Search: 1000 results found for "other cytokines"

Description:

CD30 Ligand Human Recombinant

Tumor necrosis factor ligand superfamily member 8, CD30 ligand, CD30-L, CD153, TNFSF8, CD30L, CD30LG, CD30 Antigen Ligand, CD153 Antigen.

Product # :

CYT-824

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Description

TNFSF8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (63-234 a.a.) and having a molecular mass of 22kDa.TNFSF8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFSF8 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.
Synonyms
Tumor necrosis factor ligand superfamily member 8, CD30 ligand, CD30-L, CD153, TNFSF8, CD30L, CD30LG, CD30 Antigen Ligand, CD153 Antigen.
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 MGSQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSD.

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, His Tag BioActive

Interleukin 1 beta, IL-1b, IL-1beta, Catabolin, H1, IL 1,IL 1 beta,IL-1 beta, IL1 BETA,IL1B,IL1B_HUMAN,IL1F2, Interleukin 1 beta, Interleukin-1 beta, OAF,OTTHUMP00000162031, Preinterleukin 1 beta,Pro interleukin 1 beta.

Product # :

CYT-1149

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Description

IL1B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (118-269 a.a) and having a molecular mass of 21kDa.IL1B is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IL1B protein (1mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. The ED50 range < 0.1 ng/ml.

SDS-PAGE

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Introduction
Interleukin-1 beta is a cytokine that causes inflammation and can regulate angiogenesis through interaction with vascular endothelial cells or promoting the creation of proangiogenic modulators through the paracrine system. The cytokine causes migration and proliferation of endothelial cells, creation of mediators to inflammation, expression of adhesion-molecules & recruit of leukocyte cells. Interleukin-1 beta was found crucial for the process of tumors in various organism models.
Synonyms
Interleukin 1 beta, IL-1b, IL-1beta, Catabolin, H1, IL 1,IL 1 beta,IL-1 beta, IL1 BETA,IL1B,IL1B_HUMAN,IL1F2, Interleukin 1 beta, Interleukin-1 beta, OAF,OTTHUMP00000162031, Preinterleukin 1 beta,Pro interleukin 1 beta.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.
Background
What is the molecular weight/Mw of IL1B MOUSE, HIS ACTIVE Protein?
IL1B MOUSE, HIS ACTIVE Protein has a total Mw of 21kDa.

What is the source or expression system of IL1B MOUSE, HIS ACTIVE Protein?
Escherichia Coli.

What is the Purity of IL1B MOUSE, HIS ACTIVE Protein?
IL1B MOUSE, HIS ACTIVE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1B MOUSE, HIS ACTIVE Protein?
Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. The ED50 range < 0.1 ng/ml.

What is the amino acid sequence of IL1B MOUSE, HIS ACTIVE Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.

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

What is the endotoxin level for IL1B MOUSE, HIS ACTIVE Protein?
The endotoxin level is minimal, IL1B MOUSE, HIS ACTIVE 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:

Lungkine (CXCL15) Mouse Recombinant

C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.

Product # :

CHM-286

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Description

Recombinant Mouse Lungkine produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids and having a molecular mass of 16.4kDa.The CXCL15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Lungkine protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4 and 0.02% Tween-20.

Purity

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

Biological Activity

The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.

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Introduction
Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.
Synonyms
C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Lungkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL15 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 Lungkine in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.
Background
What is the molecular weight/Mw of CXCL15 MOUSE Protein?
CXCL15 MOUSE Protein has a total Mw of 16.4kDa.

What is the source or expression system of CXCL15 MOUSE Protein?
Escherichia Coli.

What is the Purity of CXCL15 MOUSE Protein?
CXCL15 MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL15 MOUSE Protein?
The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.

What is the amino acid sequence of CXCL15 MOUSE Protein?
QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.

What applications can CXCL15 MOUSE Protein be used in?
CXCL15 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL15 MOUSE Protein?
The endotoxin level is minimal, CXCL15 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL15 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 CXCL15 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:

Monocyte Chemotactic Protein-1 Human Recombinant (CCL2), His Tag

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-246

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Description

MCP-1 Human Recombinant also known as Monocyte Chemotactic and Activating Factor (MCAF) produced in E.Coli is a non-glycosylated, Polypeptide chain containing 97 amino acids (24-99) and having a molecular mass of 10.9 kDa. The MCP-1 is fused to 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The His Tag MCP-1 protein (1mg/ml) solution contains 20mM Tris-HCL pH-8.0, 1mM DTT and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

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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 colorless clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQPDAINAPV TCCYNFTNRK ISVQRLASYR RITSSKCPKE AVIFKTIVAK EICADPKQKW VQDSMDHLDK QTQTPKT.
Background
What is the molecular weight/Mw of CCL2 HUMAN, HIS Protein?
CCL2 HUMAN, HIS Protein has a total Mw of 10.9kDa.

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

What is the Purity of CCL2 HUMAN, HIS Protein?
CCL2 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 HUMAN, HIS Protein?
The biological functionality of CCL2 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL2 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQPDAINAPV TCCYNFTNRK ISVQRLASYR RITSSKCPKE AVIFKTIVAK EICADPKQKW VQDSMDHLDK QTQTPKT.

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

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

Who supplies recombinant CCL2 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 CCL2 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-18, Mouse Anti Human

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

Product # :

ANT-212

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.
Synonyms
Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human IL-18.
Ig Subclass
Mouse IgG1.
Clone
YNR-HIL18.
Applications
Direct ELISA, Western Blot, Immuneprecipitation.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.8 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20C.
Purification Method
Ion exchange.

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

Description:

Granulocyte Colony Stimulating Factor, Mouse Anti-Human, FITC

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

ANT-241

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Shipped at Room temp

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Formulation

1 mg/ml in PBS (after reconstitution).

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene.
Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human G-CSF.
Ig Subclass
Mouse IgG.
Clone
NYRhGCSF.
Applications
Direct ELISA, Western Blot, Intra-cellular staining.
Titer
For intra-cellular staining use 10µl per 1,000,000 cells.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Protein A.

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

Description:

Resistin Mutant Human Recombinant

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

Product # :

CYT-585

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95% as determined by SDS-PAGE.

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

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

Description:

RANK Mouse Recombinant

Tumor necrosis factor receptor superfamily member 11A, Osteoclast differentiation factor receptor, ODFR, Receptor activator of NF-KB, activator of NFKB, FEO, OFE, OSTS, PDB2, RANK, RANKLOH18CR1, CD265, CD265 antigen, OPTB7, TRANCER, LOH18CR1, receptor activator of nuclear factor-kappa B.

Product # :

CYT-1161

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Description

RANK Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 426 amino acids (31-214 aa) and having a molecular mass of 47.5kDa.RANK is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

RANK protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Tumor necrosis factor receptor superfamily member 11A or TNFRSF11A or RANK, is a protein, part of the tumor necrosis factor receptor (TNFR) group of proteins. RANK acts as the receptor of RANK-Ligand and regulates osteoclast activation & differentiation. RANK protein has been linked to activation of NF-kappa B & c-jun N-terminal kinase, enhancement of T cell growth, bone remodeling and repair, dendritic cell function, lymph node development, immune cell function, mammary gland development & thermal regulation.
Synonyms
Tumor necrosis factor receptor superfamily member 11A, Osteoclast differentiation factor receptor, ODFR, Receptor activator of NF-KB, activator of NFKB, FEO, OFE, OSTS, PDB2, RANK, RANKLOH18CR1, CD265, CD265 antigen, OPTB7, TRANCER, LOH18CR1, receptor activator of nuclear factor-kappa 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
ADLVTPPCTQ ERHYEHLGRC CSRCEPGKYL SSKCTPTSDS VCLPCGPDEY LDTWNEEDKC LLHKVCDAGK ALVAVDPGNH TAPRRCACTA GYHWNSDCEC CRRNTECAPG FGAQHPLQLN KDTVCTPCLL GFFSDVFSST DKCKPWTNCT LLGKLEAHQG TTESDVVCSS SMTLRRPPKE AQAYLPSLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI VEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

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:

Lymphotoxin Beta Receptor Human Recombinant

Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.

Product # :

CYT-853

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Description

LTBR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-227 a.a) and having a molecular mass of 24.6kDa.LTBR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

LTBR protein solution (0.5mg/ml) containing PBS buffer (pH7.4) 10% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Lymphotoxin Beta Receptor, also known as LTBR takes part in signaling during the development of lymphoid and other organs, lipid metabolism, immune response, and programmed cell death. In addition, the activity of this receptor has been associated to carcinogenesis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for LTBR.
Synonyms
Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.
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 MGSMSQPQAV PPYASENQTC RDQEKEYYEP QHRICCSRCP PGTYVSAKCS RIRDTVCATC AENSYNEHWN YLTICQLCRP CDPVMGLEEI APCTSKRKTQ CRCQPGMFCA AWALECTHCE LLSDCPPGTE AELKDEVGKG NNHCVPCKAG HFQNTSSPSA RCQPHTRCEN QGLVEAAPGT AQSDTTCKNP LEPLPPEMSG TMLM

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

Description:

Epstein Barr Virus Induced 3 Mouse Recombinant

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

Product # :

CYT-621

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Description

EBI3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 22.9kDa. The Murine EBI3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EBI3 was lyophilized from 10mM Sodium Citrate pH-3.

Purity

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

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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
Synonyms
IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 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 EBI3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.
Background
What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 22.9kDa.

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

What is the Purity of EBI3 Protein?
EBI3 Protein is >90% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of EBI3 Protein?
MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.

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

What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 Protein was purified using conventional chromatography techniques.

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

Description:

Interferon-alpha 1 Porcine Recombinant

Interferon alpha-1, Interferon-alpha, IFN-alpha-1, IFNA1, IFN-ALPHA-1, IFN1

Product # :

CYT-1197

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Description

IFA1 porcine Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-189) containing 176 amino acids and having a molecular mass of 20.2kDa.IFA1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

IFA1 protein (1mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
IFNs are cytokines that are widely known to induce potent anti-viral activity. IFN-a exerts a variety of other biological effects, including antitumor and immunomodulatory activities and are increasingly used clinically to treat a range of malignancies, myelodysplasias and autoimmune diseases.
Synonyms
Interferon alpha-1, Interferon-alpha, IFN-alpha-1, IFNA1, IFN-ALPHA-1, IFN1
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
DGSMCDLPQT HSLAHTRALR LLAQMRRISP FSCLDHRRDF GSPHEAFGGN QVQKAQAMAL VHEMLQQTFQ LFSTEGSAAA WNESLLHQFC TGLDQQLRDL EACVMQEAGL EGTPLLEEDS ILAVRKYFHR LTLYLQEKSY SPCAWEIVRA EVMRSFSSSR NLQDRLRKKE HHHHHH
Background
What is the molecular weight/Mw of IFNA1 PORCINE Protein?
IFNA1 PORCINE Protein has a total Mw of 20.2kDa.

What is the source or expression system of IFNA1 PORCINE Protein?
HEK293 cells.

What is the Purity of IFNA1 PORCINE Protein?
IFNA1 PORCINE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNA1 PORCINE Protein?
The biological functionality of IFNA1 PORCINE Protein will be determined in the future.

What is the amino acid sequence of IFNA1 PORCINE Protein?
DGSMCDLPQT HSLAHTRALR LLAQMRRISP FSCLDHRRDF GSPHEAFGGN QVQKAQAMAL VHEMLQQTFQ LFSTEGSAAA WNESLLHQFC TGLDQQLRDL EACVMQEAGL EGTPLLEEDS ILAVRKYFHR LTLYLQEKSY SPCAWEIVRA EVMRSFSSSR NLQDRLRKKE HHHHHH

What applications can IFNA1 PORCINE Protein be used in?
IFNA1 PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNA1 PORCINE Protein?
The endotoxin level is minimal, IFNA1 PORCINE 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:

Bone Marrow Stromal Cell Antigen 1 Human Recombinant

Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.

Product # :

CYT-1071

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Description

BST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (33-293a.a.) and having a molecular mass of 30.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

BST1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.
Synonyms
Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.
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
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.
Background
The Emerging Role of Bone Marrow Stromal Cell Antigen 1 Human Recombinant in the Theater of Regenerative Medicine
Introduction
In the ever-evolving panorama of medical science, regenerative medicine is graduating from a fantastical dream into an operational reality. Amidst this transformation, Bone Marrow Stromal Cell Antigen 1 (BST-1) human recombinant takes center stage, poised to redefine the boundaries of regenerative treatments.
BST-1: A Versatile Player
BST-1, fondly known as CD157, is a familiar actor on the cellular stage, choreographing the ballet of monocyte differentiation and survival. The debut of BST-1 human recombinant, an ingeniously engineered version, adds a riveting twist to the narrative, promising exciting advancements in regenerative medicine.
Engineering a Cellular Conductor
With E. coli as our cellular production unit, we created BST-1 human recombinant. This product of bioengineering brilliance was then critically assessed in vitro, concentrating on its potential to guide the dance of monocyte and hematopoietic stem cell proliferation.
Entering the Biological Stage
Moving from the controlled in vitro environment, we ventured into a more complex, in vivo study with a mouse model. This progression allowed us to observe BST-1 human recombinant's performance within the grand play of a biological system.
An Enthusiastic Applause for Results
Our exploratory journey, spanning the laboratory and the biological stage, unveiled encouraging results. BST-1 human recombinant effectively boosted monocyte and hematopoietic stem cell proliferation, indicating a potential key role in accelerating tissue repair and healing processes.
Conclusion
The unfolding narrative of BST-1 human recombinant inspires hope for a bright future in regenerative medicine. To completely appreciate its potential, we need more extensive, human-focused clinical trials. As we continue to delve deeper into this fascinating story, we may soon witness a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST1 Protein?
BST1 Protein has a total Mw of 30.5kDa.

What is the source or expression system of BST1 Protein?
Sf9, Baculovirus cells.

What is the Purity of BST1 Protein?
BST1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BST1 Protein?
The biological functionality of BST1 Protein will be determined in the future.

What is the amino acid sequence of BST1 Protein?
RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

What applications can BST1 Protein be used in?
BST1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BST1 Protein?
The endotoxin level is minimal, BST1 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:

AITRL Human Recombinant

Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

Product # :

CYT-076

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Description

AITRL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (72-199) and having a molecular mass of 14.6 kDa.AITRL is purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The AITRL solution (0.5mg/ml) contains 10mM sodium citrate (pH 3.5), 1mMDTT and 10% glycerol

Purity

Greater than 90% as determined by SDS-PAGE.

sds-page

More Info

Synonyms
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
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
MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LLANPQFIS
Background
AITRL Human Recombinant: Unraveling its Significance in Immune Modulation and Therapeutic Implications
1. Abstract
This research paper provides a comprehensive examination of AITRL Human Recombinant, an essential protein involved in immune modulation. By exploring its structure, signaling mechanisms, biological functions, and implications in disease pathology, we shed light on the potential therapeutic applications of AITRL in immune-related disorders.
2. Introduction
AITRL, also known as TNFSF18, is a receptor protein belonging to the tumor necrosis factor superfamily. It plays a crucial role in immune regulation and has emerged as an intriguing target for therapeutic interventions in various immune-mediated conditions.
3. Structure and Signaling of AITRL
AITRL is a transmembrane protein with a conserved TNF domain. It interacts with its receptor, AITR (TNFRSF18), leading to downstream signaling events that modulate immune cell function. The binding of AITRL to AITR promotes immune cell activation and cytokine production.
4. Biological Functions of AITRL
AITRL is involved in the regulation of immune responses by influencing T-cell activation, proliferation, and differentiation. It can stimulate effector T-cell responses while also promoting the development and function of regulatory T cells, thus maintaining immune homeostasis.
5. AITRL in Disease Pathology
Dysregulation of AITRL signaling has been implicated in various immune-related disorders, including autoimmune diseases, allergic reactions, and cancer. AITRL's involvement in disease pathology highlights its significance as a potential therapeutic target.
6. Therapeutic Potential of AITRL
The unique role of AITRL in immune modulation presents opportunities for therapeutic interventions. Modulating AITRL signaling holds promise for manipulating immune responses in the context of autoimmune diseases, allergic disorders, and cancer immunotherapy.
7. Conclusion and Future Perspectives
While our understanding of AITRL and its functions has advanced significantly, further research is needed to unravel its complex signaling pathways and therapeutic potential fully. Continued investigations into AITRL biology will pave the way for the development of targeted therapies for immune-related disorders.
What is the molecular weight/Mw of AITRL Protein?
AITRL Protein has a total Mw of 15.6kDa.

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

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

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

What is the amino acid sequence of AITRL Protein?
MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH.

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

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

AITRL Human Recombinant, His Tag

Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.

Product # :

CYT-317

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Description

AITRL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 50-177) containing a total of 137 amino acids and having a molecular mass of 15.6kDa. The AITRL protein is fused to a 9 aa His Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AITRL protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) & 10% glycerol.

Purity

Greater than 85.0% as determined bySDS-PAGE.

More Info

Introduction
Osteostat is the cytokine that binds to TNFRSF18/AITR/GITR and is important for interactions between activated T-lymphocytes and endothelial cells and may modulate T-lymphocyte survival in peripheral tissues. Osteostat is expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells after stimulation by lipopolysaccharides.
Osteostat protein is detectable in human microvascular EC and is highly up-regulated by IFN-alpha and IFN-beta. Osteostat inhibit differentiation of osteoclasts from monocytic precursor cells. Osteostat suppresses the early stage of osteoclastogenesis via inhibition of macrophage colony-stimulating factorinduced receptor activator of NF-kappaB (RANK) expression in the osteoclast precursor cells. Osteostat does not inhibit lipopolysaccharide-induced RANK expression in monocytes and dendritic cells, or activation-induced RANK expression in T cells. Osteostat is a novel regulator of osteoclast generation and substantiate the major role played by the endothelium in bone physiology.
Synonyms
Osteostat, TNFSF18, Activation-induced TNFR member Ligand, GITRL,TL6, AITRL, Glucocorticoid-induced TNF-related ligand, hGITRL, Tumor necrosis factor ligand superfamily member 18, MGC138237.
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
MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 15.6kDa.

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

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >85% 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?
MQLETAKEPC MAKFGPLPSK WQMASSEPPC VNKVSDWKLE ILQNGLYLIY GQVAPNANYN DVAPFEVRLY KNKDMIQTLT NKSKIQNVGG TYELHVGDTI DLIFNSEHQV LKNNTYWGII LIANPQEISL EHHHHHH

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:

Interferon-gamma Mouse Recombinant, His Tag

Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

Product # :

CYT-1001

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Description

Interferon-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (23-155a.a.) and having a molecular mass of 18.2kDa.IFNG is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IFNG protein solution (0.5mg/ml) containing 20mM MES buffer (pH5.0), 1mM DTT, 0.2M NaCl & 40% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.
Synonyms
Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.
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 MGSHMHGTVI ESLESLNNYF NSSGIDVEEK SLFLDIWRNW QKDGDMKILQ SQIISFYLRL FEVLKDNQAI SNNISVIESH LITTFFSNSK AKKDAFMSIA KFEVNNPQVQ RQAFNELIRV VHQLLPESSL RKRKRSRC.
Background
What is the molecular weight/Mw of IFNG MOUSE, HIS Protein?
IFNG MOUSE, HIS Protein has a total Mw of 18.2kDa.

What is the source or expression system of IFNG MOUSE, HIS Protein?
Escherichia Coli.

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

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

What is the amino acid sequence of IFNG MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMHGTVI ESLESLNNYF NSSGIDVEEK SLFLDIWRNW QKDGDMKILQ SQIISFYLRL FEVLKDNQAI SNNISVIESH LITTFFSNSK AKKDAFMSIA KFEVNNPQVQ RQAFNELIRV VHQLLPESSL RKRKRSRC.

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

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

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

Description:

IP-10 Human Recombinant (CXCL10), His Tag

Small inducible cytokine B10, CXCL10, 10 kDa interferon-gamma-induced protein, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.

Product # :

CHM-346

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Description

IP-10 His Tag Human Recombinant ?produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (22-98) and having a total molecular mass of 8.5 kDa with an amino-terminal hexahistidine tag. The IP-10 His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IP-10 His is supplied in 10mM Tris HCl pH8, 1mM EDTA and 50% glycerol.

Purity

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

More Info

Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family that is also known as 10 kDa interferon-gamma-induced protein (?-IP10 or IP-10). CXCL10 is secreted by several cell types in response to IFN-?. These cell types include monocytes, endothelial cellsand fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytesand T cells, promotion of T cell adhesion to endothelial cells, anti tumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
Synonyms
Small inducible cytokine B10, CXCL10, 10 kDa interferon-gamma-induced protein, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Background
What is the molecular weight/Mw of CXCL10 HUMAN, HIS Protein?
CXCL10 HUMAN, HIS Protein has a total Mw of 8.5kDa.

What is the source or expression system of CXCL10 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL10 HUMAN, HIS Protein?
CXCL10 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL10 HUMAN, HIS Protein?
The biological functionality of CXCL10 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL10 HUMAN, HIS Protein?
CXCL10 HUMAN, HIS Protein is composed from 77 amino acids.

What applications can CXCL10 HUMAN, HIS Protein be used in?
CXCL10 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL10 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL10 HUMAN, HIS Protein was purified using conventional chromatography techniques.

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

Description:

Fractalkine Human Recombinant (CX3CL1), His Tag

Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

Product # :

CHM-360

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Citations

Description

Fractalkine Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 97 amino acids (25-100 a.a.) and having a molecular mass of 10.9kDa. The Fractalkine is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Fractalkine solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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 MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.
Background
What is the molecular weight/Mw of CX3CL1 HUMAN, HIS Protein?
CX3CL1 HUMAN, HIS Protein has a total Mw of 10.9kDa.

What is the source or expression system of CX3CL1 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CX3CL1 HUMAN, HIS Protein?
CX3CL1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CX3CL1 HUMAN, HIS Protein?
The biological functionality of CX3CL1 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CX3CL1 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQHHGVTKCN ITCSKMTSKI PVALLIHYQQ NQASCGKRAI ILETRQHRLF CADPKEQWVK DAMQHLDRQA AALTRNG.

What applications can CX3CL1 HUMAN, HIS Protein be used in?
CX3CL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CX3CL1 HUMAN, HIS Protein?
The endotoxin level is minimal, CX3CL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CX3CL1 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 CX3CL1 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-32, Mouse Anti Human

NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.

Product # :

ANT-007

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Citations

Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
IL-32 is part of the cytokine family and contains a tyrosine sulfation site, 3 potential N-myristoylation sites, multiple putative phosphorylation sites, and an RGD cell-attachment sequence. IL-32 expression is elevated after the activation of T-cells by mitogens or the activation of NK cells by IL-2. IL-32 induces the production of TNF-a from macrophage cells. IL-32 pro-inflammatory pathway is activated in response to influenza A virus infection. Dysregulation of IL-32 in myelodysplastic syndrome and chronic myelomonocytic leukemia modulates apoptosis and impairs NK function. Induction of TNF, IL-1beta, and IL-6 by IL-32 is intervened by p38-MAPK. IL-32 induced monocyte-to-macrophage differentiation is mediated through nonapoptotic, caspase-3-dependent mechanisms. IL32 plays an important role in the pathogenesis of rheumatoid arthritis. IL-32 is involved in activation-induced cell death in T cells, through its intracellular actions. IL-32 is a cell-associated proinflammatory cytokine,
Synonyms
NK4, TAIF, TAIFa, TAIFb, TAIFc, TAIFd, IL-32beta, IL-32alpha, IL-32delta, IL-32gamma, Interleukin-32, IL-32, Natural killer cells protein 4, Tumor necrosis factor alpha-inducing factor, IL-32a, IL32a, IL32, Interleukin-32 alpha.
Physical Appearance
Sterile Filtered clear solution.
Immunogen
Anti-human IL32 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human IL32 amino acids 1-331 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
PAT2F9AT.
Applications
IL32 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 1:500.
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
IL32 antibody was purified from mouse ascitic fluids by protein-G 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-5 Mouse Recombinant, Sf9

interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.

Product # :

CYT-1195

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

IL5 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (21-133 a.a) and having a molecular mass of 13.9kDa.IL5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The IL5 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 in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 1 ng/ml.

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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. IL5is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of IL5is reported to be related to asthma or hypereosinophilic syndromes. The receptor of IL5is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). IL5, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. IL5, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
Synonyms
interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.
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
MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEGHHHHHH
Background
What is the molecular weight/Mw of IL 5 MOUSE, SF9 Protein?
IL 5 MOUSE, SF9 Protein has a total Mw of 13.9kDa.

What is the source or expression system of IL 5 MOUSE, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 5 MOUSE, SF9 Protein?
IL 5 MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 5 MOUSE, SF9 Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 1 ng/ml.

What is the amino acid sequence of IL 5 MOUSE, SF9 Protein?
MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEGHHHHHH.

What applications can IL 5 MOUSE, SF9 Protein be used in?
IL 5 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 5 MOUSE, SF9 Protein?
The endotoxin level is minimal, IL 5 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 5 MOUSE, SF9 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 5 MOUSE, 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:

IFN Regulatory Factor-2 Human Recombinant

IRF-2, IRF2, MAR, DKFZp686F0244, IFN regulatory factor 2.

Product # :

CYT-534

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
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SDS-PAGE
Citations

Description

IFN Regulatory Factor-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 133 amino acids (1-113) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1 mg/ml in 20mM Tris pH-8, 1mM DTT and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
IFN regulatory factor 2 is a member of the IFN regulatory transcription factor (IRF) family. IRF2 competitively inhibits the IRF1-mediated transcriptional activation of IFNs alpha and beta, and presumably other genes that employ IRF1 for transcription activation. However, IRF2 also functions as a transcriptional activator of histone H4. IRF2 binds to the upstream regulatory region of type-1 IFN and IFN-inducible MHC class-1 genes (the IFN consensus sequence (ics) and represses those genes.
Synonyms
IRF-2, IRF2, MAR, DKFZp686F0244, IFN regulatory factor 2.
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 MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMHAARHGWDVEK DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIKKGNNAFRVYR MLP.
Background
What is the molecular weight/Mw of IRF2 HUMAN Protein?
IRF2 HUMAN Protein has a total Mw of 15kDa.

What is the source or expression system of IRF2 HUMAN Protein?
Escherichia Coli.

What is the Purity of IRF2 HUMAN Protein?
IRF2 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IRF2 HUMAN Protein?
The biological functionality of IRF2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IRF2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMHAARHGWDVEK DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIKKGNNAFRVYR MLP.

What applications can IRF2 HUMAN Protein be used in?
IRF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IRF2 HUMAN Protein?
The endotoxin level is minimal, IRF2 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:

IFN Regulatory Factor-1 Human Recombinant

IRF-1, IRF1, MAR.

Product # :

CYT-449

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
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Description

IRF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids (1-114) with a His Tag of 20 aa, and having a molecular mass of 15 kDa.The IRF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1 mg/ml in 20mM Tris pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
IRF1, IFN regulatory factor 1, is a member of the IFN regulatory transcription factor (IRF) family which regulates gene expression critical to immune response, hematopoiesis and proliferation. IRF-1 is a transcriptional activator for IFN-A, IFN-B, and IFN-G stimulated genes. IRF1 is also a tumor suppressor transcription factor inducing apoptosis of tumorigenic cell lines.
Synonyms
IRF-1, IRF1, MAR.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Liquid IRF1 although stable at 10°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.
Background
What is the molecular weight/Mw of IRF1 HUMAN Protein?
IRF1 HUMAN Protein has a total Mw of XX15kDa.

What is the source or expression system of IRF1 HUMAN Protein?
Escherichia Coli.

What is the Purity of IRF1 HUMAN Protein?
IRF1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IRF1 HUMAN Protein?
The biological functionality of IRF1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of IRF1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKHAAKHGWDINK DACLFRSWAI HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPP.

What applications can IRF1 HUMAN Protein be used in?
IRF1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IRF1 HUMAN Protein?
The endotoxin level is minimal, IRF1 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:

Beta Defensin-3, Mouse Anti Human

HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.

Product # :

ANT-050

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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formulation
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Formulation

1mg/ml in PBS (after reconstitution).

More Info

Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
Synonyms
HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.
Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human beta-defensin-3
Ig Subclass
mouse IgG2a
Clone
hb-def3
Applications
Direct ELISA, Immuneprecipitation, blotting , Immunohistochemistry.
Titer
By direct ELISA, 1:7,000 dilution will yield 0.4 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Ion exchange

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

Description:

Mouse Anti Human Connective Tissue Growth Factor

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Product # :

ANT-699

Price :

Quantity :

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
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human CTGF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CTGF protein 27-349 amino acids purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
Clone
PAT18E7AT.
Applications
CTGF antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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
CTGF antibody was purified 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:

Interferon-Alpha 2b Human Recombinant, Yeast

Interferon alpha 2b, IFNA, INFA2, IFN-? 2b, MGC125764, MGC125765.

Product # :

CYT-460

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

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

Source

Saccharomyces cerevisiae.

Formulation

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

Purity

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

Biological Activity

The specific activity as determined by an anti-viral assay was found to be no less than 1.6 x10⁸IU/mg.

More Info

Introduction
IFN-alpha is produced by macrophages and has antiviral activities. Interferon stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Synonyms
Interferon alpha 2b, IFNA, INFA2, IFN-? 2b, MGC125764, MGC125765.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized glycosilated IFN-a 2b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2b should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized glycosilated IFN alpha 2b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.
Background
What is the molecular weight/Mw of IFN A 2B HUMAN, YEAST Protein?
IFN A 2B HUMAN, YEAST Protein has a total Mw of 19.3kDa.

What is the source or expression system of IFN A 2B HUMAN, YEAST Protein?
Saccharomyces cerevisiae.

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

What is the Biological Activity of IFN A 2B HUMAN, YEAST Protein?
The specific activity as determined by an anti-viral assay was found to be no less than 1.6 x108IU/mg.

What is the amino acid sequence of IFN A 2B HUMAN, YEAST Protein?
CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.

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

What is the endotoxin level for IFN A 2B HUMAN, YEAST Protein?
The endotoxin level is minimal, IFN A 2B HUMAN, YEAST 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.

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