GCSAIEKTQRMLSGFCPHKVSAGQFSSLHVRDTKIEVAQFVKDLLLHLKKLFRE
GRFN.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.57 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:

Endothelial-Monocyte Activating Polypeptide II Human Recombinant

AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

Product # :

CYT-607

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Description

EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.

Purity

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

Biological Activity

Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

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Introduction
EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
Synonyms
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EMAP-II although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EMAP-II 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 EMAP-II in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
Background
What is the molecular weight/Mw of EMAP II HUMAN Protein?
EMAP II HUMAN Protein has a total Mw of 18.3kDa.

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

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

What is the Biological Activity of EMAP II HUMAN Protein?
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

What is the amino acid sequence of EMAP II HUMAN Protein?
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

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

What is the endotoxin level for EMAP II HUMAN Protein?
The endotoxin level is minimal, EMAP II 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 1 Family, Member 10 Human Recombinant

Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.

Product # :

CYT-012

Price :

Quantity :

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Shipped at Room temp

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Description

IL1F10 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 152 amino acids and having a molecular mass of 17kDa.The IL1F10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL1F10 was lyophilized after extensive dialysis against 20mM Phosphate buffer, pH7.4.

Purity

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

Biological Activity

As measured by its binding ability in a functional ELISA, immobilized IL1F10 at 1 µg/ml (100 µl/well) can bind rHuIL-1 Rrp2/Fc Chimera with a linear range of 0.15- 5 µg/ml.

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Introduction
Human interleukin family 1, member 10 (IL1F10) belongs to the interleukin 1 cytokine family. IL1F10 is expressed in the fetal skin, spleen and tonsil, generally in the basal epithelia of skin and in proliferating B-cells of the tonsil. IL1F10 binds soluble IL1 receptor type 1 and may be implicated in the regulation of adapted and innate immune responses.
Synonyms
Interleukin-1 family member 10, IL-1F10, FIL1 theta, Interleukin-1 HY2, IL-1HY2, Interleukin-1 theta, IL-1 theta, IL1F10, FIL1T, IL1HY2, FKSG75, MGC119831, MGC119832, MGC119833, FIL1-theta.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL1F10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F10 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 quick spin followed by reconstitution of IL1F10 in PBS to a concentration no less than 100 µg/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-Cys-Ser-Leu-Pro.

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:

Aminoacyl tRNA Synthetase Complex-Interacting Multifunctional Protein 1 Human Recombinant

Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.

Product # :

CYT-021

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Shipped with Ice Packs

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Description

AIMP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 356 amino acids (1-336 a.a.) and having a molecular mass of 39.2kDa (Molecular size on SDS-PAGE will appear higher). The AIMP1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The AIMP1 solution (0.25mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

sds-page

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Introduction
AIMP1 (EMPA2 or p43) is a cytokine that is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of the AIMP1 cytokine renders the tumor-associated vasculature sensitive to tumor necrosis factor. Furthermore, AIMP1 is involved in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
Synonyms
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
Background
What is the molecular weight/Mw of AIMP1 HUMAN Protein?
AIMP1 HUMAN Protein has a total Mw of 39.2kDa.

What is the source or expression system of AIMP1 HUMAN Protein?
Escherichia Coli.

What is the Purity of AIMP1 HUMAN Protein?
AIMP1 HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of AIMP1 HUMAN Protein?
The biological functionality of AIMP1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of AIMP1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

What applications can AIMP1 HUMAN Protein be used in?
AIMP1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for AIMP1 HUMAN Protein?
The endotoxin level is minimal, AIMP1 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-29 Human Recombinant

Interleukin-29, IL-29, IFN-Lambda 1, IFN-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.

Product # :

CYT-603

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Shipped at Room temp

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Description

IL-29 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2 μm filtered solution containing no additives.

Purity

Greater than 90% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
IL-29 is distantly related to type I IFNs and the IL-10 family. Expression of IL-29 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-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-29 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-lambda3 are closely positioned genes on human chromosome 19.
IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 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.
IFN-Lambda 1 antiviral and antiproliferative activity requires IFN-Lambda 2 receptor tyrosine residues.
Synonyms
Interleukin-29, IL-29, IFN-Lambda 1, IFN-Lambda 1, Cytokine ZCYTO21, IL29, IFNL1, ZCYTO21.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-Lambda 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 1 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-29 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPVPTSKPTTT GKGCHIGRFK SLSPQELASF KKARDALEES LKLKNWSCSS PVFPGNWDLR LLQVRERPVA LEAELALTLK VLEAAAGPAL EDVLDQPLHTLHHILSQLQA CIQPQPTAGP RPRGRLHHWL HRLQEAPKKE SAGCLEASVT FNLFRLLTRD LKYVADGNLC LRTSTHPEST.

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 Human Recombinant

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

Product # :

CYT-269

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Shipped at Room temp

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Description

Interleukin-18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 18.2 kDa. The IL-18 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.

Purity

Greater than 95.0% 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
IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin 18 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL18 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 18 in sterile PBS at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
YFGKLESKLS VIRNLNDQVL FIDQGNRPLF EDMTDSDCRD NAPRTIFIIS MYKDSQPRGM AVTISVKCEK ISTLSCENKI ISFKEMNPPD NIKDTKSDII FFQRSVPGHD NKMQFESSSY EGYFLACEKE RDLFKLILKK EDELGDRSIM FTVQNED
Background
Also known as IFN-gamma inducing factor, Interleukin-18 or IL18 is a protein. In humans this protein is encoded by the IL18 gene. The protein is a proinflammatory cytokine.
Mechanism
The levels of IL-18 in the human body are increased at sites of inflammation. This includes cases of rheumatoid arthritis as well as other similar conditions. Osteoblastic cells express the protein and it is capable of inhibiting osteoclast formation. It is able to do this through a variety of mechanisms.
For instance, it is able to stimulate GM-CSF. This is created by T cells and is a response to treatment using IL-18. As well as this, the cytokine does stimulate INF-y production through vivo in bone. Furthermore, the impact on bone resorption and osteoclastogenesis is increased when used in conjunction with IL-12 treatment. Studies have shown that IL-18 provides an indirect stimulus on osteoclastogenesis due to the effect it has on T lymphocytes.
Furthermore, evidence has shown that IL-18 does increase the production of OPG. This was studied in research on transgenic mice that overexpressed IL-18. In these cases osteoclasts decreased as did bone mass. This suggested that IL-18 also has an impact on bone growth.

Interactions
Research has also explored the different interactions of IL-18 on other proteins. This includes the interaction between IL-18 and IL-18R. This has been shown to decrease the power of protective immunity and increase pathogenic responses during an infection involving intracellular bacteria. This interaction suggests that the presence or absence of IL-18R signal does impact the pathogenic compared to protective immunity.
Another interaction between interleukin 19 and Astrocyte has shown that it can improve neuropathic pain processing following nerve injury. It is proposed this is due to the fact that the nociceptive signals in the spinal cord are augmented due to this reaction.

Function
Belonging to the IL-1 superfamily, this cytokine is produced by macrophages as well as various other cells. It operates after binding with the interleukin-18 receptor. Working with IL-12, the protein is then able to induce-cell mediated immunity after an infection from lipopolysaccharide and other microbial products.
Once stimulated by IL-18 other cells including natural killer and T cells then release IFN-y. This type II IFN plays a crucial part in activating the macrophages of various other cells.
Together IL12 and IL-18 are able to successfully inhibit IgE and IG1 production that is dependent on IL-4. As well as this, the protein is also able to increase IgG2a production through B cells. IL-18 will interact specifically with this type of cytokine and has a negative impact on regulation of biological activity.

Structure
Many researchers have suggested that the structure of IL-18 is a key way to understand it’s receptor activation mechanism. The structure of IL-18 closely resembles of IL-1 and has various similarities. It is folded into a beta-trefoil structure and three sites have been shown to be important for receptor activation. These were revealed through extensive mutagenesis. Two of the sites provide binding sites for the IL-18 receptor and are located in positions similar to IL-1. The third structure seems to be used for IL-18 receptor beta binding.

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.

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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.

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