Search: 1000 results found for "procalcitonin"

Description:

Interleukin-1 alpha Human Recombinant, HEK

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-964

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Description

Interleukin-1 alpha Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight of 18kDa due to glycosylation.The IL1A is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The IL-1A protein was lyophilized from a 0.2µm filtered solution of PBS pH 7.4 with 10% trehalose as protectant.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

Assay # 1: The biological activity was measured by its binding ability in a functional ELISA, the ED50 is typically 0.5-5 µg/ml. Assay # 2: The biological activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells, the ED50 is typically less than 1pg/ml, corresponding to a specific activity of >1x10⁹ unit/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-1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL1A in deionized water to a stock solution of 0.5mg/ml.
Background
What is the molecular weight/Mw of IL1A HUMAN, HEK Protein?
IL1A HUMAN, HEK Protein has a total Mw of 18kDa.

What is the source or expression system of IL1A HUMAN, HEK Protein?
HEK.
What is the Purity of IL1A HUMAN, HEK Protein?
IL1A HUMAN, HEK Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A HUMAN, HEK Protein?
Assay # 1: The biological activity was measured by its binding ability in a functional ELISA, the ED50 is typically 0.5-5 µg/ml. Assay # 2: The biological activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells, the ED50 is typically less than 1pg/ml, corresponding to a specific activity of >1x109 unit/mg.

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

What is the endotoxin level for IL1A HUMAN, HEK Protein?
The endotoxin level is minimal, IL1A HUMAN, HEK 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:

HCC-1 Human Recombinant (CCL14) (66 a.a.)

Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

Product # :

CHM-006

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Description

HCC-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 66 amino acids and having a molecular mass of 7.8kDa. The HCC-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CCL14 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.

Purity

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

Biological Activity

The Biological activity is determined by its ability to chemoattract human monocytes using a concentration range of 5.0-20.0 ng/ml.

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Introduction
Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.
Synonyms
Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized HCC1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL14 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 HCC-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPYHPSECCF TYTTYKIPRQ RIMDYYETNS QCSKPGIVFI TKRGHSVCTN PSDKWVQDYI KDMKEN.
Background
What is the molecular weight/Mw of CCL14 HUMAN (66 A.A.) Protein?
CCL14 HUMAN (66 A.A.) Protein has a total Mw of 7.8kDa.

What is the source or expression system of CCL14 HUMAN (66 A.A.) Protein?
Escherichia Coli.

What is the Purity of CCL14 HUMAN (66 A.A.) Protein?
CCL14 HUMAN (66 A.A.) Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL14 HUMAN (66 A.A.) Protein?
The Biological activity is determined by its ability to chemoattract human monocytes using a concentration range of 5.0-20.0 ng/ml.

What is the amino acid sequence of CCL14 HUMAN (66 A.A.) Protein?
GPYHPSECCF TYTTYKIPRQ RIMDYYETNS QCSKPGIVFI TKRGHSVCTN PSDKWVQDYI KDMKEN.

What applications can CCL14 HUMAN (66 A.A.) Protein be used in?
CCL14 HUMAN (66 A.A.) Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL14 HUMAN (66 A.A.) Protein?
The endotoxin level is minimal, CCL14 HUMAN (66 A.A.) Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL14 HUMAN (66 A.A.) that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL14 HUMAN (66 A.A.)?
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:

Adiponectin Human Recombinant, His tag

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

Product # :

CYT-433

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Description

The Acrp30 Human is created as a recombinant protein with N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is 26.4 kDa protein containing 230 amino acid residues of the Acrp30 Human and 12 additional amino acid residues - HisTag (underlined).

Source

Escherichia Coli.

Formulation

Acrp30 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.02M Tris buffer pH7.5, 0.15M NaCl.

Purity

Acrp30 Human purity is greater than 95% as determined by SDS-PAGE.

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Introduction
Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
MRGSHHHHHHGSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN.
Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26.4kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
MRGSHHHHHHGSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN.

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

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

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

Description:

Tachykinin-1 Human Recombinant

Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 1.

Product # :

PRO-1338

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Description

TAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (20-129 a.a) and having a molecular mass of 15.6kDa.TAC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TAC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 2M Urea.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Tachykinin-1 (TAC1) belongs to the tachykinin peptide hormone family. TAC1 are a family of peptides which have similar biologic activities and share a common C-terminal sequence, phe-X-gly-leu-met-NH2, however they have distinct N-terminal sequences that convey receptor specificities. TAC1 is assumed to act as neurotransmitters which interact with nerve receptors and smooth muscle cells. TAC1 induces behavioral responses and serves as vasodilators and secretagogues.
Synonyms
Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 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
MGSSHHHHHH SSGLVPRGSH MGSHMEEIGA NDDLNYWSDW YDSDQIKEEL PEPFEHLLQR IARRPKPQQF FGLMGKRDAD SSIEKQVALL KALYGHGQIS HKRHKTDSFV GLMGKRALNS VAYERSAMQN YERRR.

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:

Platelet Factor-4 Mouse Recombinant (CXCL4)

CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

Product # :

CHM-245

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Description

CXCL4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 8.2kDa.

Source

Escherichia Coli.

Formulation

The Mouse CXCL4 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 1.5M NaCl.

Purity

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

Biological Activity

Determined by its ability to chemoattract human neutrophils using a concentration range of 10-100ng/ml.

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Introduction
Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets. Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily.
Synonyms
CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized CXCL4 Mouse Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CXCL4 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 CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VTSAGPEESD GDLSCVCVKT ISSGIHLKHI TSLEVIKAGR HCAVPQLIAT LKNGRKICLD RQAPLYKKVI KKILES.
Background
What is the molecular weight/Mw of PLATELET FACTOR 4 MOUSE Protein?
PLATELET FACTOR 4 MOUSE Protein has a total Mw of 8.2kDa.

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

What is the Purity of PLATELET FACTOR 4 MOUSE Protein?
PLATELET FACTOR 4 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of PLATELET FACTOR 4 MOUSE Protein?
Determined by its ability to chemoattract human neutrophils using a concentration range of 10-100ng/ml.

What is the amino acid sequence of PLATELET FACTOR 4 MOUSE Protein?
VTSAGPEESD GDLSCVCVKT ISSGIHLKHI TSLEVIKAGR HCAVPQLIAT LKNGRKICLD RQAPLYKKVI KKILES.

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

What is the endotoxin level for PLATELET FACTOR 4 MOUSE Protein?
The endotoxin level is minimal, PLATELET FACTOR 4 MOUSE 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:

Leukocyte Cell Derived Chemotaxin 1 Human Recombinant

BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

Product # :

PRO-1846

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Description

LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 144 amino acids (214-334) and having a molecular mass of 16.3kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Leukocyte Cell Derived Chemotaxin 1, also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.
Synonyms
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV.

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:

Platelet Endothelial Cell Adhesion Molecule 1 MouseRecombinant

Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 1.

Product # :

CYT-1211

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Description

PECAM1 Mouse Recombinant produced in HEK293 is a single, non-glycosylated polypeptide chain containing 579 amino acids (18-590 a.a.) and having a molecular mass of 65.3 kDa. PECAM1 Mouse is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

PECAM1 Mouse protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Platelet endothelial cell adhesion molecule (PECAM1) induces susceptibility to atherosclerosis. PECAM1 averts phagocyte ingestion of closely apposed viable cells by transmitting detachment signals, and transforms function upon apoptosis, thus promoting tethering of dying cells to phagocytes. The encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces as a result causing the viable cell's active repulsion from the phagocyte.
Synonyms
Platelet endothelial cell adhesion molecule, PECAM1, CD31, CD31/EndoCAM, endoCAM, GPIIA', PECA1, PECAM-1, Platelet Endothelial Cell Adhesion Molecule 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
EENSFTINSI HMESLPSWEV MNGQQLTLEC LVDISTTSKS RSQHRVLFYK DDAMVYNVTS REHTESYVIP QARVFHSGKY KCTVMLNNKE KTTIEYEVKV HGVSKPKVTL DKKEVTEGGV VTVNCSLQEE KPPIFFKIEK LEVGTKFVKR RIDKTSNENF VLMEFPIEAQ DHVLVFRCQA GILSGFKLQE SEPIRSEYVT VQESFSTPKF EIKPPGMIIE GDQLHIRCIV QVTHLVQEFT EIIIQKDKAI VATSKQSSEA VYSVMAMVEY SGHYTCKVES NRISKASSIM VNITELFPKP KLEFSSSRLD QGELLDLSCS VSGTPVANFT IQKEETVLSQ YQNFSKIAEE SDSGEYSCTA GIGKVVKRSG LVPIQVCEML SKPSIFHDAK SEIIKGHAIG ISCQSENGTA PITYHLMKAK SDFQTLEVTS NDPATFTDKP TRDMEYQCRA DNCHSHPAVF SEILRVRVIA PVDEVVISIL SSNEVQSGSE MVLRCSVKEG TSPITFQFYK EKEDRPFHQA VVNDTQAFWH NKQASKKQEG QYYCTASNRA SSMRTSPRSS TLAVRVFLAP WKK HHHHH

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

Description:

Interleukin-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:

Monocyte Chemotactic Protein-1/MCAF (CCL2) Human Recombinant, HEK

CCL2, C-C motif chemokine 2, GDCF-2, HSMCR30, JE, HC11, MCAF, MCP-1, MCP1, Scya2, Sigje, SMC-CF, Immediate-early serum-responsive protein JE, Monocyte chemoattractant protein 1, Small-inducible cytokine A2.

Product # :

CHM-048

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

MCP1 Human HEK Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 82 amino acids (24-99a.a) and having a molecular mass of 9.5 kDa.MCP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The MCP1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured its ability to chemoattract using THP-1 human acute monocytic leukemia cells. The ED50 range ≤ 30 ng/ml.

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Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B).CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection.This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans.The cell surface receptors that bind CCL2 are CCR2 and CCR5
Synonyms
CCL2, C-C motif chemokine 2, GDCF-2, HSMCR30, JE, HC11, MCAF, MCP-1, MCP1, Scya2, Sigje, SMC-CF, Immediate-early serum-responsive protein JE, Monocyte chemoattractant protein 1, Small-inducible cytokine A2.
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
QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKTHHHH HH
Background
What is the molecular weight/Mw of CCL2 HUMAN, HEK Protein?
CCL2 HUMAN, HEK Protein has a total Mw of 9.5kDa.

What is the source or expression system of CCL2 HUMAN, HEK Protein?
HEK293 Cells.

What is the Purity of CCL2 HUMAN, HEK Protein?
CCL2 HUMAN, HEK Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 HUMAN, HEK Protein?
Measured its ability to chemoattract using THP-1 human acute monocytic leukemia cells. The ED50 range ≤ 30 ng/ml.

What is the amino acid sequence of CCL2 HUMAN, HEK Protein?
QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKTHHHH HH

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

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

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

Where can I order bulk mg quantities of CCL2 HUMAN, HEK?
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, HEK

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

Product # :

CYT-1192

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
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Description

IL19 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 25-177) containing 164 amino acids and having a molecular mass of 19.1 kDa.IL19 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

IL19 protein (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
IL19 is a cytokine that belongs to the IL10 cytokine subfamily. IL-19 is found to be preferentially expressed in monocytes. IL19 binds 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 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
DGSHMLRRCL ISTDMHHIEE SFQEIKRAIQ AKDTFPNVTI LSTLETLQII KPLDVCCVTK NLLAFYVDRV FKDHQEPNPK ILRKISSIAN SFLYMQKTLR QCQEQRQCHC RQEATNATRV IHDNYDQLEV HAAAIKSLGE LDVFLAWINK NHEVMFSAHH HHHH

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:

Follistatin Human Recombinant

FST, FS

Product # :

CYT-232

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
Synonyms
FST, FS
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.
Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.

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

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

What is the Biological Activity of FOLLISTATIN HUMAN Protein?
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.

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

What is the endotoxin level for FOLLISTATIN HUMAN Protein?
The endotoxin level is minimal, FOLLISTATIN 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 beta Human Recombinant, HEK

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

Product # :

CYT-094

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
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Description

Interleukin-1 beta Human Recombinant produced in HEK cells is a glycosylated monomer, having a molecular weight range of 18-25kDa due to glycosylation.The IL-1 beta is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

The IL-1 beta was lyophilized from 1mg/ml in 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells and is typically 0.02-0.08ng/ml.

More Info

Introduction
Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B 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
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-1 beta although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1 beta 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-1b in sterile PBS containing 0.1% endotoxin-free recombinant HSA.
Amino Acid Sequence
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIP
VALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFES
AQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS.
Background
What is the molecular weight/Mw of IL1B HUMAN, HEK Protein?
IL1B HUMAN, HEK Protein has a total Mw of 21.5kDa.

What is the source or expression system of IL1B HUMAN, HEK Protein?
HEK.
What is the Purity of IL1B HUMAN, HEK Protein?
IL1B HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B HUMAN, HEK Protein?
The specific activity was determined by the dose-dependent stimulation of the proliferation of mouse D10S cells and is typically 0.02-0.08ng/ml.

What is the amino acid sequence of IL1B HUMAN, HEK Protein?
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIP
VALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFES
AQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS.

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

What is the endotoxin level for IL1B HUMAN, HEK Protein?
The endotoxin level is minimal, IL1B HUMAN, HEK 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-8 (1-72) (CXCL8) Human Recombinant, GST Tag

Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8

Product # :

CHM-047

Price :

Quantity :

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Shipped with Ice Packs

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Description

Recombinant Human Interleukin-8 produced in E. coli containing 72 amino acids.Recombinant Human Interleukin-8 is fused to GST tag at its N-terminus and purified by proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

IL8 GST solution contains 25mM Tris-Base/ 25mM K2CO3.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

More Info

Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8
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.
Applications
Immunoassay.
Background
What is the source or expression system of CXCL8 HUMAN, GST Protein?
Escherichia Coli.

What is the Purity of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL8 HUMAN, GST Protein?
The biological functionality of CXCL8 HUMAN, GST Protein will be determined in the future.

What is the amino acid sequence of CXCL8 HUMAN, GST Protein?
CXCL8 HUMAN, GST Protein is composed from 72 amino acids.

What applications can CXCL8 HUMAN, GST Protein be used in?
CXCL8 HUMAN, GST Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL8 HUMAN, GST Protein?
The endotoxin level is minimal, CXCL8 HUMAN, GST Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL8 HUMAN, GST 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 CXCL8 HUMAN, GST?
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:

Growth Arrest and DNA-Damage-Inducible Gamma Interacting Protein 1 Human Recombinant

Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

Product # :

PRO-972

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

GADD45GIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (48-222) and having a molecular mass of 22.6 kDa.GADD45GIP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GADD45GIP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2M NaCl and 40% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.
Synonyms
Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.
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 MPRWQLGPRY AAKQFARYGA ASGVVPGSLW PSPEQLRELE AEEREWYPSL ATMQESLRVK QLAEEQKRRE REQHIAECMA KMPQMIVNWQ QQQRENWEKA QADKERRARL QAEAQELLGY QVDPRSARFQ ELLQDLEKKE RKRLKEEKQK RKKEARAAAL AAAVAQDPAA SGAPSS

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:

Recombinant Flagellin Listeria Monocytogenes

Product # :

PRO-2772

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Quantity :

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Shipped with Ice Packs

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Description

Flagellin Listeria Monocytogenes Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of approximately 31.2kDa. The Flagellin FLA is fused to a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Flagellin Listeria Monocytogenes 1mg/ml solution contains 10mM PBS (pH-7.2).

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Listeria monocytogenes is a pathogenic bacteria that manufactures flagella.At 37 °C inside humans, it causes MogR to repress the expression of flagellar proteins, thus stopping the manufacturing of flagella. Though, in the low-temperatures externally of the host, the GmaR inactivates MogR, enabling flagellar formation.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Lyophilized Flagellin FLA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flagellin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

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

Description:

Cardiac Troponin-C Human

Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.

Product # :

PRO-2571

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Description

Troponin-C Human produced from Human Cardiac Tissue, having a molecular mass of 18kDa. The Troponin-C is purified using a combination of ion-exchange and affinity chromatography steps.

Source

Human cardiac tissue

Formulation

The protein solution contains 150 mM NaCl, 10 mM sodium phosphate and 0.05% NaN3, (pH 7.0).

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Troponin is a fundamental regulatory protein of striated muscle contraction, and together with tropomyosin, is positioned on the actin filament. Troponin has 3 subunits: TnI- the inhibitor of actomyosin ATPase; TnT- contains the binding site for tropomyosin; and TnC- the protein encoded by the TNNC1 gene. The binding of calcium to TnC stops the inhibitory action of TnI, consequently allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in the TNNC1 gene are linked to cardiomyopathy dilated type 1Z.
Synonyms
Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
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.

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:

Peroxisome Proliferator Activated Receptor Gamma Human Recombinant, (1-477 a.a)

Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.

Product # :

PKA-334

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Description

PPARG Human Recombinant encoding amino acids 1-477 expressed in E.coli, is fused to a GST tag and it is antibody reactive.The PPARG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PPARG at 0.1mg/ml in 50mM Tris-HCl and 10mM L-glutathione (reduced).

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Introduction
Peroxisome proliferators are non-genotoxic carcinogens which are purported to exert their effect on cells through their interaction with members of the nuclear hormone receptor family termed peroxisome proliferators activated receptors (PPARs). Nuclear hormone receptors are ligand-dependent intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate ligand. Studies indicate that PPARs are activated by peroxisome proliferators such as clofibric acid, nafenopin, and WY-14,643, as well as by some fatty acids.
Synonyms
Peroxisome proliferator-activated receptor gamma, PPAR-gamma, PPARG, NR1C3, PPARG1, PPARG2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Avoid multiple freeze-thaw cycles.
Applications
ELISA.
Inhibition Assays.
Western Blotting.

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 2 Human Recombinant

IL1R2, CD121b, CDw121b, IL-1R-2, IL-1RT-2, IL-1RT2, IL1R2c, IL1RB, IL-1 type II receptor, Interleukin-1 receptor beta, CD121 antigen-like family member B.

Product # :

CYT-1056

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL1R2 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 338 amino acids (14-343a.a.) and having a molecular mass of 38.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL1R2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

IL1R2 protein solution (0.5mg/ml) contains PBS (pH7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is ≤ to 400 ng/ml with IL-1beta.

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Introduction
IL1R2 is a cytokine receptor which is a part of the interleukin-1 receptor family. IL1R2 is expressed mainly by T cells, endothelial cells and fibroblasts. IL1R2 binds IL1A, IL1B and IL1RN preventing them from binding to their regular receptors and thus inhibiting the transduction of their signaling. Also, Interleukin-4 antagonizes the activity of interleukin-1 by inducing the expression and release of this protein.
Synonyms
IL1R2, CD121b, CDw121b, IL-1R-2, IL-1RT-2, IL-1RT2, IL1R2c, IL1RB, IL-1 type II receptor, Interleukin-1 receptor beta, CD121 antigen-like family member B.
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
FTLQPAAHTG AARSCRFRGR HYKREFRLEG EPVALRCPQV PYWLWASVSP RINLTWHKND SARTVPGEEE TRMWAQDGAL WLLPALQEDS GTYVCTTRNA SYCDKMSIEL RVFENTDAFL PFISYPQILT LSTSGVLVCP DLSEFTRDKT DVKIQWYKDS LLLDKDNEKF LSVRGTTHLL
VHDVALEDAG YYRCVLTFAH EGQQYNITRS IELRIKKKKE ETIPVIISPL KTISASLGSR LTIPCKVFLG TGTPLTTMLW WTANDTHIES AYPGGRVTEG PRQEYSENNE NYIEVPLIFD PVTREDLHMD FKCVVHNTLS FQTLRTTVKE LEHHHHHH.
Background
What is the molecular weight/Mw of IL1R2 HUMAN Protein?
IL1R2 HUMAN Protein has a total Mw of 38.8kDa.

What is the source or expression system of IL1R2 HUMAN Protein?
Sf9, Insect cells.

What is the Purity of IL1R2 HUMAN Protein?
IL1R2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1R2 HUMAN Protein?
Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is ≤ to 400 ng/ml with IL-1beta.

What is the amino acid sequence of IL1R2 HUMAN Protein?
FTLQPAAHTG AARSCRFRGR HYKREFRLEG EPVALRCPQV PYWLWASVSP RINLTWHKND SARTVPGEEE TRMWAQDGAL WLLPALQEDS GTYVCTTRNA SYCDKMSIEL RVFENTDAFL PFISYPQILT LSTSGVLVCP DLSEFTRDKT DVKIQWYKDS LLLDKDNEKF LSVRGTTHLL
VHDVALEDAG YYRCVLTFAH EGQQYNITRS IELRIKKKKE ETIPVIISPL KTISASLGSR LTIPCKVFLG TGTPLTTMLW WTANDTHIES AYPGGRVTEG PRQEYSENNE NYIEVPLIFD PVTREDLHMD FKCVVHNTLS FQTLRTTVKE LEHHHHHH.

What applications can IL1R2 HUMAN Protein be used in?
IL1R2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1R2 HUMAN Protein?
The endotoxin level is minimal, IL1R2 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL1R2 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 IL1R2 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-8 (1-77 a.a) Human Recombinant (CXCL8)

IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

Product # :

CHM-327

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Quantity :

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Description

Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8904 Dalton. The IL-8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.

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Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.
Background
What is the molecular weight/Mw of CXCL8 HUMAN (1-77) Protein?
CXCL8 HUMAN (1-77) Protein has a total Mw of 8.9kDa.

What is the source or expression system of CXCL8 HUMAN (1-77) Protein?
Escherichia Coli.

What is the Purity of CXCL8 HUMAN (1-77) Protein?
CXCL8 HUMAN (1-77) Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL8 HUMAN (1-77) Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.

What is the amino acid sequence of CXCL8 HUMAN (1-77) Protein?
AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.

What applications can CXCL8 HUMAN (1-77) Protein be used in?
CXCL8 HUMAN (1-77) Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL8 HUMAN (1-77) Protein?
The endotoxin level is minimal, CXCL8 HUMAN (1-77) Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL8 HUMAN (1-77) 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 CXCL8 HUMAN (1-77)?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-13 109 a.a. Rat Recombinant

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

Product # :

CYT-182

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Shipped at Room temp

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

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

More Info

Introduction
IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.
Synonyms
NC300, ALRH, BHR1, P600, IL-13.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VRRSTSPPVA LRELIEELSN ITQDQKTSLC NSSIVWSVDI TAGGFCAALE SLTNISSCNA IHRTQRILNG LCNQKASDVA SSPPDTKIEV AQFISKLLNY SKQLFRYGH.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-13 as a Reference Standard.

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

Description:

Interleukin-10 Human Recombinant

B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

Product # :

CYT-500

Price :

Quantity :

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Description

Interleukin-10 Human Recombinant produced in E.coli is a single non-glycosylated polypeptide chains containing 161 amino acids each and having a molecular mass of 18.6kDa.The IL-10 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent co-stimulation (with murine IL-4) of MC/9 cells was found to be less than 2.0ng/ml, corresponding to a specific activity of 5.0×10⁵ IU/mg.

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Introduction
Recombinant IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL10 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-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.
Background
What is the molecular weight/Mw of IL10 HUMAN Protein?
IL10 HUMAN Protein has a total Mw of 18.6kDa.

What is the source or expression system of IL10 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL10 HUMAN Protein?
IL10 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10 HUMAN Protein?
The ED50 as determined by the dose-dependent co-stimulation (with murine IL-4) of MC/9 cells was found to be less than 2.0ng/ml, corresponding to a specific activity of 5.0×105 IU/mg.

What is the amino acid sequence of IL10 HUMAN Protein?
MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.

What applications can IL10 HUMAN Protein be used in?
IL10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10 HUMAN Protein?
The endotoxin level is minimal, IL10 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10 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 IL10 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-36 Alpha Mouse Recombinant

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

Product # :

CYT-162

Price :

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Shipped at Room temp

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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-10 Human Recombinant, His

B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

Product # :

CYT-486

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Description

Interleukin-10 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 181 amino acids fragment (19-178) and having a total molecular mass of 20.94kDa with a 20 amino acids N-Terminal His tag. The IL-10 His-Tag protein is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Interleukin-10 His is supplied in 20mM Tris-HCl pH-8 and 20% glycerol.

Purity

Greater than 95.0% by SDS-PAGE.

More Info

Introduction
Interleukin-10 is a multifunctional cytokine produced by a variety of cell types including T helper cells activated B cells and activated macrophages. Interleukin-10 regulates immune-mediated inflammation and modulates the function of cells such as lymphocytes, monocytes, natural killer cells and dendritic cells.
Synonyms
B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.
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
MGSSHHHHHH SSGLVPRGSH MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.
Background
What is the molecular weight/Mw of IL10 HUMAN, HIS Protein?
IL10 HUMAN, HIS Protein has a total Mw of 20.94kDa.

What is the source or expression system of IL10 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of IL10 HUMAN, HIS Protein?
IL10 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL10 HUMAN, HIS Protein?
The biological functionality of IL10 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of IL10 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLK ESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N.

What applications can IL10 HUMAN, HIS Protein be used in?
IL10 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL10 HUMAN, HIS Protein?
The endotoxin level is minimal, IL10 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL10 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 IL10 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-1 beta Human Recombinant

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

Product # :

CYT-208

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Shipping Method :

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Description

Interleukin-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton.The IL-1 Beta is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL-1 Beta was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Phosphate buffer pH=7.1 and 150mM NaCl.

Purity

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

Biological Activity

The specific activity as determined in the test of augmentation of lymphocyte proliferation assay using mouse thymus was found to be 200,000,000 IU/mg.

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Introduction
Interleukin-1b is produced by activated macrophages, IL-1 Beta stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.
Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1 Beta 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-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Val-Arg-Ser.
Background
What is the molecular weight/Mw of IL1B HUMAN Protein?
IL1B HUMAN Protein has a total Mw of 17kDa.

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

What is the Purity of IL1B HUMAN Protein?
IL1B HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B HUMAN Protein?
The specific activity as determined in the test of augmentation of lymphocyte proliferation assay using mouse thymus was found to be 200,000,000 IU/mg.

What is the amino acid sequence of IL1B HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Val-Arg-Ser.

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

What is the endotoxin level for IL1B HUMAN Protein?
The endotoxin level is minimal, IL1B HUMAN Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.631 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-1 beta Recombinant 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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