Search: 1000 results found for "Interleukin 8 (CXCL8)"

Description:

Interleukin-1 alpha Mouse Recombinant, Sf9

Il1a, Il-1a, 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-1062

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Description

IL1AMouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 165 amino acids (115-270a.a.) and having a molecular mass of 19.0kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). IL1A is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL1A protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined in a cell proliferation assay using D10.G4.1 mouse helper T cells is < 0.15 ng/ml.

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Introduction
The cytokine IL-1 alpha or hematopoietin 1 is a member to the interleukin 1 family, encoded by the IL1A gene in humans. Essentially Il-1 is in charge of inflammation and the rising of fever and sepsis. In order to disturb the mentioned processes and treatment for diseases, inhibitors for Interleukin 1 alpha are being developed. Neutrophils and macrophages are the main activators of IL-1 alpha, as well as endothelial and epithelial cells. By binding to the il1 receptor it is a major part in the immune response regulation. In the activation process of tumor necrosis factor-alpha the IL1A has a part as well, and has physiological, metabolic and hematopoietic activities.
Synonyms
Il1a, Il-1a, 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 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
ADPSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQISH HHHHH.
Background
What is the molecular weight/Mw of IL1A MOUSE, SF9 Protein?
IL1A MOUSE, SF9 Protein has a total Mw of 19kDa.

What is the source or expression system of IL1A MOUSE, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL1A MOUSE, SF9 Protein?
IL1A MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A MOUSE, SF9 Protein?
The ED50 as determined in a cell proliferation assay using D10.G4.1 mouse helper T cells is < 0.15 ng/ml.

What is the amino acid sequence of IL1A MOUSE, SF9 Protein?
ADPSAPYTYQ SDLRYKLMKL VRQKFVMNDS LNQTIYQDVD KHYLSTTWLN DLQQEVKFDM YAYSSGGDDS KYPVTLKISD SQLFVSAQGE DQPVLLKELP ETPKLITGSE TDLIFFWKSI NSKNYFTSAA YPELFIATKE QSRVHLARGL PSMTDFQISH HHHHH.

What applications can IL1A MOUSE, SF9 Protein be used in?
IL1A MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A MOUSE, SF9 Protein?
The endotoxin level is minimal, IL1A MOUSE, SF9 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 Protein-4 Human Recombinant (CCL18)

Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.

Product # :

CHM-322

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Description

Macrophage Inflammatory Protein-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7813 Dalton. The MIP-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MIP-4 protein is lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.

Purity

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

Biological Activity

The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

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Introduction
Chemokine (C-C motif) ligand 18 (CCL18 / MIP-4) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). MIP-4 is approximately 60% identical in amino acid sequence to CCL3. MIP-4 is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.
Synonyms
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIP-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized MIP-4 in sterile 18M-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 of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.
Background
What is the molecular weight/Mw of CCL18 HUMAN Protein?
CCL18 HUMAN Protein has a total Mw of 7.8kDa.

What is the source or expression system of CCL18 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL18 HUMAN Protein?
CCL18 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL18 HUMAN Protein?
The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of CCL18 HUMAN Protein?
The sequence of the first five N-terminal amino acids of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.

What applications can CCL18 HUMAN Protein be used in?
CCL18 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL18 HUMAN Protein?
The endotoxin level is minimal, CCL18 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL18 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 CCL18 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:

LD78-beta (CCL3L1) Human Recombinant

C-C motif chemokine 3-like 1, G0/G1 switch regulatory protein 19-2, LD78-beta(1-70), PAT 464.2, Small-inducible cytokine A3-like 1, Tonsillar lymphocyte LD78 beta protein, CCL3L1, D17S1718, G0S19-2, SCYA3L1, LD78, 464.2, SCYA3L, LD78BETA, MGC12815.

Product # :

CHM-263

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Shipped at Room temp

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Description

CCL3L1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.7kDa. The CCL3L1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The biological activity was determined by its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 ng/ml.

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Introduction
CCL3L1 is a small cytokine that belongs to the CC chemokines. The CCL3L1 gene is one of several cytokine genes clustered on the q-arm of chromosome 17. CCL3L1 is involved in immunoregulatory and inflammatory processes. CCL3L1 binds to several chemokine receptors including CCBP2 and CCR5. CCR5 is a co-receptor for HIV, and binding of the CCL3L1 protein to CCR5 inhibits HIV entry.
Synonyms
C-C motif chemokine 3-like 1, G0/G1 switch regulatory protein 19-2, LD78-beta(1-70), PAT 464.2, Small-inducible cytokine A3-like 1, Tonsillar lymphocyte LD78 beta protein, CCL3L1, D17S1718, G0S19-2, SCYA3L1, LD78, 464.2, SCYA3L, LD78BETA, MGC12815.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CCL3L1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3L1 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 CCL3L1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPSV IFLTKRGRQV CADPSEEWVQ KYVSDLELSA.
Background
What is the molecular weight/Mw of CCL3L1 HUMAN Protein?
CCL3L1 HUMAN Protein has a total Mw of 7.7kDa.

What is the source or expression system of CCL3L1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL3L1 HUMAN Protein?
CCL3L1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL3L1 HUMAN Protein?
The biological activity was determined by its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 ng/ml.

What is the amino acid sequence of CCL3L1 HUMAN Protein?
APLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPSV IFLTKRGRQV CADPSEEWVQ KYVSDLELSA.

What applications can CCL3L1 HUMAN Protein be used in?
CCL3L1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL3L1 HUMAN Protein?
The endotoxin level is minimal, CCL3L1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL3L1 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 CCL3L1 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:

CD8, Mouse Anti-Human, Biotin

CD8, MAL, p32.

Product # :

ANT-134

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
CD8 is a cell surface glycoprotein found on most cytotoxic T lymphocytes that mediates efficient cell-cell interactions within the immune system. CD8 acts as a co-receptor, and the T-cell receptor on the T lymphocyte recognize antigen displayed by an antigen presenting cell (APC) in the context of class I MHC molecules. The functional CD8 is either a homodimer composed of two alpha chains, or a heterodimer composed of one alpha and one beta chain. Both alpha and beta chains share significant homology to immunoglobulin variable light chains.
CD8 identifies cytotoxic/suppressor t-cells that interact with MHC class I bearing targets. CD8 is thought to play a role in the process of t-cell mediated killing. CD8 alpha chains binds to class-I MHC molecules alpha-3 domains.
Synonyms
CD8, MAL, p32.
Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Purified human PBL CD8+ T cells.
Ig Subclass
Mouse IgG2a.
Clone
hCD8.
Applications
Staining antibody, weakly cytotoxic. For staining, use 10µl/1,000,000 cells. Titer for cytotoxicity should be determined by the investigator.
Available Conjugates
This antibody is also available conjugated to FITC.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
Lyophilized: store at 4C. After reconstitution, if not intended for use within a month, aliquot and store at -20C.
Purification Method
Ion exchange column.

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

Description:

Interleukin-3 Human Recombinant, Sf9

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

Product # :

CYT-417

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Description

Interleukin-3 Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15000 Dalton. The IL-3 CSF is fused to a C-terminal His-tag (6x His) and purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 0.5X PBS pH-7.4.

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 the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Pro-Thr.
Background
What is the molecular weight/Mw of IL3 HUMAN, SF9 Protein?
IL3 HUMAN, SF9 Protein has a total Mw of 15kDa.

What is the source or expression system of IL3 HUMAN, SF9 Protein?
Insect Cells.
What is the Purity of IL3 HUMAN, SF9 Protein?
IL3 HUMAN, SF9 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL3 HUMAN, SF9 Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of IL3 HUMAN, SF9 Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Pro-Thr.

What applications can IL3 HUMAN, SF9 Protein be used in?
IL3 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL3 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL3 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL3 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 IL3 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-12 Human Recombinant, Sf9

23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

Product # :

CYT-1111

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Shipped at Room temp

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Description

Interleukin 12 Human Recombinant is a glycosylated heterodimer containing 503 amino acids (306 amino acid rHuIL-12 p40 and the 197 amino acid rHuIL-12 p35 subunits) and having a molecular mass of 60kDa. IL12 is purified by proprietary chromatographic techniques.

Source

Baculovirus.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

Purity

Greater than 97.0% as determined by analysis by SDS-PAGE.

Biological Activity

Determined by cell proliferation assay using PHA-stimulated human T lymphoblasts. The ED50 for this effect is 0.01-0.05 ng/mL corresponding to a specific activity of 11,000 units/μg.

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Introduction
interleukin 12 subunit beta/alpha or IL12b/IL12a is a growth factor cytokine which increases the lytic activity of NK/lymphokine-activated killer cells, activated T and NK cells and prompt IFN-gamma production (through resting PBMC). IL12b/IL12a is an essential part to the process of cellular-immunity and activates the differentiation of Th1 cells originates from the precursor T helper cells. The protein is linked to IL23A and creates the IL-23 interleukin, by that, the autoimmune inflammation is induced and autoimmune inflammatory diseases and tumorigenesis are being affected.
Synonyms
23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin 12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond:
>IL-12 ARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS.
>IL-12B
IWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC RKNASISVRA QDRYYSSSWS EWASVPCS.
Background
What is the molecular weight/Mw of IL12 HUMAN, SF9 Protein?
IL12 HUMAN, SF9 Protein has a total Mw of 60kDa.

What is the source or expression system of IL12 HUMAN, SF9 Protein?
Baculovirus.

What is the Purity of IL12 HUMAN, SF9 Protein?
IL12 HUMAN, SF9 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL12 HUMAN, SF9 Protein?
Determined by cell proliferation assay using PHA-stimulated human T lymphoblasts. The ED50 for this effect is 0.01-0.05 ng/mL corresponding to a specific activity of 11,000 units/μg.

What is the amino acid sequence of IL12 HUMAN, SF9 Protein?
IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond:
>IL-12 ARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS.
>IL-12B
IWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC RKNASISVRA QDRYYSSSWS EWASVPCS.

What applications can IL12 HUMAN, SF9 Protein be used in?
IL12 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL12 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL12 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL12 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 IL12 HUMAN, SF9?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin 13 Receptor, Alpha 2 Human Recombinant

CD213A2, CT19, IL-13R, IL13BP, IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, CD_antigen=CD213a2, Interleukin-13-binding protein.

Product # :

CYT-757

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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SDS-PAGE
Citations

Description

IL13RA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (27-343 a.a.) and having a molecular mass of 39.5kDa.IL13RA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL13RA2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Interleukin 13 Receptor, Alpha 2 (IL13RA2) is a member of the type I cytokine receptor family, Type 5 subfamily. IL13RA2 is related to l13RA1, a subunit of the interleukin 13 receptor complex. IL13RA2 binds IL13 with high affinity, though lacking the cytoplasmic domain, and does not appear to function as a signal mediator. IL13RA2 plays a role in the internalization of IL13.
Synonyms
CD213A2, CT19, IL-13R, IL13BP, IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, CD_antigen=CD213a2, Interleukin-13-binding protein.
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 MGSDTEIKVN PPQDFEIVDP GYLGYLYLQW QPPLSLDHFK ECTVEYELKY RNIGSETWKT IITKNLHYKD GFDLNKGIEA KIHTLLPWQC TNGSEVQSSW AETTYWISPQ GIPETKVQDM DCVYYNWQYL LCSWKPGIGV LLDTNYNLFY WYEGLDHALQ CVDYIKADGQ NIGCRFPYLE ASDYKDFYIC VNGSSENKPI RSSYFTFQLQ NIVKPLPPVY LTFTRESSCE IKLKWSIPLG PIPARCFDYE IEIREDDTTL VTATVENETY TLKTTNETRQ LCFVVRSKVN IYCSDDGIWS EWSDKQCWEG EDLSKKTLLR.
Background
What is the molecular weight/Mw of IL13RA2 HUMAN Protein?
IL13RA2 HUMAN Protein has a total Mw of 39.5kDa.

What is the source or expression system of IL13RA2 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL13RA2 HUMAN Protein?
IL13RA2 HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13RA2 HUMAN Protein?
The biological functionality of IL13RA2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL13RA2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSDTEIKVN PPQDFEIVDP GYLGYLYLQW QPPLSLDHFK ECTVEYELKY RNIGSETWKT IITKNLHYKD GFDLNKGIEA KIHTLLPWQC TNGSEVQSSW AETTYWISPQ GIPETKVQDM DCVYYNWQYL LCSWKPGIGV LLDTNYNLFY WYEGLDHALQ CVDYIKADGQ NIGCRFPYLE ASDYKDFYIC VNGSSENKPI RSSYFTFQLQ NIVKPLPPVY LTFTRESSCE IKLKWSIPLG PIPARCFDYE IEIREDDTTL VTATVENETY TLKTTNETRQ LCFVVRSKVN IYCSDDGIWS EWSDKQCWEG EDLSKKTLLR.

What applications can IL13RA2 HUMAN Protein be used in?
IL13RA2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13RA2 HUMAN Protein?
The endotoxin level is minimal, IL13RA2 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13RA2 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 IL13RA2 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:

Matrix Metalloproteinase-8 Human Recombinant, His Tag

CLG1, HNC, MMP-8, PMNL-CL, Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase.

Product # :

ENZ-766

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Description

MMP 8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (101-467a.a) and having a molecular mass of 44.3kDa. MMP 8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MMP 8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form.
Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collagens, acting preferentially on collagen type I.
Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes.
Synonyms
CLG1, HNC, MMP-8, PMNL-CL, Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase.
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 MGSLTPGNPK WERTNLTYRI RNYTPQLSEA EVERAIKDAF ELWSVASPLI FTRISQGEAD INIAFYQRDH GDNSPFDGPN GILAHAFQPG QGIGGDAHFD AEETWTNTSA NYNLFLVAAH EFGHSLGLAH SSDPGALMYP NYAFRETSNY SLPQDDIDGI QAIYGLSSNP IQPTGPSTPK PCDPSLTFDA ITTLRGEILF FKDRYFWRRH PQLQRVEMNF ISLFWPSLPT GIQAAYEDFD RDLIFLFKGN QYWALSGYDI LQGYPKDISN YGFPSSVQAI DAAVFYRSKT YFFVNDQFWR YDNQRQFMEP GYPKSISGAF PGIESKVDAV FQQEHFFHVF SGPRYYAFDL IAQRVTRVAR GNKWLNCRYG.

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

Description:

Interleukin-17 Mouse Recombinant

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

Product # :

CYT-378

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-17 Murine Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 268 (2x134 a.a.) amino acids and having a molecular mass of 30 kDa. The IL-17 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED50 as determined by the dose-dependant induction of IL-6 production in cultured mouse NIH 3T3 fibroblasts was found to be 0.4 ng/ml, corresponding to a specific activity of 2,500,000 units/mg.

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Introduction
IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.
Synonyms
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin 17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAAIIPQSSA CPNTEAKDFL QNVKVNLKVF NSLGAKVSSR RPSDYLNRST SPWTLHRNED PDRYPSVIWE AQCRHQRCVN AEGKLDHHMN SVLIQQEILV LKREPESCPF TFRVEKMLVG VGCTCVASIV RQAA.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.942 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).2. Analysis by RP-HPLC, using a standard solution of IL-17 as a Reference Standard.

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

Description:

Interleukin 9 Human Recombinant, Sf9, Active

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

Product # :

CYT-1143

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Citations

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

More Info

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:

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 :

Shipping Method :

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:

Stromal Cell-Derived Factor-1 gamma Human Recombinant (CXCL12)

Stromal cell-derived factor 1, SDF-1, hSDF-1, C-X-C motif chemokine 12, Intercrine reduced in hepatomas, IRH, hIRH, Pre-B cell growth-stimulating factor, PBSF, CXCL12, SDF1, hSDF-1gamma, SDF-1g, TLSF, TPAR1, SCYB12.

Product # :

CHM-020

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

SDF-1 gamma Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 99 amino acids and having a molecular mass of 11.6kDa.The SDF-1g is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SDF-1g protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/ml.

More Info

Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1a/CXCL12a and SDF-1b/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
Stromal cell-derived factor 1, SDF-1, hSDF-1, C-X-C motif chemokine 12, Intercrine reduced in hepatomas, IRH, hIRH, Pre-B cell growth-stimulating factor, PBSF, CXCL12, SDF1, hSDF-1gamma, SDF-1g, TLSF, TPAR1, SCYB12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SDF-1 gamma 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 SDF-1g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN.
Background
What is the molecular weight/Mw of CXCL12 HUMAN GAMMA Protein?
CXCL12 HUMAN GAMMA Protein has a total Mw of 11.6kDa.

What is the source or expression system of CXCL12 HUMAN GAMMA Protein?
Escherichia Coli.

What is the Purity of CXCL12 HUMAN GAMMA Protein?
CXCL12 HUMAN GAMMA Protein is > 96% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 HUMAN GAMMA Protein?
The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/ml.

What is the amino acid sequence of CXCL12 HUMAN GAMMA Protein?
GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN.

What applications can CXCL12 HUMAN GAMMA Protein be used in?
CXCL12 HUMAN GAMMA Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL12 HUMAN GAMMA Protein?
The endotoxin level is minimal, CXCL12 HUMAN GAMMA Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL12 HUMAN GAMMA 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 CXCL12 HUMAN GAMMA?
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-17E Rat Recombinant

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

Product # :

CYT-576

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Interleukin-17E Rat Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing 145 amino acids and having a molecular mass of 35.5 kDa. The IL-25 Rat 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.

More Info

Introduction
IL-25 also called IL-17E cytokine has a sequence similarity with IL17.
IL-17E indluces NF-kappaB activation, and stimulates the production of IL-8. IL17E and IL17B are ligands for the cytokine receptor IL17BR. IL-25 is a proinflammatory cytokine favoring Th2-type immune response. The upregulation of costimulation-induced IL-17E receptors and release of cytokines and chemokines from IL-17E treated costimulated Th cells are differentially regulated by intracellular JNK, p38 MAPK and NF-kappaB activity. Blocking Iinterleukin-25 prevents airway hyperresponsiveness, a critical feature of clinical asthma. IL25 produced by innate effector eosinophils and basophils increase the allergic inflammation by enhancing the maintenance and functions of TSLP-DC activated adaptive Th2 memory cells. Over expression of IL-25 up-regulates gene expression of Th2 cytokines and induces growth retardation, jaundice, and multiorgan inflammation in a transgenic mouse model. IL-25 contributes to the induction and maintenance of eosinophilic inflammation by acting on lung fibroblasts which supports the fact that IL-17E is an important factor in asthma pathophysiology. IL-17E operates by amplifying TH2 cell-mediated allergic airway inflammation but doesn’t induce allergic inflammation in vivo.
Synonyms
IL-25, IL-17E, IL17E, IL25, Interleukin-25.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin Rat IL17E although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat IL-25 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin Rat IL25 in sterile 10mM HCL not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CSHLPRCCPS KQQEFPEEWL KWNPAPVSPP EPLRHTHHPE SCRASKDGPL NSRAISPWSY ELDRDLNRVP QDLYHARCLC PHCVSLQTGS HMDPMGNSVP LYHNQTVFYR RPCHGEQGAH GRYCLERRLY RVSLACVCVR PRMMA.

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:

Galectin-8 Mouse Recombinant

Galectin-8, Gal-8, LGALS-8, AI326142, D13Ertd524e, 1200015E08Rik.

Product # :

CYT-185

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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SDS-PAGE
Citations

Description

LGALS8 mouse Recombinant produced E. coli is a single polypeptide chain containing 339 amino acids (1-316) and having a molecular mass of 38kDa.LGALS8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LGALS8 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ for this effect is ≤ 2ug/ml. Measured by its ability to agglutinate human red blood cells.

SDS-PAGE

More Info

Introduction
LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.
Synonyms
Galectin-8, Gal-8, LGALS-8, AI326142, D13Ertd524e, 1200015E08Rik.
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 MGSMLSLNNL QNIIYNPIIP YVGTITEQLK PGSLIVIRGH VPKDSERFQV DFQLGNSLKP RADVAFHFNP RFKRSSCIVC NTLTQEKWGW EEITYDMPFR KEKSFEIVFM VLKNKFQVAV NGRHVLLYAH RISPEQIDTV GIYGKVNIHS IGFRFSSDLQ
SMETSALGLT QINRENIQKP GKLQLSLPFE ARLNASMGPG RTVVIKGEVN TNARSFNVDL VAGKTRDIAL HLNPRLNVKA FVRNSFLQDA WGEEERNITC FPFSSGMYFE MIIYCDVREF KVAINGVHSL EYKHRFKDLS SIDTLSVDGD IRLLDVRSW.
Background
What is the molecular weight/Mw of LGALS8 MOUSE Protein?
LGALS8 MOUSE Protein has a total Mw of 38kDa.

What is the source or expression system of LGALS8 MOUSE Protein?
Escherichia Coli.

What is the Purity of LGALS8 MOUSE Protein?
LGALS8 MOUSE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS8 MOUSE Protein?
The biological functionality of LGALS8 MOUSE Protein will be determined in the future.

What is the amino acid sequence of LGALS8 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMLSLNNL QNIIYNPIIP YVGTITEQLK PGSLIVIRGH VPKDSERFQV DFQLGNSLKP RADVAFHFNP RFKRSSCIVC NTLTQEKWGW EEITYDMPFR KEKSFEIVFM VLKNKFQVAV NGRHVLLYAH RISPEQIDTV GIYGKVNIHS IGFRFSSDLQ
SMETSALGLT QINRENIQKP GKLQLSLPFE ARLNASMGPG RTVVIKGEVN TNARSFNVDL VAGKTRDIAL HLNPRLNVKA FVRNSFLQDA WGEEERNITC FPFSSGMYFE MIIYCDVREF KVAINGVHSL EYKHRFKDLS SIDTLSVDGD IRLLDVRSW.

What applications can LGALS8 MOUSE Protein be used in?
LGALS8 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS8 MOUSE Protein?
The endotoxin level is minimal, LGALS8 MOUSE Protein was purified using conventional chromatography techniques.
Assay Conditions
1. Mix equal volumes of human blood and Alsever’s solution (pH 7.0). (Alsever’s solution: NaCl 0.42g, Sodium citric acid 0.8g, Citric acid 0.055g, D-glucose 2.05g in DW100 ml).2. Centrifuge at 15000rpm for 10 minutes and wash 4 times with PBS.3. Dilute packed cells in a 0.5mg/ml trypsin-EDTA solution to give 4% red cell suspension.4. Incubate for 1 hour at 37°C and wash 4 times with PBS.5. Dilute packed cells in PBS to give a 4% red cell suspension.6. Load 50µl of 0.5%BSA-in-0.15M-NaCl solution and 25µl of 4%-Red-Cell-in-PBS in U shaped wells.7. Add 25µl of serial diluted galectin protein in PBS to each well plate (Round bottom 96 well plate).8. Incubate for 30 minutes at room temperature to observe visible agglutination.

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

Description:

Interleukin-17E Human Recombinant

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

Product # :

CYT-583

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Citations

Description

Interleukin-17E Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2x145 amino acids (with an N-terminal Methionine for each chain total aa for each chain 146) and having a total predicted molecular mass of 33.7kDa. The IL-25 Human 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 SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent production of IL-8 by Human PBMCs is 26-40ng/ml, corresponding to a specific activity of 3.8x10⁴ units/mg.

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

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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source
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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:

Eotaxin-2 Human Recombinant (CCL24)

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 # :

CHM-238

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source
formulation
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Description

CCL24 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8.8 kDa. The CCL24 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.

Purity

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

Biological Activity

The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

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Introduction
Eotaxin-2, also called MPIF2 & Ckb6, 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.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Human Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
DPKQEWV QRYMKNLDAKQKKASPRARAVA.
Background
What is the molecular weight/Mw of CCL24 HUMAN Protein?
CCL24 HUMAN Protein has a total Mw of 8.8kDa.

What is the source or expression system of CCL24 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL24 HUMAN Protein?
CCL24 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL24 HUMAN Protein?
The activity is determined by the chemoattract of human PBE (peripheral blood eosinophils) at a concentration between 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

What is the amino acid sequence of CCL24 HUMAN Protein?
VVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKGGVIFTTKKGQQFCG
DPKQEWV QRYMKNLDAKQKKASPRARAVA.

What applications can CCL24 HUMAN Protein be used in?
CCL24 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL24 HUMAN Protein?
The endotoxin level is minimal, CCL24 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL24 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 CCL24 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:

LEC/NCC-4 Human Recombinant

C-C motif chemokine 16, Small-inducible cytokine A16, IL-10-inducible chemokine, Chemokine LEC, Monotactin-1, Chemokine CC-4, Lymphocyte and monocyte chemoattractant, CCL-16, HCC-4, HCC4, NCC4, NCC-4, Liver Expressed Chemokine, LMC, LCC-1, LCC1, MTN-1, MTN1, SCYL4, ckB12, SCYA16, LEC, ILINCK, MGC117051.

Product # :

CHM-237

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Description

CCL16 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 97 amino acids and having a molecular mass of 11.2 kDa. The CCL16 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CCL16 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.

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 total human monocytes using a concentration range of 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

More Info

Introduction
Human CCL16, also called HCC-4, liver-expressed chemokine (LEC), and lymphocyte and monocyte chemoattractant (LMC), is a novel CC chemokine recognized by bioinformatics. NCC-4 cDNA encodes a 120 amino acids along with a 23 amino acids signal peptide that is cleaved to generate 97 amino acid protein. HCC4 is vaguely related to other CC chemokines, showing less than 30% sequence identity. Among CC chemokines, CCL-16 has the largest similarity to HCC-1. 2 potential polyadenylation signals are present on the human HCC-4 gene, and as a result, 2 transcripts containing roughly 1,500 base pairs and 500 base pairs have been detected. HCC-4 is expressed weakly by some lymphocytes, including NK cells, T cells, and some T cell clones. The expression of HCC-4 in monocytes is greatly upregulated in the presence of IL-10.
CCL16 shows chemotactic activity for lymphocytes and monocytes rather than to neutrophils. NCC-4 has potent myelosuppressive activity, suppresses proliferation of myeloid progenitor cells. CCL16 demonstrates chemotactic activity for monocytes and thp-1 monocytes, rather than for resting lymphocytes and neutrophils. HCC-4 induces a calcium flux in thp-1 cells that desensitized prior to the expression of rantes.
Synonyms
C-C motif chemokine 16, Small-inducible cytokine A16, IL-10-inducible chemokine, Chemokine LEC, Monotactin-1, Chemokine CC-4, Lymphocyte and monocyte chemoattractant, CCL-16, HCC-4, HCC4, NCC4, NCC-4, Liver Expressed Chemokine, LMC, LCC-1, LCC1, MTN-1, MTN1, SCYL4, ckB12, SCYA16, LEC, ILINCK, MGC117051.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL16 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 CCL16in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.
Background
What is the molecular weight/Mw of CCL16 HUMAN Protein?
CCL16 HUMAN Protein has a total Mw of 11.2kDa.

What is the source or expression system of CCL16 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL16 HUMAN Protein?
CCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL16 HUMAN Protein?
Determined by its ability to chemoattract total human monocytes using a concentration range of 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CCL16 HUMAN Protein?
QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.

What applications can CCL16 HUMAN Protein be used in?
CCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL16 HUMAN Protein?
The endotoxin level is minimal, CCL16 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL16 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 CCL16 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 Human Recombinant (CCL2)

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

Product # :

CHM-271

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Description

Monocyte Chemotactic Protein-1 Human Recombinant also known as Monocyte Chemotactic and Activating Factor (MCAF) produced in E.Coli is a non-glycosylated, Polypeptide chain containing 76 amino acids and having a molecular mass of 8.6kDa. The MCP-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CCL2 was lyophilized from a concentrated (1mg/ml) sterile solution without any additives.

Purity

Greater than 98.0% as determined by RP-HPLC and SDS-PAGE.

Biological Activity

The specific activity as determined by the ability of MCP-1 to chemoattract human THP-1 cells is detectable starting at 1ng/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
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCP-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL2 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 Monocyte Chemotactic Protein-1in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT.
Background
What is the molecular weight/Mw of CCL2 HUMAN Protein?
CCL2 HUMAN Protein has a total Mw of 8.6kDa.

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

What is the Purity of CCL2 HUMAN Protein?
CCL2 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 HUMAN Protein?
The specific activity as determined by the ability of MCP-1 to chemoattract human THP-1 cells is detectable starting at 1ng/ml.

What is the amino acid sequence of CCL2 HUMAN Protein?
QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT.

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

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

Who supplies recombinant CCL2 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 CCL2 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-5 Mouse Recombinant (CCL12)

C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.

Product # :

CHM-266

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Description

MCP-5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 82 amino acids and having a molecular mass of 9.3kDa. The MCP5 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 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.

More Info

Introduction
MCP-5 (CCL12) is a cloned mouse CC chemokine most closely related to human MCP1 (66% amino acid sequence identity in the mature protein). MCP5 is expressed constitutively in the thymus and the lymph nodes. Under inflammatory conditions, moreover CCL12 expression is induced in activated macrophages and mast cells. The mouse MCP1 gene is mapped to the CC chemokine cluster on chromosome 11. Recombinant CCL12 is a potent chemoattractant for monocytes and lymphocytes but not neutrophils. At high concentrations, MCP-5 also chemoattracts eosinophils. CCL12 is a functional ligand for CCR2.
Synonyms
C-C motif chemokine 12, MCP-1-related chemokine, Monocyte chemoattractant protein 5, Monocyte chemotactic protein 5, MCP-5, Small-inducible cytokine A12, Ccl12, Mcp5, Scya12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CCL12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCP5 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 MCP5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.
Background
What is the molecular weight/Mw of CCL12 MOUSE Protein?
CCL12 MOUSE Protein has a total Mw of 9.3kDa.

What is the source or expression system of CCL12 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL12 MOUSE Protein?
CCL12 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL12 MOUSE Protein?
Determined by its ability to chemoattract human peripheral blood monocytes using a concentration range of 10.0-50.0 ng/ml.

What is the amino acid sequence of CCL12 MOUSE Protein?
GPDAVSTPVT CCYNVVKQKI HVRKLKSYRR ITSSQCPREA VIFRTILDKE ICADPKEKWV KNSINHLDKT SQTFILEPSC LG.

What applications can CCL12 MOUSE Protein be used in?
CCL12 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL12 MOUSE Protein?
The endotoxin level is minimal, CCL12 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL12 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL12 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Bone Morphogenetic protein-8b, Mouse Anti Human

Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.

Product # :

ANT-558

Price :

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Shipping Method :

Shipped with Ice Packs

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formulation
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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Bone Morphogenetic protein-8b (BMP8B) belongs to a family of secreted signaling molecules which can induce ectopic bone growth. BMP8B is known for having a possible bone inductive activity as it is related to BMP5 and BMP7. BMP8B is the osteoinductive factor accountable for epithelial osteogenesis.
Synonyms
Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human BMP8B mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human BMP8B protein 264-402 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
Clone
PAT13E6AT.
Applications
BMP8B antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
BMP8B antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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 Rhesus Macaque Recombinant

Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Lymphocyte stimulatory factor 1, IL4.

Product # :

CYT-172

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Description

IL-4 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 14.9kDa.The IL4 Rhesus Macaque is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent stimulation of TF1 cells is less than 0.2ng/ml, corresponding to a specific activity of >5.0×10⁶ IU/mg.

More Info

Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
Synonyms
Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Lymphocyte stimulatory factor 1, IL4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleikin-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HNCHIALREI IETLNSLTEQ KTLCTKLTIT DILAASKNTT EKETFCRAAT VLRQFYSHHE KDTRCLGATA QQFHRHKQLI RFLKRLDRNL WGLAGLNSCP VKEANQSTLE DFLERLKTIM REKYSKCSS.
Background
What is the molecular weight/Mw of IL 4 RHESUS MACAQUE Protein?
IL 4 RHESUS MACAQUE Protein has a total Mw of 14.9kDa.

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

What is the Purity of IL 4 RHESUS MACAQUE Protein?
IL 4 RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 4 RHESUS MACAQUE Protein?
The ED50 as determined by the dose-dependent stimulation of TF1 cells is less than 0.2ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.

What is the amino acid sequence of IL 4 RHESUS MACAQUE Protein?
HNCHIALREI IETLNSLTEQ KTLCTKLTIT DILAASKNTT EKETFCRAAT VLRQFYSHHE KDTRCLGATA QQFHRHKQLI RFLKRLDRNL WGLAGLNSCP VKEANQSTLE DFLERLKTIM REKYSKCSS.

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

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

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

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

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

Description:

Coagulation Factor-VIII Human

Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.

Product # :

PRO-317

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
biological activity
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Description

Human Factor VIII produced from Human Plasma contains 2332 amino acids and having a molecular mass of 330kDa. Factor-VIII is effective in the correction and prevention of severe bleeding episodes attributed to Factor VIII deficiency. The Factor-VIII is purified by proprietary chromatographic techniques.

Source

Human Plasma.

Formulation

The lyophilized protein 200IU/ml was lyophilized from a sterile solution containing 1.5% Glycine, 160mM Calcium chloride and 25mM NaCitrate and 25mM NaCl.

Biological Activity

The potency was found to be 10 Units/mg.

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Introduction
Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.
Synonyms
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Factor-VIII although stable at room temperature for 1 week, should be stored desiccated between 2-8°C. Upon reconstitution Factor-VIII should be stored at 4°C.
Solubility
It is recommended to reconstitute the lyophilized Factor-VIII in sterile 18MΩ-cm H2O at a concentration of 200IU/ml, which can then be further diluted to other aqueous solutions.
Make sure that the vial has reached room temperature prior to its reconstitution, otherwise it might precipitate.
Human Virus Test
The plasma is collected from donors with Hepatitis B vaccinated. Each unit of plasma has been tested for HBsAg, Anti-HIV-1/2 plus O and Anti-HCV by using the imported kits which are approved by Federal Drug Administration (FDA).

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-5 Mouse Recombinant

EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor II, IL-5, BCGF-II, Cytotoxic T-lymphocyte inducer, Il5.

Product # :

CYT-689

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
biological activity
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Citations

Description

Interleukin-5 Mouse Recombinant produced in E.Coli is a dimeric, non-glycosylated polypeptide chain containing 2 x 113 amino acids forming a disulfide linked homodimer and having a molecular mass of 26.2 kDa.The Mouse IL-5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 20mM Sodium Phosphate and 50mM NaCl pH-7.5.

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 the proliferation of TF-1 cells was found to be 1.7ng/ml, corresponding to a specific activity of 588,235.3IU/mg.

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Introduction
The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
Synonyms
EDF, BCDFII, TRF, T-cell replacing factor, Eosinophil differentiation factor, B cell differentiation factor II, IL-5, BCGF-II, Cytotoxic T-lymphocyte inducer, Il5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Mouse Interleukin-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse IL5 should be stored at 4°C between 2-7 days and for future use below -18°C.Please avoid freeze thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Mouse Interleikin-5 in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEG.
Background
What is the molecular weight/Mw of IL 5 MOUSE Protein?
IL 5 MOUSE Protein has a total Mw of 26.2kDa.

What is the source or expression system of IL 5 MOUSE Protein?
Escherichia Coli.

What is the Purity of IL 5 MOUSE Protein?
IL 5 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 5 MOUSE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of TF-1 cells was found to be 1.7ng/ml, corresponding to a specific activity of 588,235.3IU/mg.

What is the amino acid sequence of IL 5 MOUSE Protein?
MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEG.

What applications can IL 5 MOUSE Protein be used in?
IL 5 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 5 MOUSE Protein?
The endotoxin level is minimal, IL 5 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 5 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 5 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

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